ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q12X66
|
MSDILRRGRLASVPDEEIINFTSSMNADKWIFKADILVDLAHTIMLKERKIIKAEDCKKILEGLLTIKEEGIEKLDHTYEDIHISLESRLIDMVGEDTGGRMHSGRSRNDEVATCIRLTLRNDLLLLMEELIALRNTLNDTSSENLNTLMPGFTHLQHAQPTTLAHHLTAHANAIGRDLERTMDCYKRVNLSPLGAAAFASTGFDLDRERTCKLLGFDGLIENSMDAVSSRDFLIESASVFANLMINLSKVAEEIVIWSTSEFAFIELDDRYASTSSIMPQKKNPDTAELLRGKSGVTIGSLMSLLAICKALPLSYNRDLQEATPNIMQSLETTRASVRIMNGMIATMSINKENMAGLATAGFTTATELADTMVRVCDIPFRTAHQIVGVLARGSGEPTLGEIDAVAHNVIGESLSSRGLTEKMVKEALDPILNVSKRSVIGGPSPESMERLIESSRERIANNTEILESLIANRDNAIESLFCEVEKCIDV
|
Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 54140
Sequence Length: 491
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Subcellular Location: Cytoplasm
EC: 4.3.2.1
|
A0KGY2
|
MSNDHPQGQLPASPARSALKGYLYVLGSILLVTAAQLGMKWGVIQLPTWQMDLAVMLAHPLPLLVILAGVGCYALSLLCWLAALHSTPLNIAYPLLSTSYALVYLLAVNIPLFAEPLEPGKALGVLFILLGAVLVGIKPAAGTKQTG
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Function: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15454
Sequence Length: 147
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
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A7ZP77
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MGLIWGLFSVIIASVAQLSLGFAASHLPPMTHLWDFIAALLAFGLDARILLLGLLGYLLSVFCWYKTLHKLALSKAYALLSMSYVLVWIASMVLPGWEGTFSLKALLGVACIMSGLMLIFLPTTKQRY
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Function: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14067
Sequence Length: 128
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
|
Q8F6P5
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MIPKKTKLKSREIEVPGDKSLSHRSVLFAALSKGKSKVTGFLEAEDPLNTMSAFAKLGLKVQKVKPGEYEFESPGKNKLVSPNVDLDFGNAGTGIRLSAGLICGLPGINATLTGDNSLKKRPMGRIIKPLSSMGASIVGLGEKETAPLKIEGKKLKGFRYESPIASAQVKSCLMLAAISSETDLEYSENILSRDHTENMFRFLGNKIEQISPLHFKIKPPYVLNGGEFRVPGDISSAAFFLVLGVLAKEGNLLIKNIGLNPARTGILTALQSMGAKIEIQNKRIECGETVGDLKTYPSNLKKSNIPESLIPSIIDEIPILSVAGFFAEGGFEIRHAEELRAKESDRIHTMVSNFRELGIEVEEYTDGYSFDGTSKKSSEVWTRLSTVKKIPIQSYMDHRIAMSFLIFKTLSGLDLQIDETSWIETSFPGFEKLLESCINE
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Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Mass (Da): 48266
Sequence Length: 440
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Subcellular Location: Cytoplasm
EC: 2.5.1.19
|
B1MYD1
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MIRLTPASAHGLHGHVTVPGDKSISHRALMFGAIAKGQTVITNFLASDDVLHTMTVFRNLGVAIQQNENSVRIQGQGFDGLTPPKKPLDMGNSGTSTRLLMGLLSKQNFDMSIIGDESLSQRPMTRVMKPLTEMGAKIDLTANGTLPGIIQANATLRGITYDMPVASAQVKSAILLAGIQAEGETCVIEKIASRDHTERMLRQFGGQLESKNGVITLKKQQQLQGQHVDVPADISSAAFFLVAALITPNSELTINRVGINPTRDGILKILTRMGASIEVTPIDTQGEPLADLTVRTQTLHGIDITAADIPSAVDELPIIALAATQADGDTIISGAEELRVKETDRIATVISELSKLGANIEEKPDGMIIHGGQSLTADNDAVLLDSCGDHRIAMMNAIAALITTGDVILTGEDAMSVSYPGFLEDLSEVML
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Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Mass (Da): 45796
Sequence Length: 431
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Subcellular Location: Cytoplasm
EC: 2.5.1.19
|
P0CZ72
|
MKRMKLRTNAGPLQGTIQVPGDKSISHRAVILGAVAKGETRVKGLLKGEDVLSTIQAFRNLGVRIEEKDDQLVIEGQGFQGLTAPCQTLNMGNSGTSMRLIAGLLAGQPFSVKMIGDESLSKRPMDRIVYPLKQMGVEISGETDRQFPPLQLQGNRNLQPITYTLPISSAQVKSAILLAALQAKGTTQVVEKEITRNHTEEMIQQFGGRLIVDGKRITLVGPQQLTAQEITVPGDISSAAFWLVAGLIIPGSELLLKNVGVNPTRTGILEVVEKMGAQIVYEDMNKKEQVTSIRVVYSRLKGTIISGGLIPRLIDELPIIALLATQAQGTTCIKDAQELRVKETDRIQVVTDTLNSMGANIKATADGMIIKGPTVLYGANTSTYGDHRIGMMTAIAALLVKQGQVHLDKEEAIMTSYPTFFKDLERLCHD
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Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Mass (Da): 46691
Sequence Length: 430
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Subcellular Location: Cytoplasm
EC: 2.5.1.19
|
Q9S400
|
MKLKTNIRHLHGSIRVPGDKSISHRSIIFGSLAEGETKVYDILRGEDVLSTMQVFRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNMGNSGTSIRLISGVLAGADFEVEMFGDDSLSKRPMDRVTLPLKKMGVSISGQTERDLPPLRLKGTKNLRPIHYELPIASAQVKSALMFAALQAKGESVIIEKEYTRNHTEDMLKQFGGHLSVDGKKITVQGPQKLTGQKVVVPGDISSAAFWLVAGLIAPNSRLVLQNVGINETRTGIIDVIRAMGGKLEITEIDPVAKSATLIVESSDLKGTEIGGALIPRLIDELPIIALLATQAQGVTVIKDAEELKVKETDRIQVVADALNSMGADITPTADGMIIKGKSALHGARVNTFGDHRIGMMTAIAALLVADGEVELDRAEAINTSYPSFFDDLESLIHG
|
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Mass (Da): 45766
Sequence Length: 427
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Subcellular Location: Cytoplasm
EC: 2.5.1.19
|
Q9PNT2
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MQVEVKLKENAYKVYIDELEELEFDSKVFILSNPKISGLHLKTLLSKIKAKEIFIATVKDGEEYKNLSTMEEILNQMFNSKLDRKSVLISFGGGVISDMGGFAASIYQRGIDFINIPTTLLACVDAAVGGKTGVNNNFGKNLIGTFYQPKAVYCESFFLKTLSSRELAAGMAEFIKMAAMFDYSILDFIEKIDEKSFLNATCENEIFTQIIAKSIELKSRVVEQDEKESRLRMLLNYGHTFAHVIENFTDYKLYLHGEAVAIGMVMANQLALNLGLLDKMQSQRIKDILLKFGLPISYKINNVDEFYEAFFMDKKSSNKKINFVLASPLGKGLIKGDISKEDIIATLREFQ
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Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 39596
Sequence Length: 351
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q9A434
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MIRTVPVGLGERAYDVVIGPGLLDQAGERVAAVLGKRKRVAVVTDAHVGAHHGERLSAALQGAGITVDLITIAPGEESKSFEGLADLSDRLLALNLERGDQIVALGGGVVGDLAGFAAAIYKRGIDFVQVPTTLLAQVDSSVGGKTAIDTPRGKNLIGAFHQPRLVLADLDVLATLPARELACGYAEIIKYGLLGDFAFFEWLETNVQAVLDRDVDALVRAVGRSVEMKAEIVAEDEKEAGRRALLNLGHTFGHAIEAEMGFGEALKHGEAVGVGMAQAFRFSARLGLCPSQDAVRAQAAIKAAGLPTTLADVRPEPFSADALIAHCGQDKKAQGGKLTFVLARGIGDAFVAKDVDRAALKAFLVEEGAV
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Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 38726
Sequence Length: 370
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q9PK25
|
MIELITDKPHPMHLVDSLCDPQLFATLAKTSPLIFITNSTLEILVLPPLLETARSLGFSVEILIIPEGEQAKTETTFLYLHKQLATLTIPRQATLIGVGGGVVLDIVGFVASTHCRGMPFIAVPTTLVAMIDASIGGKNGINLDHIKNRIGSFYLPKDVWICPSVLSSLPEQEFYHGIAECIKHAYIADASILPILQNPASLRSTKQLSLLIKRNCLCKASIVGKDIRDHGIRQILNFGHTLGHALEMLFTGKISHGFAISVGMVLETKLSLAMGVARNPNILHFLVQDLLRYQLPTSLKDLYAQAQIPIHSCSQILSALSYDKKKQNASLPPFVMIEEIGLAASCNGSFCQPASNHFLTHILKEDLHAMHDH
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 40842
Sequence Length: 373
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q9JY01
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MKTLTVHTPSHSYPIFIGNGLLPQAGSLLKPHLGKRAAIIANETVAPLYLGTLQTALDAAGVSHFSIILPDGEAHKNWQTLNLIFDGLMQNRAERKTTLIALGGGVIGDMVGFAAATYQRGAPFVQIPTTLLSQVDSSVGGKTAINHPLGKNMIGAFYQPQAVLADLDTLHTLPARELSAGMAEVIKYGALGDIGFFEWLEQHMPELMTLDREKLAQAVYRCCQMKADIVAQDETEQGIRAWLNLGHTFGHAIETEMGYGTWLHGEAIAAGCVLAARLSEQLGKTSAADTARLAALLEAAGLPSAPPVFAFEKWLEHMSHDKKVSGGIMRFIGLNRLGEANITEITDTDILRRTLQPYL
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 38745
Sequence Length: 359
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q1QQW6
|
MSAPLKNSDPVTVDVALGDRSYDIVIGRGILPSLGERIAALRPGARVAIVTDEYVATHWLRATEASLLGAGIATSRIVVDEGEVSKSYEGIEFVCEELIKARIERNDLVVALGGGVVGDLAGFAAAIVRRGVDFVQVPTSLLAQVDSSVGGKTGINSPQGKNLVGAFHQPILVVADTAVLDTLSPRQFRAGYAEVAKYGLLGDEAFFAWLETNHADIVKGSAARESAVAASCRAKAAIVARDERETGERALLNLGHTFGHALETATGFSDRLYHGEGVSIGMVLAAELSAQLGMIADADVARIRRHLATAGLPTRLQDIAGFRQEGLADADGLMALMAQDKKVKRGRLTFILLQAIGQAVVSSDVEPSTVRDFLARKLADAPA
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 40346
Sequence Length: 383
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q8EQB7
|
MEEMTVQSNQSSYPIYIGQGLRYQLSSYIEKKYTKLFIITDDQVGSRYLKDVLHGYPSEENICHFTIPSGESSKSIDNFYRLQTEALQNGLDRHSLIIALGGGVVGDLAGLVAATFMRGIDYIQVPTTILAHDSSVGGKVAINHHLGKNLIGSFFPPVAVIYDIETLSTLPPHEIRSGYAEIVKEGLIANQKMFLSLLDHSLASIKPHQLEIYLKAGIQVKSRIVEQDEKEANIRKFLNLGHTLGHALETIHGYGNITHGEAVANGLLFALHVSEYEFEIQLPFYQLYQWLKDNEYPILSFSEEEITQLIELMKTDKKSVGGTIQMVLLKEVEDPVTVSLDNSMMKQHLSTYLERMEKL
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 40347
Sequence Length: 359
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
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B1ZQS6
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MPNTLTVDLGHRSYPIVFAADVRNNVRDQVAELTTAGRKVAVFTDEQVASAQVGALEAMFGSSPRLAFAPGESAKSLASFGRAMDFLAAQKVDRRGVVFAFGGGVIGDLAGFIAASWLRGIDFYQVPTTLLAMVDSSVGGKTGINIPAGKNLVGAFHQPRGVFIGTDFLRTLPAREFAAGMAEVIKYGLLGDAALLELLERAPLSFVSPELAGVIRQCCALKAAFVQADERELAPEGGRALLNLGHTFGHAIEQVTGYGVYLHGEAVAIGMCAAARLSAKLGHLGGADVARVDAVVAAHRLPVKLRTPLVLMDLLAAMARDKKVRAGMPRFVVLRKLGEAVTQDDVPAELAAECFREVGAS
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 37995
Sequence Length: 361
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
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A6LEZ7
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MSEQKVVICKDLKSELQDFLSSLKYDKLFILMDTNTKEKCFPLVEDIPAFQKAPILVMEAGDMNKGFVSLAQIWTALSNEGASRNSLLVNLGGGMITDMGGFAGATFKRGIRTINIPTTLMASVDAAVGGKTGINFNGLKNEVGSFYPPLCVFIDCDFLRTLDRDNILSGYAEMIKHGLISSMENYASVMLFDIDTMNYSYLNSLVGQSVAVKERIVEEDPKEQGIRKALNFGHTIGHAFESLSFLKMRPILHGHAVAAGIVSELYLSHKLCGFPMEKLSQVVYYIKEYYPALFFDCTDYDTLYELMTHDKKNEGGIINFTLLKNVGDVRINQSVTKEKILESLDFYRESFGI
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Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 39407
Sequence Length: 353
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q6MF52
|
MLNSSNYVIQSHCLDDLKYYLESLSYSKVVIITHPQLWVMYEQKITEQLFKLSWNFSVLLIPEGETSKSLKQTTRCWRHFIKHQLDRYSLVVALGGGVICDLAGFVASCYMRGIDTIYLPTTLLAMVDASIGGKTGINTSKSKNIIGSFHLPKKILIDPFTLKTLSKKHYQAGFAEIIKYGMIASPSLFEFLENSWSLIEQRDEGLLEIIIQQSCAIKKKYVEADFKDLGIRAQLNYGHTFGHVIEMMSRYQYLHGEAVSIGMSCAAYLSCQMGLTTQETMQRQDALCQQAQLPIHLPHFPLTRFTYLMAKDKKGRNGSINLILPEKVGKVTQIFDVDPHLIKNTLSTKMTK
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 39939
Sequence Length: 352
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q47QY7
|
MTVTRIGVGGTSTPYDVVVGNGILGELPALVGERAQRVAVIHPDTLEEKARPVCEILRTAGYDVFPLPVPDGEAAKDVSVAADLWARLGQAAFTRTDVIVGVGGGATTDLAGFVAATWLRGVRAILVPTTLLGMVDAAVGGKTGINTAEGKNLVGAFHPPAGVVCDLDTLPSLPREDYIGGLAEVIKAGFIADPVILDLVEADPEAATRPDGAHTRELIERAIAVKAEVVSADLRESGRREILNYGHTLGHAIERAENYTFRHGYAISIGMVFAAELARLDGRIDAALVARHRRILESVGLPVRYRADAWPALRDTIRVDKKTRGATLRFVVLDDVAAPAILAGPSDALLAQAYQAVSGVAPDAPDTD
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Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 38705
Sequence Length: 368
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
B0K924
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MDFITIDLKERSYPIYFAYDSFDKLGEIVKKHVRSSKTFIITDFNVYPLYFEKLNESLKKSRFDVSYEVIPAGETSKTMEMAQRLLEKAYDYGLLRDSSVIALGGGVVGDIAGFVAATYMRGIDFVQIPTTLLAQVDSSVGGKVAVNLKKGKNIIGAFHQPKMVYIDTAVLNTLDKREILGGLAEIIKYGIIWDFSLFEYIESNIYEILDLEEDKLRHIIKKSCEIKGKIVSLDEKEENLRSILNFGHTIGHAIEALTGYERYIHGEAVAIGMVYACKLALNLGYIDEKYFERIFSLIQRTGLPTDYEDLHKEDIVEAIKLDKKSREAKINFVLLRGLGKAEVTTVKEEEILKVLK
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 40371
Sequence Length: 356
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q8DKS3
|
MTTLIPVPLGEHSYRIAIGANTRRQLPALLAAYTPLTPKAPALIVSNPQIWRHYGTDVQGALTQAGWQVTPCILPAGERYKTLRTVEKIYDAALSQRLERGSTLFALGGGVIGDMTGFAAATWLRGIAVVQIPTSLLAMVDAAIGGKTGVNHPQGKNLIGAFHQPRLVVIDPDVLATLPPREFRAGMAEVIKYGVIWDAELFHLLSQLPRLDCMGALPSEQFIQVLRRSCQAKVDVVSKDEREAGLRAILNYGHTIGHALESIGNYRLLNHGEAVAIGMIAAGELAVALGYWSAEAAAAQRALILKAKLPTTIPPHFDVEGLLALLQHDKKVQAQNVRFILPTAIGHGQICDQVPAELIRETLHRLQA
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 39775
Sequence Length: 368
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q978S6
|
MDTQRFVITMNGDNISFIVGDNAINHLSEEAGKYDSIVIMISKTVEEMYANHIPDVGSFGNSVVKISLNDGESLKSLRNYQKIVKVLLERKVDRRSLLVYIGGGTVGDLAGFVASTYKRGVMMIAVPTTLLAQVDSSIGGKNGLDFSDVKNVIGTFYNPYMVIDDTVFLKNNSFIIREGMSEVIKYAIISGGDMYDTLNRCSIDNFDACATNIIKLSVKIKSEIVNRDFYDRTGIRSVLNLGHTIAHGIEGATKGSISHGKAVATGMLVEAHIGEKYGNTNHEVIEAIRDLMKRYGIEELNLKEIGPGNILRYISNDKKIMEGYINMPVPSEIGKVITMKATERMISDGINTFIKENDAS
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 39616
Sequence Length: 360
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
B5YHI4
|
MEKLRVELGERSYEILIDRGNLSLIGERLLRFSISKKIGIISNPKVSELYGQKVISSLQKEGFEPFVILIPDGEHYKDYFWAYHILTQLLEFGFDRGSFLIALGGGVIGDITGFVASIYMRGISYIQIPTTLLAQVDSSVGGKTAVNHPLGKNMIGTFWQPSLVWIDVDTLESLPEREFISGLAEVIKYGVIWDKEFFEFLEINRTKILKKDKDILISIIKRACEIKAEVVSKDERESALRAILNYGHTIGHAIETLTGYSSYLHGEAISIGMVHEAKLSSMLGFLDKEDFEKIRNILKEFGLPVNLPINMDSSAMLKTILLDKKNIEGKIRMVIPDSIGKMKINFEISGEDLKKVLNE
|
Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 40436
Sequence Length: 359
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
|
Q83GD7
|
MMKKYSLTTHSTETCQILFTSVSNVFKYIPSGTRRILIMYQDSVSQVLPIFSAASGVQCYRYLIPDSESAKQLGVAEQCWRFLAQNNFTRSDLIVSCGGGAASDLSGFVASSYLRGIKVIHIPTTLVGMVDAAIGGKTGINLKEGKNLVGSFYSPYIVLCDPSMLTTLNEEHLKSGLAEIIKCGFIQDESILSILEHNAQDHMDCSQRVCAETLPPKLLEELIHKAVSVKITMVDSDFRDTHKRQFLNYGHTLAHALEAATSHKLPHGQAVSIGMVYAAQVAFAKGLIGRNILTRHERILETYGLPICPPEVQWRNITPYMQRDKKNMQSNDTDSDKDSREMPQISTQSKLVLLREIANPFISSVSHTVLLKAYEAMFPQ
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Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 42194
Sequence Length: 380
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
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A5CX62
|
MKILNLDLGYKSYPIYIGQNLLLKGELLTKHISGKQVMIVTNTTVAPLYLKKVQNLLLSFEFAQVILPDGEKYKTLDTVNCIFSALLEKRFDRSCTLIALGGGVVGDMTGFVAASYQRGVNFIQIPTTLLSQVDSSVGGKTGVNHMLGKNMIGAFHQPKCVLIDIYTLDTLDSQQYSSGMAEVIKYGLLVEYLNFFNFLQENIKDLMDRKQSLIIEMIYQSCQHKINIVAQDELEMGKRTLLNLGHTFGHAIENTLGYGTFLHGEAISVGILMATRLSQLEGYLSSKQVAKIQDLLEKANLPISIIGKINASAFMKAMLVDKKVINGNIRLILLKRLGQAFICDNYNNHLLDQVVNEFCQ
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Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 40112
Sequence Length: 360
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
EC: 4.2.3.4
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C7PC56
|
MNSFGRLFRVNVFGESHGASVGVNIDGIPAGIPLTQEDFLPDLERRKAGAKGTTPRKEEDLPFIKSGVFNDHTTGAPITILFENNNTRSTDYEKLREFPRPGHADFVATHKYGGFEDYRGGGHFSGRLTLNLVAAGVIAKKILGPGISVKATLKEVAGLPDAEQGLEAAIAAKDSVGGIVECVVEGLPIGLGEPFFDSVESTIAHAVFSIPAIKGIEFGAGFAAARMKGVEHNDAILDASGKTATNHAGGVVGGITNGNPLVFRVAVKPTSSTPKEQHTLNIKSGEVENFSVKGRHDLCIALRVPVVLEAVAAMALADFMLLEQRSNRVFKN
|
Cofactor: Reduced FMN (FMNH(2)).
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Mass (Da): 35153
Sequence Length: 332
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
|
A1BHE5
|
MIRYLTSGESHGPALSAIVEGVPAGVGITPEMINTELARRQQGYGRGGRMKIETDQAEVLSGIRFGKTIGSPITLIIRNRDWENWTTTMSQFSEPAEDIAKITIPRPGHADLTGKIKYGLNDIRPVIERSSARETTARVAAGTISRIFLKAIGIEIGSYISAIGSAGETTADTQIEKLLRSGAETLARKADRSAVRMLDKKKEAEAIIAIDAAKDAGDTLGGIIEIFITGVPMGLGSYMQHDRRLDANLAAALISIQAIKGVEIGTAFANALKPGSQVHDEFIIEPEKGLTRSSNRAGGIEGSMSSGQTIHLRAAMKPISSLLTPLHSFDSETLQPTLSRFERSDTCAVPAAGVVAEAMVSTVIANAVLEKFGGDHLGEIQTRISLHRDLTRKAFIA
|
Cofactor: Reduced FMN (FMNH(2)).
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Mass (Da): 42410
Sequence Length: 397
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
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Q58575
|
MVTLMNTYGDMFRVTVFGESHGKAVGAVVDGCPANLPLSEEDIQKELDRRRPGQSIFSTPRKEEDKVEILSGIFEGKTTGAPICSIVYNKNMRPKDYSKIKDTPRPGHADLTYRLKYKNYDYRGGGRASGRVTIGHVIGGAIAKKLLSYTYNIKIIGYTIKIGKIEGDFSYYKNPEVFENEKSLERLIEIIESNPLRCPSMNEKEMEEYVLKAMENKDSVGGVVEIVALNVPVGVGNPIFNKLNGELARALMSINAVKGVEIGAGFKAAEMYGSEMNDEMYFDDDKNIRFKTNNCGGILGGISCGTPIVLRIAVKPTPSIGKKQKTINLKTLENVEIEIEGRHDPVIVPRIVPVAEAMVAITLADLMIKGGFIHPCSL
|
Cofactor: Reduced FMN (FMNH(2)).
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Mass (Da): 41615
Sequence Length: 378
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
|
Q1AW05
|
MRFGFSTAGESHGPAEVVIVHGVPAGLRLLAEDVDRDLARRQLGYGRGGRQKIERDRVEFLGGVRHGRTLGSPVAMLVRNRDYANWERRMNPAPVEDPPEPITLPRPGHADLAGMQKYGFGDLRNVLERSSARETVARVAAGAVARRLLGEFGVRVFSAVYRIGEVAMDRALAAAGAGKADRSEVRCPDPEVSERMKAEIDAARHARDALGGEFVVVAEGCPPGLGSYADWRDRLDARLAAAVVSINAIKGVEIGDAFEAARRRSSEVQDEIVRRGGALGRASNRLGGLEGGMTNGEPVVVAAAMKPISTIARALRTVDLSTGEEARAFRERADSCAVPAAAVIGEAMVAVVLAEAFLEKFGADALEDIRASYEHYMRRIGLPARRADA
|
Cofactor: Reduced FMN (FMNH(2)).
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Mass (Da): 41724
Sequence Length: 389
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
|
Q980I7
|
MPGNSFGKLFRITTFGESHGPAVGVVIDGVPAGLPLTVEDIKFELEFRRPGRLYVSGRREKDEPEILSGIFNNRTTGSPIAVIVRNTDVISSFYDEIKYKPRPGHADLPFIMKYGYENWDYRGGGRASARETVSRVIAGAVAKKLLMLTDTWIAGHLRSLGPEELSEEVTFEEVLCSKYSPVRASKKDLEEKYEALIKKATQEGDSYGGIAEVIAKNPPIGLGEPVFDKMKAELAKAIMSIPAVMGFEYGLGFIASKMKGSEANDEIIRKNNRIGWKYNYAGGILGGLTNGEDLIVRCAFKPTSSIRKPQKTIDLRNLEESYISVIGRHDPAVAIRGVTVVESMVALTIVDHAMRAGAIPLVKLTEDQANTIQQRWERYVKSCKPMEESQS
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Cofactor: Reduced FMN (FMNH(2)).
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Mass (Da): 43179
Sequence Length: 391
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
|
Q2S0W2
|
MLRYLTAGESHGEAIIGVLEGAPAQLPLTPDDINEHLARRWLGYGRGGRSKIENDTVHIYSGVRFGKTLGSPISFRIDNGAYEKDKAGWPEKMAIEGEPPEDMEKVTMPRPGHADLAGKQKYEHDDMRPVIDRSSARETAMRVACCSVARRLLNEFGIEVGSHVVRIGDVGFDEPEEWADRRNALIEEGGGASALYETADESATRMIDDGMTERCVEHIDQTKKDRDSLGGVYEVVVTGVPPGLGSYVHWDRRLDGQLVQAICSIQAQKAAEVGDGFFNAHRPGSQVHDPIEPREDGAQAYPRRTNHAGGTEGGTTTGMPLVVRGYMKPIPTLIKPLDSVDTATGEPEPTRYERSDITSVPAASTVAEATVAYTVANAFLRKYGGDSVPAIRRHVEADRAAPNE
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Cofactor: Reduced FMN (FMNH(2)).
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Mass (Da): 43986
Sequence Length: 404
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
|
P35146
|
MNVLTIKGVSIGEGMPKIIIPLMGKTEKQILNEAEAVKLLNPDIVEWRVDVFEKANDREAVTKLISKLRKSLEDKLFLFTFRTHKEGGSMEMDESSYLALLESAIQTKDIDLIDIELFSGDANVKALVSLAEENNVYVVMSNHDFEKTPVKDEIISRLRKMQDLGAHIPKMAVMPNDTGDLLTLLDATYTMKTIYADRPIITMSMAATGLISRLSGEVFGSACTFGAGEEASAPGQIPVSELRSVLDILHKNTRG
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Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 28132
Sequence Length: 255
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
A7Z2G6
|
MQSITIRNTVIGEGLPKIIVPLMAAGEKELLEEIEAVNRLRPDIIEWRADVYEHVDSLDAVKDMLEMLRKAAGATPLLFTFRTHKEGGNKVIDDRFYIELLKTAIETKHIDLADVELFTGEAEVKLIVKTAEDNGVYVVMSNHDFHQTPKKEEIISRLRNMQAYGAHIPKIAVMPQSTEDVFVLLDATHTMKTQYADRPIITMSMAGTGLISRLAGEVFGSACTFGAGKEASAPGQIPVEELRSVLSILNKHM
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Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 28085
Sequence Length: 253
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
B2TQ57
|
MKRIVQVKNVKIGEGIPKICVPIVGATSKEILDEAEKLKELTLDIVEWRVDFYEEVFDIEKVKDTLSKLTTTLNEVPLIFTFRNKIEGGEREIPIEYYLKLNLEVAKTKLVDLIDVELFIGDDLVKEIVEVAHDNDVKVIISNHDFFKTPCKEEIISRLIKMIQLNGDLPKIAVMPQCEIDVLTLLYATNEVKHKYPNNSIITMSMSGRGIISRIAGEIFGSCLTFGAAKKASAPGQIGVEELNSVLKVLHENI
|
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 28552
Sequence Length: 254
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
Q186A6
|
MKRKVQVKNITIGEGRPKICVPIIGKNKKDIIKEAKELKDACLDIIEWRVDFFENVENIKEVKEVLYELRSYIHDIPLLFTFRSVVEGGEKLISRDYYTTLNKEISNTGLVDLIDVELFMGDEVIDEVVNFAHKKEVKVIISNHDFNKTPKKEEIVSRLCRMQELGADLPKIAVMPQNEKDVLVLLEATNEMFKIYADRPIITMSMSGMGVISRLCGEIFGSALTFGAAKSVSAPGQISFKELNSVLNLLHKSIN
|
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsilon-amino group of Lys-170 at the active site.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 28876
Sequence Length: 255
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
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B9E0D7
|
MGSIVKIRDVKLGEGIPKIAVPLVGSNEEEIMEEIAGVKTTKLDIVEWRIDYYKYVEEVEKVKKLLQKMRKNLNNIPILVTFRTAKEGGKREISLEYYIELNKAIAATGNTDMIDIELFAAEDEAVKKIVEELHEYNIKVIMSNHDFHKTPHKDELISRMCRMQQLGADIAKIAVMPCSTKDVLELLSATCEMKCKHNDTPIITMSMGTLGVITRLAGETFGSALTFGSAKAASAPGQLEVNELYKVLKLISAYR
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Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 28536
Sequence Length: 255
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
A0PYE7
|
MKTVNIRGVILGEGIPKVCTPLVGRSLKELREEINLLKDIDCDLVEFRADFFEHVENIQKVKEVLLEIREALKEKPILFTFRSAKEGGEREVESEFYCKLNKEIIKTKLIDAIDIELFNEEESILELIKIAHDEDVKVVMSNHDFHKTPPKEEMISRLVKMQELGADVTKIAVMPKGSSDVLTLLEATNDMKIKYAKTPFITMSMKGVGMISRISGEVFGSAVTFGASKKASAPGQLQVKELKEILNVVHNVL
|
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 28470
Sequence Length: 253
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
B6J6K1
|
MLNTPRICVVVIGKTLEEFLSQLEAAQTAVDFVELRIDYLEQINPNWVRIIKNHTQKKAILCCRARADGGKFLGTPEAQQEILQAGNDLGFDYLDIDLPVANKISIHEKKAKIIISYHNFLHTPPITELNFLLENMRLFNPDVFKFATKSEQYEDVKTLFKLLINKKNNENMIVLGMGEQGKIIRLLSPLLGGYLTFSSINGAISAPGQIDFKTMQDFYQRFYKISSPLKGED
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Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 26499
Sequence Length: 233
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
Q3Z989
|
MKNPPVCCVITRLPEAESLKKSEGAAFYELRLDLLGESWREAAAMLDKPFMATCRRSAEGGSFSGSEEERIGLLEKAAAAGAFMLDIEYSTPHLGEVLKRLRTQSKCLVSHHNFADTPSAGDLKTLVKDMLNYPADIYKVITTATSINDNIKLLNLIKEIPDKKIVAFAMGNLGILSRILCPLAGSPFTYASLNDSNQSASGQMTLAQMIEIYRSVNYENHT
|
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 24366
Sequence Length: 222
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
Q6AIT8
|
MHSRKICVSLGQPTMPQALEASLRIFGADVIEVRLDYIDVPEIDPFVESLATDLLFTCRPTWEGGLFAGTEEDRLALLAEAVRAGAAYIDLELRSAEESHQYLRTYLAERETELILSYHDFESTATLAKLTGIIDQMQDAGADIGKLITTANSAADVVRVFQVLEYAAKKGLPLIAFCMGEAGAVSRVASCDLGGYMTYCCADGAEVTAAGQITISEMRGIFARYP
|
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 24531
Sequence Length: 226
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
A5G270
|
MILSGHARLAGVIGYPVAHSRSPRLHGTWLERHGIDGAYLPLAIAPDDFAACVAALAKMGFAGANVTIPHKEAAFAVCDRVADSARRAGAVNTLVFTPTGIEGANTDGSGFLANLRAHGVNPAAGPALVLGAGGAARAIATALQDAGAVVTLCNRSPERAVALARDFGLVHIPWEARSAALADHALVVNTTSLGMAGHNPLELDLARAAPGMAVADIVYVPLETPLLAAARARGLVAVEGLGMLLHQAVPGFAAWFGVTPVVDDALYRAVAADLMG
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 28086
Sequence Length: 276
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q9YEK4
|
MIRLALFGSGVSSSLSPAIYRGFAAKRGLRLEYRVYEAGPGGLAPALRMAGELHGFNVTKPLKREALSLASTLDSHARAIGAVNTMVAGEEGWEGFNTDWKGFLDSLKLYTASPPDTALVIGAGGAGRAAAYALATWGAGRVLIASRTGLTARRAAQDLAGLGAEVEPVPPGGLEDAAAASDVVVNATPLGWDGVSTPVERGFREGCIAVDMVYRPLATPFLRRAAASGCTPVDGLWMLAIQAAENIAVWLGLEASPVELRTYALEAMRGGRG
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 28352
Sequence Length: 273
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
B6JIM2
|
MSETPTACLIGWPAAHSRSPIIHKYWLKELGIAGDYRIEAVEPAAFPDFIASLAARGYCGANVTIPHKEKALALSLPDARARAVGAANTLYFRDDKLHSTNTDVEGFIGNLDASAQRWRADDDAVVLGAGGSARAVVFGLIERGVPRIHLVNRSRERAQALAQPYGERVSVASWDDVESLLPKAGLVVNTTSLGMKGQPPLPLDVALLRADATVADLVYVPLRTELLTAAAGRGLQTADGLGMLLHQAVRGFELWFGRRPQVSPALRALVEADLTVK
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 29703
Sequence Length: 277
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q8UJC5
|
MADSRETLTINAFVVGYPIKHSRSPIIHSYWLKKFGIAGSYTAVEVSPDDFPKFIATLKEGKPGAAVGGNATIPHKEAAYRLADHPDALAEELGAANTIWMEEGKLHATNTDGYGFVSNLDERHPGWDKTQRAVVFGAGGASRAVIQSLRDRDVAEIHVVNRTVERARELADRFGPRVFSHPQAALQEVMHGAGLFVNTTSLGMNGTEAPHLDFSHLAANAVVTDIVYVPLKTPILNMAQEQGIATVDGLGMLLHQAKPGFRRWFGRIPEVDETLRSLIIADMEKH
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 31237
Sequence Length: 286
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
B9JG24
|
MGDSRETHGLNAFVTGYPVKHSRSPLIHGYWLRTLNLAGSYRAVEVTPDDFPAFIAALKDRSSGFVGGNVTIPHKEIAFKLADRPDELSEELGASNTLWLEDGLLHATNTDGRGFTANLDECHPGWDRTDRAVILGAGGASRAVIQAVRDRGVNEIHVVNRTVERAQELSDRFGAQVHAHPMAALGEVMRSAGLFVNTTSLGMENEVAPTIDFSPLAENAVVTDIVYVPLKTPLLAQAEEQGFATVDGLGMLLHQAAPGFETWFGKRPVVDEVLRALIIADMDKHR
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 31070
Sequence Length: 286
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q82U74
|
MDTYAVIGNPVAHSKSPFIHARFAQQTGRIIHYTALLAPLDRFEQTVLDFRKTGGKGMNITVPFKFEAFTLASRLTDRASAARAVNTFRFEETGEILGDNTDGVGLIRDIEVNLNFPLAGKRILLMGAGGAASGVILPLLQQQPDLLAIANRTPDKAVSLQRQFASYSNITTGHYHDFAGQHFDLIINATSASLHNELPPVPADLFRNAFAYDMLYSSRLTPFLELARVQGAGYLADGAGMLVEQAAESFLLWHGIRPETQTVIRQLRDNLRHPTS
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 30350
Sequence Length: 276
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
A9A233
|
MGKTFAVIGDPIDHSLSPNIHSAAFRELNLDCSYIAYRIPKDELGEGIEGLKKIQIAGFNVTIPHKIEMMKYLDKIDESCSLIGAVNTVVSNDGVLKGYNTDMDGFLEPLKKRNIEIENSNVLLLGAGGAARAIVAGFAKEKAKSITIANRTIEKANNLVEFAKKISLDANAITIDQVGESAKDYNIIVNATSIGLQNESSPISFEGVNEKTVVYDIVYLPMNTDFLKKAKEKNATIIFGYEMLLGQAVRAFEIWHGMEAPYNAMKKALLGGF
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 29824
Sequence Length: 273
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q2YBM5
|
MSDLYAVIGNPVAHSKSPLIHAGFARQSGQDVRYEAILAPLDGFVETVAAFRQRGGKGANVTVPFKLEAHTLSSCLTERAKAAGAVNTLVFGADDILGDNTDGAGLVRDVAVNLGYALDDRRVLLMGAGGAARGVIRPLLEHEPAALVIANRTPQKADDLQRLFASSGNVLSAAYEDLRGQEFDLVINATSASLQGDLPPLPKGIFAGASLAYDMMYGKGLTSFLQFAQQQGAARLADGIGMLVEQAAESFFLWRGIRPETEPVIGMLRSSLGSP
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 28997
Sequence Length: 275
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q3J818
|
MPDRYAVMGNPIAHSKSPQIHTAFAQQTGQALTYTGLQVEAGKLAEAITAFQQQEGKGLNITIPLKAEAWRLVDQCSPQAQRAKAVNTILLEKNGALLGDNTDGVGLVRDLINNHGGRITGQQVLLLGAGGAASGVIEALLKEHPSHLIIVNRTPAKAIELAARFSPFGAITGGGYELLENNSFHLIINATASSLQGELPPLPRGILRSGGWVYDMMYGNEPTIFMKWGQTHGAARSLDGLGMLVEQAAEAFFIWRKVRPKSAPIIAQLRREMDIKNPAMPL
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 30329
Sequence Length: 282
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q8EPU9
|
MTLSLKLIGYPIEHSMSPWIHNEFLKRSNLEGTYELFEISPEESFEDNVTTLKKSVLTGFNVTVPYKQKIMQFLDEVDDTANLMGAVNTVSIRDGKWIGYNTDGIGYLRSLYAAYPFLKGVTNKRVLILGAGGAARGIFHALVNEGYNNIKIANRTLSRAESIIGTNKQALAISLEEAAEELHQFDLVIQTSAVGMNEPRSIIILDRINEDTVVSDIVYQPLETHFLQLAKQRTPYIHHGHTMLLYQAQAAFEIWTGTNVNVSGMDMQIEQILKGR
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 30965
Sequence Length: 276
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q30VD9
|
MTIPRIPRQLYGIIGYPLGHSMSPLLHNWGFELLGEQAAYMAFPVAPEKLAEFICCARMLPVSGLSVTIPHKQAVMPLLDAVTPRAQAAGAVNTLFYDDGKLTGDNTDVYGFLHPLDSCGTAHAAALVLGAGGAANAVLAALTARGMCNVTVTNRNGDRARILAERFGVRCVAWEERHAVDADLVVNTTPLGMAGDRQAQTPLDPAFFSSRPAGLAYDLIYNPAQTFFLASAQAAGWRVLNGLDMFVAQGAEQFRIWRGRELPFAQARALIADALASGC
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 29799
Sequence Length: 279
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
A1B5V3
|
MVDTLPTPKHAPLAGVIGWPVAHSRSPRLHGHWLERYGIAGHYVSLPVMPEHLAEVLRAMPHMGFVGANVTIPHKESVLALADVVTDRAALIGAANTLIFRADGKIHADNTDGYGFIANIRQHAPDWIPDLGPAAVIGAGGAARAVVASLLESGVPELRIANRTRIRAEQIRAEFGAKVVVYDWAQAGNMLEGAMTVVNATSMGMEGKPPLRVPLEALAPSTLVTDLVYTPLMTPFLAEAQARGCEVVDGLGMLLHQAAPGFERWFGQRPEVDDDLRRAVLA
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 30207
Sequence Length: 282
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
A7HSJ1
|
MKKVCVIGWPVEHSRSPLIHNYWIGLHGIEGAVYERLAVPPDAAAETIRNLGGLGFIGANVTVPHKETAFAALARHDAIAKRLKAVNTIVTTPAGLEGRNTDGYGFIANLKDRAPGWDAKAGPAVLLGAGGAARAIAAALEDEGAPEIRIINRTPSRAEALARDLGLRNALVFADGEAKTALDGAALLVNTTTLGMKGESDVDLDISPLPAPALVTDIVYTPLETRLLRRAREAGYKTVDGLGMLLHQAVPGFEAWFGVRPQVTPELRALVLADMGMK
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 29385
Sequence Length: 278
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q6D006
|
MSEVTSFAVFGNPIAHSKSPRIHELFAAQTGITLTYQRVLAPLDNFEQMLRQYFHDGAGGANVTAPFKERAFAEADERSECAALAGAVNTLKRLSDGRLYGDNTDGIGLLSDLQRLALVKPLDRVLLVGAGGAARGVIQPLLASGCTVVLTNRTFFKAEALAKIFCDIGDIQATALDGLHGQSFDLIINATSSGMYDSIPNLPAELISPETSCYDMFYLPQLTPFLSWCVQQGAIHYADGLGMLVGQAAHAFKLWHGVMPDVEPVIDLLKQDLAK
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 29628
Sequence Length: 275
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
A1ARJ6
|
MNPCSTPSLYGVIGYPLGHSLSPLLHNTAFRELGIPGVLLPWSIEPERLPAFIQSVRLLNIRGACVTIPHKQSIIPLLDRVTDRVKALGAANTLYWDGDLLCGDNTDILGFMSPLQADPPSAEQTRVLVLGAGGVARAAVAGLKSLGLNQITITDIVDASSATLAETFDLKTIPWSQRSEVDAHILINTTPLGMKGKFEEESPYPTEALAARQGIAYDIVYTPFVTRFLREARAAGWKTIGGLEMFISQADHQFLTWTGRNLPQAAKQAVIDALTAT
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 29915
Sequence Length: 277
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q4FNS5
|
MKKTFLVIGNPIKHSLSPKLHNYWIKKYKINATYEKNLLDHSEIEDLIFNIRKEKIHGLNITVPFKKMIIPFLDELSEEAEISQSVNTIYKRDNKIIGDNTDIEGFKLSLEKTEQNVKNKKALILGAGGVVSSIIIALKKIQIEKIYLSNRTELKAIELKKHFPEIEIIKWGETIDFDMIINATSIGLKEEDEININYQKISKDKFFYDVIYNPPETNFLKNAKKYGGITKNGKMMFIYQAQKAFFIWHKIVPEVDSETINLLDV
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 30740
Sequence Length: 265
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q7MYI6
|
MDQFAVFGNPVAHSKSPRIHQLFARQTGIEHRYGKILVPISKFQEALDTFLKQGGIGVNITVPFKEQAFIRANELTERARLSGAVNTLKLLNNNQLLGDNTDGIGLLTDLMRLEFITQGQHILIIGAGGAARGVLFPLLEFGCKITITNRTFSRAIQVANNFSAIGSIRPAEMKVLNSPEFDLIINATASGINGEIPTISPFIFNENCVCYDMFYQANLTPFISFARKHGVSRYADGLGMLVGQAAHSFKLWHGVLPEISPVLLTLEQELRS
|
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Mass (Da): 29914
Sequence Length: 272
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
P34725
|
MFITNEHVGDRSRMEDWRIRGYDPLTPPDLLQHEYPLTPESQKIIVEGRNAACDILNGKDRRLIGPCSIHDPQAALDYCERLYQASEKHKGELLIVMRAYLEKPRTTVGWKGLINDPDIDGTFHINKGLRIARKLFVQLTSKLPIAGEMLDTISPQFLSDLFSVGAIGARTTESQLHRELASGYHSQLDSKTVPMVLWVLPLTPLRAASHPHHFLSVTKPGVVAIVGTDGNQDCFVILRGGKKGTNYDAKSVQETQEELIKSKVVTEMKPGPRIMVDCSHGNSNKDHRNQPKVAQVVAEQVAGGDKSICGLMIESNINDGRQDVPPKEQGGKDALKYGVSITDACIGWETTEEVLEVLANAVKTRRSL
|
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Mass (Da): 40731
Sequence Length: 368
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
|
A0MH68
|
MAMSNTSALASKLLPSCKPHQPTLTFFSPSTTCQKKPRSSRPISAAVHVTQPPKTPISSATATKRRLSLLNGVWESWKSKKALQLPEYPDEGKLDGVLKTIEAFPPLVFAGEARSLEEKLAQAAMGNAFLLQGGDCAESFKELMPLYSRYFQNTASDECRLTFGGQCPVIKVGRMAGQFAKPRLDPFEEKDGLWLSGANGWPVAWEAYCKLQQLSPSRALLLVVCCYAESHPMDLDFVEHSEQGDRYQELAHRVDEALGFMDACGLTVDHPIMATTEFWTSHECLLLPYEQALTREDSTSGLFYDCSAHMLWVGERTRQLDGAHVEFLRGVANPLGIKVSQKMDPNELVNLIEILNPTNKPGRITVIVRMGAENMRVKLPHLIRAVRGAGQIVTWVCDPMHGNTIKAPCGLKTRAFDAILAEVRAFYDVHEQEGTLPGTECVGGSRTITYDDRQTRYHTHCDPRLNASQSLELAFIIAERLRKEESVLNAHSP
|
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Mass (Da): 54743
Sequence Length: 493
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Subcellular Location: Plastid
EC: 2.5.1.54
|
P00888
|
MQKDALNNVHITDEQVLMTPEQLKAAFPLSLQQEAQIADSRKSISDIIAGRDPRLLVVCGPCSIHDPETALEYARRFKALAAEVSDSLYLVMRVYFEKPRTTVGWKGLINDPHMDGSFDVEAGLQIARKLLLELVNMGLPLATEALDPNSPQYLGDLFSWSAIGARTTESQTHREMASGLSMPVGFKNGTDGSLATAINAMRAAAQPHRFVGINQAGQVALLQTQGNPDGHVILRGGKAPNYSPADVAQCEKEMEQAGLRPSLMVDCSHGNSNKDYRRQPAVAESVVAQIKDGNRSIIGLMIESNIHEGNQSSEQPRSEMKYGVSVTDACISWEMTDALLREIHQDLNGQLTARVA
|
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Mass (Da): 38804
Sequence Length: 356
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
|
Q02285
|
DPNSPQYLGDLFSWSAIGARTTESQTHREMASGLSMPVGFKNGTDGSLGTAINAMRAAAMPHRFVGINQAGQVCLLQTQGNPDGHVILRGGKAPNYGPEDVAQCEKEMLKAGLRPALMIDCSHGNSNKDYSRQPGVAESAIAQIKDGNRSIIGLMLESHINEGNQSSEQPRSEMKYGVSVTDACINWEVTETLLREMHQDLQGVLSARLSQEV
|
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Mass (Da): 22967
Sequence Length: 213
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
|
P80576
|
MSQQTTPNAPGWAPDSWRSKPIKQCPEYPDKAALEKATNELKTLPPIVLPNEIIRLREHLRDVAQGKAFLLQGGDCAELFSYCQQDVIESKIKLLLQMSLVLLWGADKPVVRIGRMAGQYAKPRSSPVETINGKEVPSFRGDILNGFHPDERELDPNRLVRAYQYSSATLNYIRGAIGSGIADLHGPLDWGLGHVRDPALKSKYQETVDRIQEMLRFMHTIGADQNEKLSTVELFTSHEGLLLEYEEPLTRLLNHPSVRSYPPDSTTPPKKEYYNTSAHFLWIGDRTRQIDHAHVEYFRGIANPIGVKIGPSTPTSDLLPMLRTLNPNREPGKVTLITRYGADKVASLLPAHIRTVESSEYARTVVWQCDPMHGNTQSVSGGIKTRKFSDIFSELQQTLRIHKEEKSYLGGMHLELTGDAVTECLGGGAGLDEDDLSTNYTSFCDPRLNEKQALELAFLVADHYRQERKEKEAERRKSSVV
|
PTM: The N-terminus is blocked.
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Mass (Da): 54067
Sequence Length: 481
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
|
Q75LR2
|
MSLATSSSMAGGAAVVPRSATATTASAFVTMKRRATAVRAVHAAEPSKNPPVGVPSAAKTSSPSVAAPEKAPVAAAPAPVAPAPAATKQVAPARWAVDSWRTKKALQLPEYPNAAELEAVLKTIEAFPPIVFAGEARHLEERLADAAMGRAFLLQGGDCAESFKEFNGNNIRDTFRVLLQMSAVLTFGGQMPVIKVGRMAGQFAKPRSEAFEERDGVKLPSYRGDNINGDAFNEKSRIPDPQRMVRAYAQSAATLNLLRAFATGGYAAMQRVTQWNLDFTQHSEQGDRYRELAHRVDEALGFMSAAGLTVDHPLMTSTDFWTSHECLLLPYEQSLTRQDSTTGHFYDCSAHMLWVGERTRQLDGAHVEFLRGVANPLGIKVSDKMNPTELVKLIEILNPSNKPGRITIITRMGAENMRVKLPHLIRAVRHAGQIVTWITDPMHGNTIKAPCGLKTRPFDSIAEVRAFFDVHDQEGSHPGGVHLEMTGQNVTECIGGSRTVTFDDLGDRYHTHCDPRLNASQSLELSFIIAERLRRKRIRSSKLNNMLPLPPFGV
|
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Mass (Da): 60490
Sequence Length: 554
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Subcellular Location: Plastid
EC: 2.5.1.54
|
Q09755
|
MDKHTPLLPGDSVFSRCKTEDSRIKGYDPVISPALIQSELAASDETLAFVSDQRRQAADIIAGRDDRLLLIVGPCSLHDPVAAKEYAIRLQKEAIKHKKDLHIIMRAYLEKPRTTVGWKGLINDPDLDGSYNINKGIRVARRIFLELLETGVGIASEMLDTISPQYLADLICWGAIGARTTESQLHRELASGLSFPIGFKNATDGNIGIAIDAMNSSANPHHFLSVTKQGVVAIVTTTGNPDTHIILRGGKSGTNFDADSVAGAKAKLEECNKLPSIMIDCSHGNSSKNHKNQPKVAACIAEQVANGQKAITGVMIESHLNEGKQAIPEDDLSSMKYGVSVTDACIGWDDTTAVFEQLAAAVRSRRSH
|
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Mass (Da): 39760
Sequence Length: 368
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
|
Q834S1
|
MESIVLIGFMGAGKTTIGQSLANKLKMPHLDLDTALIEKIGRSIPDYFEKYGEAAFREQETQLLKELSKNTAVLSTGGGIVVGPENRSLLKSFQQVIYLHATPEELLKRITEDTENQRPLAIERSSKEIITLFESRKNFYEECAKMTIDTTNRSPEEIINEILQQLKE
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19004
Sequence Length: 168
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
A5FNY2
|
MEKIVLLGYMGCGKSTIAQNLSKITQIPFLDLDICIEKRANLSIKEIFEQHGEIYFRKLEHEMFLELLQSSENAIIGLGGGTPCYANNHLLLQRDDIVSVYLKASIDTLYNRLVHNKSKRPLIANMDEEEMKEFIAKHLFDRSFYYNHAQHKVAVDNRTIDETVQDILDILA
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19815
Sequence Length: 172
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
A6GZJ6
|
MKKIVLVGYMASGKTEIGKLLSKKVNLPFLDIDYLIEESLSKTVNEIFEEKGEVFFRKKEHEVFKNKINSKQSFILSLGGGTPCYAENHLFLQKDDVISIYLKGSVATLVDRLKMNKDKRPLLKNLANDELAEFVAKHLFDRNFYYSHCKYTIIIDDKSPFDIVEEIHKILF
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19927
Sequence Length: 172
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
Q2J827
|
MGEPATDAWTGPMAWTGPMVVLVGAPGAGKTTVGTQLARRWGVGFRDTDADIEAALGTTVADIFLDHGEEYFRLAERRAVAAALADHRGVLALGGGAVLDAENRTLLAGHRVVYLEVGVSDAVRRVGLARDRPLLVEGPRTRLAALLRARRPLYAEVATVVIDTAGHEPDEVTDLLAAALGPLLAGGSEPDEAADAAGGSEPDEAADAAGGSEPDEAADAAGGKR
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 23047
Sequence Length: 225
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
B0TXQ6
|
MIRTKNIFLIGPVGAGKSTIGKQLAKQLKLEFIDSDDTIEKKCGVDINWIFDLEGEEGFRKRERDVIAEILAEKQNIVLATGGGAILDPDTRSLLSSRGKVVYLEATIEQQLERTAKDTKRPLLRVDDKKPVLEQLMAEREPLYRSIADVVVETNGATVKNIVNKISTFLVEETIL
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19667
Sequence Length: 176
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
Q8RF94
|
MKDNIALIGFMGSGKTTVGKLLAKTMDMKFVDIDKVIEAHEKKSINDIFHEKGQIYFRDLEREIILQESLKNDCVIATGGGSILDNENIKRLKETSFIVFLNATIECLYLRLKDNTTRPILNDVEDKRKLIEELLEKRKFLYQISADYIIDINEHTNIYETVDKIKEIYIIS
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19948
Sequence Length: 172
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
B5YHI3
|
MKNIVLIGFMGTGKTSVGKLVAKKLGFDFVDVDEVIEKATGMEISEIFSKFGESRFRDIEEEMIKLITPKKRQVIATGGGVVLRDENMKRLKKDGVIFCLRASENVIFERLKQTTNRPLLQVENPEERIKELLQKRMPLYEKADFCIDTEGLTPEEVAEKIIKEYERLSNGKT
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19773
Sequence Length: 173
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
Q3SM89
|
MSKRDNLYLVGLMGAGKTTVGRLLAKHYGCTFYDSDHEIEARTGVKIPVIFEIEGEAGFRRREEAVIAELTTLSGIVLATGGGAVLSPANREHLRTNGLVIYLRGSPEQLCERTRNDRNRPLLQTGNPLAKLRELYQQRDPIYRELADVTVDTARQSVAGMTRVLYGKLDLLKGEATSFDPAG
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 20190
Sequence Length: 183
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
B8GPV2
|
MTQTSNIILIGPMGAGKSTIGRQLAAALHLPFRDSDKEIEKRTGVDIPTIFEFEGEEGFRNRESAMLEELCTEQGIVLATGGGAVMRPQNRALLRDCGLVVYLKTSVKTQLRRTARDRNRPLLQTENPRARLEELMRIRDPLYREIAELTVDTDRDSIRKVVQEISRYYRMNNKDSIPQDDSNTEPQGDG
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 21534
Sequence Length: 190
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
Q87L67
|
MAEKRNIFLVGPMGAGKSTIGRHLAQQLHMEFVDSDTVIEERTGADISWVFDVEGEEGFRKREEAVLEDLTQEQGIVLATGGGSVKSKENRNRLSARGVVVYLETTIEKQLARTNRDKKRPLLQTDNPREVLEQLAEERNPLYEEVADYTVRTDDQSAKVVANQIVKMLEER
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19472
Sequence Length: 172
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
Q8D1X8
|
MVEKRNIFLIGPMGAGKSTIGRQISQQLSMEFFDSDQEIEKRTGADISWVLDLEGENKFRIREEKIINEITEKQGIVLATGGGSIQSRKTRNRLSARGLVVYLETTIDKQLDRTKRDKKKPILQNKNSVKSFLEKLATERNPLYEDIADLIIKTDFKSAKIIAHQIINTLFKT
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19753
Sequence Length: 173
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
Q4UX85
|
MNPAPNLVMIGPMGAGKSCIGRRLAERFGLDFVDVDQAIVEQVGSSIPAIFEQHGEARFRQHEAEALHGLLAQSNKLVSTGGGAILDAGNRQRIRERGFVVYLHVSVPAQLTRLARDRNRPLLQRPDREQVLHGMAALRTPLYQEVADLTLETDHLSPAEATAQLVLRLAAQWRMSSTPA
|
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19761
Sequence Length: 180
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
|
Q3IWV4
|
MTTTIYILNGPNLNLLGQRQPEIYGHETLADVERRCAAVAAEKGFSVRLFQSNHEGAIVDQIHEARQAACGIVINPAAYTHTSVAILDALNAFEGPVIECHISNVHKRESFRHHSYVSLRADGVLAGFGIEGYELAVRRICSLCAGG
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 15971
Sequence Length: 147
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
Q8KD64
|
MMSATSLLVMNGPNLSRLGKREPEVYGSLTLDEINRGIAVAFPEVSFEFFQSEHEGALIEKLFEIEGRGGFSGVVLNAGALTHYSIALRDAISAVTMPVVEVHLSNVHKREEFRHKSVISAVCIGVIAGFGVESYHLGVRALLGRGNR
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16053
Sequence Length: 148
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
A8AQF2
|
MADKLHILLLNGPNLNMLGTREPDKYGTLTLTEIVNRLNAEADALNVTLDHLQSNAEYALIDRIHQAKDTVDYILINPAAFTHTSVAIRDALLAVSIPFIEIHLSNVHAREPFRQHSYLSDIAAGVICGFGADGYSYALQTAVKRLSQSH
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16520
Sequence Length: 150
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
Q97KL8
|
MKILVINGPNINFLGIREKEIYGEGTYEDLCKFIKDEGSKIGIEVEVMQSNIEGEIINFLQAAYNKVDGIVINPGAYTHYSIAIYDAIKSINIPTVEVHISNIHTREEYRRKSVTAPACIGQICGFGFYGYVMGITALKNMLSK
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16056
Sequence Length: 144
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
C1FPC5
|
MNNILVINGPNLNLLGKREPDIYGNITLENINQKIKLHFKNEDLKIDFFQSNEEGKIIDKIIESEKKYNAIVINPAAYSHYSIAILDAMRSINIPVVEVHLSNIYKREEYRKKSVTAEASLGVISGFGYYGYIMAIEFILNNLVREK
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16850
Sequence Length: 147
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
Q487R8
|
MTAKFTVLVLNGPNLNMLGKREPTIYGNQGLSEIIADLGLQADQKNIVLKHLQSNAEHELVDAIHNGYQQVDFIIINPAAFTHTSVAIRDALLSVAIPFIEVHLSNVHAREAFRKHSYLSDIATGVICGFGAQGYSFALDAAYTYLNKAQVDK
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16751
Sequence Length: 153
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
Q8DLJ7
|
MASHILVLHGPNLNLLGQREPGIYGTVTLASINQSLEALAQELGVTIECLQSNHEGVLVDAIQGALGRAQGILINPAAYTHTSVALRDAIAAVALPTVEVHLSNIHQREAFRHHSYIAPVAIGQIAGFGADSYLLGLRALVNYLQQKANS
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 15903
Sequence Length: 150
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
B8GUV7
|
MAKFLLLNGPNLNLLGTREPQIYGSQTLAQICDTLREQAKAHGHVLEDFQSNAEHELVERVHRASREGIDFILINPGAFTHTSIALRDALLGVAIPFIEVHLSNVHAREPFRHKSYLSDVARGVIMGLGPKGYALALDAAIHLTQKN
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16209
Sequence Length: 147
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
Q9KV60
|
MTAKSRILVLNGPNLNLLGLREPTHYGSQTLEQIVAILRDQAQKADIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTHTSVALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIRALQAKQ
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16574
Sequence Length: 150
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
Q87KU6
|
MSAKSRILVLNGPNLNLLGLREPTHYGNNTLAQIVDALTEQAHNAGVELEHLQSNREYELIEAIHAAYGKIDFIIINPAAFTHTSVALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAEGVICGLGAQGYEFALSAAINKLQAK
|
Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16260
Sequence Length: 149
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
|
P0AB94
|
MLLAGAIFVLTIVLVIWQPKGLGIGWSATLGAVLALVTGVVHPGDIPVVWNIVWNATAAFIAVIIISLLLDESGFFEWAALHVSRWGNGRGRLLFTWIVLLGAAVAALFANDGAALILTPIVIAMLLALGFSKGTTLAFVMAAGFIADTASLPLIVSNLVNIVSADFFGLGFREYASVMVPVDIAAIVATLVMLHLYFRKDIPQNYDMALLKSPAEAIKDPATFKTGWVVLLLLLVGFFVLEPLGIPVSAIAAVGALILFVVAKRGHAINTGKVLRGAPWQIVIFSLGMYLVVYGLRNAGLTEYLSGVLNVLADNGLWAATLGTGFLTAFLSSIMNNMPTVLVGALSIDGSTASGVIKEAMVYANVIGCDLGPKITPIGSLATLLWLHVLSQKNMTISWGYYFRTGIIMTLPVLFVTLAALALRLSFTL
|
Function: Involved in arsenical resistance. Thought to form the channel of an arsenite pump (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45497
Sequence Length: 429
Subcellular Location: Cell inner membrane
|
P15848
|
MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLPEYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM
|
Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation . Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium . In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity).
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD).
Catalytic Activity: Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate.
Sequence Mass (Da): 59687
Sequence Length: 533
Subcellular Location: Lysosome
EC: 3.1.6.12
|
Q5HF02
|
MTTLATLIFLVTLLFVLWQPKGLDIGITALTGAFIAVITGVVSFSDVFEVTGIVWNATLTFVSVILISLILDKVGLFEWSAIHMLHASKGNGLKMFVYIILLGAIVAAFFANDGAALILTPIVLAMVKNIGFSKRAIFPFIIASGFIADTTSLPLIVSNLVNIISADYFHVGFVRYFSRMIIPNLFSLLASIIVLWLYFRKAIPKTFDDNNIKHPKDAINDLKLFKISWIVLVILLFGYLISEFTKIPVSIFTGIIAFIFLMLARKSNAVNIKQVIKGAPWNIVLFSIGMYIVVFGLRNAGITLILAKILEYISNYGLFSTILGMGFISAFLSSIMNNMPTVLIDAIAIGQSNVHGMLKEGLIYANVIGSDLGPKITPIGSLATLLWLHVLTQKDVKISWGTYFKTGIIITIPVLFITLIGLYLTLIIF
|
Function: Involved in arsenical resistance. Thought to form the channel of an arsenite pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47141
Sequence Length: 429
Subcellular Location: Cell membrane
|
Q5HRI3
|
MTTVLAIVIFFITLTLIIWQPKGLDIGISAIIGALLVIITGVVNFTDILEVIGIVWNATLTFVSVILISLILDEIGFFEWSAIHMVKASNGHGLKMFIYIMILGALIAAFFANDGAALILTPIVLAMIRNLGFNNKLVFPFIIACGFIADSTSLPLVVSNLVNIVSADYFGIKFVEYLMRMFIPNLFSLLASILVLWFYFRKSIPKTFDISSISEPKDAIRDTRLFKISWIILALLLIGYLVSEFIHIPVSFITGAIAVIFILLARQSNVVHTKQVIKGAPWNIVIFSIGMYLVIFGLKNVGMTLILADILSSIAQHGLFSSIMGMGFVSAFLSAIMNNMPTVLIDAIAIDQSHAISSIKEGMIYANVIGADLGPKITPIGSLATLLWLHVLVQKGVKISWGTYFKTGIVITIPVLFFTLLGLYLTLIIF
|
Function: Involved in arsenical resistance. Thought to form the channel of an arsenite pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47142
Sequence Length: 430
Subcellular Location: Cell membrane
|
Q8CQF4
|
MTILAITIFILTLIFVIWQPKGLDIGITALIGAVIAIITGVVSFSDVLEVTGIVWNATLTFVAVILISLILDEIGFFEWSAIHMVRASKGNGLKMFVYIMLLGAIVAAFFANDGAALILTPIVLAMVRSLGFDKKAVFPFIIASGFIADTTSLPLIVSNLVNIVSADYFDIGFVEYFSKMIIPNIFSLIASILVLWLYFRKSIPRKFDAVNIREPKEAIKDKKLFNISWIVLTVLLVGYLISEFINIPVSIIAGIIALIFVLLARKSKAVHTKQVIKGAPWNIVLFSIGMYLVVFGLKNVGITTLLSDVLTNISSYGLFSSIMGMGFISAFLSSIMNNMPTVLIDAIAIGQSQTTSILKEGMIYANVIGSDLGPKITPIGSLATLLWLHVLTQKGVKISWGQYFKIGIIITIPVLFITLLGLYLTLIIF
|
Function: Involved in arsenical resistance. Thought to form the channel of an arsenite pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46839
Sequence Length: 429
Subcellular Location: Cell membrane
|
P0DKS6
|
MNNQPSVLFVCVGNGGKSQMAAALAKKHAGDALKVYSAGTKPGTKLNQQSLDSIAEVGADMSQGFPKGIDQELIKRVDRVVILGAEAQLEMPIDANGILQRWVTDEPSERGIEGMERMRLVRDDIDARVQNLVAELTQNA
|
Function: Involved in defense against toxic arsenate. Involved in the mycothiol/myoredoxin redox pathway which uses a mycothioltransferase mechanism; facilitates adduct formation between arsenate and mycothiol (By similarity).
Catalytic Activity: arsenate + mycothiol = arseno-mycothiol + H2O
Sequence Mass (Da): 15117
Sequence Length: 140
Subcellular Location: Cytoplasm
EC: 2.8.4.2
|
O60180
|
MELDPSDSNSRVVDASQFSKYRDAGALVSKAFHQVASRCVPGASTREISSYGDNLLHEYKSSIYKSQRFEKGIAEPTSICVNNCAYNYAPGPESVIAGNDNSYHLQVGDVTKISMGLHFDGYTALISHTIVVTPPPQPGMGPYIGPGADAICAAHYASKAVANLLATNNSDDPITGSRLRKIVDDIASQFRVSVCPGSRIRRISRFLVGQPTIDRLEEDQNTKHAVEWPAPEEETRKADVTNSLDPANVLSTELNTWHVMPKEAWLIDISMSSQPISSLKEHPDLKPTLYIHDVNVSYMLKLKASRSLLSEIKKEKSVFPFHFGSLSSERNLLGLRELTDRHILVPMPVLISSPSNVIAREELTVITQPNPSSDLLCLTVPTPPSYVKSDFSLEDGTDAALICEGINVNIKSININV
|
Function: Probable metalloprotease involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm (By similarity).
Sequence Mass (Da): 45673
Sequence Length: 417
Subcellular Location: Cytoplasm
EC: 3.-.-.-
|
Q6CCY2
|
MSLARSTALLDEKNTLTSSVTDKYRLAGKITQTCLQHIIQTVLTQYETYTVGEMCRMGDEFLERATTAVYKSVAEKGIAQPVRIEKQEFVGGVSPENGDKFQGGMLAPGDLVKISLGVYIDGYTAQVTQTEVVRHVPNTSAGETEQPLTGSPADAVCASYLASEAVIAYLAQVTDPNPGKAVGVVTGTKIRELVEKIAAAYHVKIVPGSSVRRIRRFLAGQHDIVLERDYKGVLWEVEGEEERALHAVKLAESEAKQESTEGAVCLYEQHIEEEENFTVEAGEAYQVDIQMAAAPQKGAIRLYDFQGYDESGTVINQYGRDFSVTYGLKIQASRKLLSQLEATTSVYPFKLSHVESNVAKARLGLGEILAHQILVPIPVKVAKFVPLAALYEFSKNSKARARDEASKAVPVARNSSSVLLTNDACLRLTGGQAFPPPYVHSAFELPEDVTNLLKLVGHKHGAKVKDVLPGDVDMAPAKEAKMEE
|
Function: Probable metalloprotease involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm (By similarity).
Sequence Mass (Da): 52671
Sequence Length: 484
Subcellular Location: Cytoplasm
EC: 3.-.-.-
|
Q03862
|
MALAISHEDTQILLKDKNILQESVLNKYRTAGQIAQTALKYVTSLINDSYHSKTTQRQLTVPELCLLTDSFILTRLEQYYKNKVNERGIAIPTTIDIDQISGGWCPEIDDTQNLLNWNKGKDSTFASSVTGTLRPGDLVKITLGVHIDGYTSEVSHTMVIYPVDETKPILQPTGPLLGGKADAVAAAHIAMETVVALLACALTPEKLPASLGGTSSGITGQLIRTIVDTIARSYNCGVVPGSRVRRIRRFLAGQNEGIVAEREYKGVVWTESHQEADLLSNTDAKDLTVVDRGQSTPFTNVSAIPSDDFVVQSGEVYLIDLKMASLEHCTKKGLVTLETVDSYTGKSHKAGELIARPGAYVRDFAQTHILKLKTSRQLLTKIDKQGVYPFKLSHLSSNFPFVHENEEELQSLKKDLKSFRLGMSEISNNYLCVESPIQIARWVPWDHILKATNPNGNLSYDATSTLTLPGHELPLPKLGVSAIKLKSLMNSTKESISLPVARECNTIVLCDSSVSTTDRPELLRLTGGSKTCQPSWIHSQHELNPQDSIVQGIFQLATLAKDKRFGLLLKETQPMKQKSVETSNGGVEETMKM
|
Function: Probable metalloprotease involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm.
Sequence Mass (Da): 65213
Sequence Length: 593
Subcellular Location: Cytoplasm
EC: 3.-.-.-
|
C0HK79
|
MNSLLSRANSLFAFTLSVMAALTLGCILTTAFKDRSAPVRLHVSRILLKKVEDFTGPRKKSDLGFITFHISADLEKTFDWNVKQLFLYLSAEYSTKSNAVNQVVLWDKILLRGENPKLNLKDVKSKYFFFDDGHGLKGNRNVTLTLSWQVIPIAGILPLVTGSGRVSVPFPDSYEIATTF
|
Function: Plays a role in adipogenesis.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 20146
Sequence Length: 180
Subcellular Location: Endoplasmic reticulum membrane
|
P18440
|
MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVVRRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYIVDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDLLEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLTHRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI
|
Function: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens.
Catalytic Activity: acetyl-CoA + an arylamine = an N-acetylarylamine + CoA
Sequence Mass (Da): 33899
Sequence Length: 290
Subcellular Location: Cytoplasm
EC: 2.3.1.5
|
A0A455R4Z0
|
MPQLAGKLILAGLIPLGAWVLHGFASCNGLIQMFEDFGKQTVLSDGVTDYTGAFTGLEGLDRLLRTLLNFFWPVANGHDWALSLHAFMFAGQGVPLLVLNMLEGARPGNKSLVVSYVTVFGILYMVVGLAIMAPLYLFLHLLTSRTATAPSKAKVAVDPNTAKAVGFGVFVGYVLPTIFMSLPHPSLLSTDTKVLSVVFWQAVPLWASVCAYFASTALGQSATSRSSSNLPSALGAVYAASLIIATATHVATFAISANLSDTWSGIFTFLIPPNPFNTDMRISSFLEGATWFLQWDYTMMSLAYMVWAIGIRHGVEVPRSSHHFETLGKIALRSMAKLLVMGPIGAALSLVWERDQLLWQLDSESGEKGEKNRSRRMSRKWMFS
|
Function: Epoxide hydrolase; part of the asc-2 gene cluster that mediates the biosynthesis of ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis . The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units . Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B . Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB . The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group . Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin . The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG . On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring . Finally, ascofuranol is oxidized into ascofuranone by ascJ .
Catalytic Activity: 16-hydroxy-ilicicolin A epoxide = ascofuranol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41823
Sequence Length: 384
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 5.4.99.-
|
A0A455R5K2
|
MTDIHIQDGDLSSLKDKVVVITGGSSGIGLATTNLLLDLGAKVVIGDLQPPTTRVDSERCSFHKVDVTVWSDQLTLFKEARELHGRIDHVFANAGVGPKADYLSTALDQNGDLVEPTFLTLDVNLKAVIYTATIACYYMREEQQSPAGGSIVIVSSVAGVSRFRAVDYATAKHGNLGFARGLHQRLTAENSPTRVNLIAPSWTNTGFMPPQIMAAVGVEPQEPASVGRAAAYLMADDSRKGQMIHIAKGRYREVEESIMLPAAEKVVDVENGGVMEDDTLAKIIETMGIFKAKATQ
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Function: Short-chain dehydrogenase/reductase; part of the asc-2 gene cluster that mediates the biosynthesis of ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis . The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units . Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B . Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB . The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group . Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin . The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG . On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring . Finally, ascofuranol is oxidized into ascofuranone by ascJ .
Catalytic Activity: A + ascofuranol = AH2 + ascofuranone
Sequence Mass (Da): 31856
Sequence Length: 296
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.1.99.-
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Q6YWS8
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MGVPPVDWEAESYPAYSDFAAIPLFAVFLFAVRYLLDRFVFEWLARRLIFEKDEKLDLATHAGRIKIRKFKESAWKCIYFLSAELLALSVTYKESWFTSTKNFWVGPGDQVWPDQRIKFKLKLVYMYAAGFYTYSIFALQFWEIKRSDFGISMVHHVVSVILIALSYIFRFARVGSIVLAIHDASDVFLELGKISKYSGYQLLADVSFLIFVCSWAVLRLIYYPFWILWSTSYEVVPMLDKKKHKFDGPLHYYVFNCLLFSLLVLNIYWWVLMYRMLVEQILSKGHVGDDVRSGRFSPPFIPP
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Function: Mediates resistance to sphinganine-analog mycotoxins (SAMs) by restoring the sphingolipid biosynthesis. Could salvage the transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted cells after SAM exposure (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35584
Sequence Length: 303
Subcellular Location: Endoplasmic reticulum membrane
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Q5UK76
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MNIFRLLLATLLVSLCFLTAYSHLAEEKPKDDRSLRSNSSVNLLDFPSVSIVALNKKSKKISRKEAEKKRSSKKKASMKNVARPRPPPPTPCVATRNSCKSPAPACCDPCASCQCRFFRSACTCRVLSPRC
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Function: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment).
Sequence Mass (Da): 14505
Sequence Length: 131
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P42127
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MDVTRLLLATLLVFLCFFTANSHLPPEEKLRDDRSLRSNSSVNLLDVPSVSIVALNKKSKQIGRKAAEKKRSSKKEASMKKVVRPRTPLSAPCVATRNSCKPPAPACCDPCASCQCRFFRSACSCRVLSLNC
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Function: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). In higher primates, agouti may affect the quality of hair pigmentation rather than its pattern of deposition. Could well play a role in neuroendocrine aspects of melanocortin action. May have some functional role in regulating the lipid metabolism with adipocytes.
Sequence Mass (Da): 14515
Sequence Length: 132
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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