ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q2KD36 | MNESESEIQARLLAQALPFMQRYENKTIVVKYGGHAMGNPELGKAFASDIALLKQSGVNPIVVHGGGPQIGAMLTKMGIESKFEGGLRVTDQKTVEIVEMVLAGSINKEIVALINQTGEWAIGLCGKDGNMVFAEKARKTIKDPDSNIERVLDLGFVGEVVEVDRTLLDLLARSEMIPVIAPVAPGRDGATYNINADTFAGAIAGALNATRLLFLTDVPGVLDKKGQLIKELSVAEAHALIADGTISGGMIPKVETCIDAIKAGVQGVVILNGKTAHSVLLEIFTEHGIGTLIVP | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 31174
Sequence Length: 295
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
Q7UQZ8 | MDQAIAKADTLIEAMGWIRRFRGKTTVIKLGGSLLEDREALQHLLLDVIFMETVGLRPVVVHGGGKAITEAMAKAGIEAQFIRGRRVTDEKSLEVVEQVLAGELNVELTEMMERFGGRAVNLSPRTTCVLKGKKLIDPEGDDLGFVGEVTEVDRDVIESLAYTDQVAVIPSLCTDDKGQLYNVNADTAAMAVAQSLGADKLVFLSDVNGVRRDPEDPATIIPALSAEEARQLIADGVIKSGMIPKVEACLETLGRGVQKVHIIDGRLRHSLLLEIFTTDGVGTEIHQ | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 31081
Sequence Length: 287
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
B6IPH3 | MSTPSPAAAPSREEWLAKARTLSEALPFMRRYAGRTVVVKYGGHAMGDESLGRRFANDIVLMKQMGISPVVVHGGGPQIGQMLERLKIKSEFVDGLRVTDKETVEIAEMVLSGSINKQIVALINDAGGDAVGLSGKDDDLIEARKVTRSKRDPDSNIEKVIDLGFVGDPFRVNPGLLHKLQQADIIPVIAPIGIGEDGQTYNINADTAAGAIAAAVNATRLLLLTDVAGVLDKQKRLIPEMSVEAAQRAIDDGTATGGMIPKIETCLRAVNGGVEAAVILDGRVPHAIVLELFTEGGAGTLIGRK | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 32274
Sequence Length: 305
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
A7NPB5 | MTDPVSRQPTLVIKVGGNELDDATFVKELARIVAAMRPIPTLVHGGGKEIGVLQETLGSAPRFVGGLRYTDATALTAAEMVLCGSVSTRLVAALIVAGADALGISGVDRGLIRVVKQEHPAGDLGRVGRPTAVRSEVLHELLNHDVIPVIAPIALGFDGPYNVNADEAAGAIAAALGADEVVFVTNVPGVLVNGDVMPRLTRHEIEHLIADGTISGGMIPKVRAALTALDAGVRAARITNLEGMLEHGTIIIAEGEVHE | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 26833
Sequence Length: 259
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
Q5E2E5 | MLKTAIIGASGYTGAELALMVFKHPHLSLSGLYVSENSLDKGKAISELHGSLKGIVDEALQPLVNVNQAAKECDVILLATAHEVSHNLAATFLENGCVVFDLSGAFRVKKEGFYSEFYGFEHQYEAWLDKAVYGLAEWNAEAIAKAQLVAVPGCYPTASQLALKPLVKSELLDKNQWPVINATSGVTGAGRKASLTSSFCEVSLQPYGVFNHRHQPEIAAHLGCDVIFTPHLGNFKRGILATITTKLAKGVTEKEIQEAFETAYTQTPAVRLLENEMPKIQSVEKTPFCDIGWKVQGEHLIVVSAIDNLLKGASSQAMQC... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 36245
Sequence Length: 334
Pathway: Amino-ac... |
Q5WEW7 | MEVGIIGATGYSGLELIRLLKNHPQVTNIMLYSSSQSGETINRLYPHLQNEQWKPLKEIDLNKISAEIDVMFLATPPGVSAEWSGPLLEAGLSVIDLSGDLRLTDRGVYEKWYKRPSAKEGLIEQAIYGLSEWNKSTIKTAKLIANPGCFPTAALLALIPLIQAGAIERDSIVIDAKSGTSGAGKSPTSMTHFSETNENFKIYQVASHKHTPEIEQQLAKWGAQPPLSFQPHLAPMVRGIMATIYAKAAKPLSNEWLTDCYNSAYENAPFVRIKENGTFPATKHVFGSNYCDIGFCYDERTGRVIVASVIDNLMKGAAGQ... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 37707
Sequence Length: 344
Pathway: Amino-ac... |
O67724 | MEQTLRVSVFGATGYTGIELLRSLLTHPHFEVKNLISQSYKGKKVREVLPFFSNTYISEIEFLEEPVEDYELAFLCLPHEVSYEIVPKLLSQGKKVVDLSGAYRIKSPKAYEEFYGFKHEREDILQRAVYGLPEVFREEIKNSDLVANPGCYPTATLLAIYPFLKERVGIESVIVHALSGVSGAGRKPKQQFHFPEMTENFFNYAVEKHRHTPEMEDVIRRVYGREVKVRFTPTVVPTSRGMISTVYLKSEKLNVKELFKEVYEDEIFVKVVDEPPQTKWVLGTNYCFIYPHYDERTGYYVIISAIDNLGKGASLQAVQN... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 38958
Sequence Length: 340
Pathway: Amino-ac... |
Q93Z70 | MSTASAFSSIQGCWFKGERKIRVADKRAKRLTLGSHVASPSSMSFRVSASSSVKPEKDIRIGLLGASGYTGAEIVRLLANHPHFQVTLMTADRKAGQSMESVFPHLRAQKLPTLVSVKDADFSTVDAVFCCLPHGTTQEIIKELPTALKIVDLSADFRLRNIAEYEEWYGQPHKAVELQKEVVYGLTEILREDIKKARLVANPGCYPTTIQLPLVPLLKANLIKHENIIIDAKSGVSGAGRGAKEANLYSEIAEGISSYGVTRHRHVPEIEQGLSDVAQSKVTVSFTPHLMPMIRGMQSTIYVEMAPGVRTEDLHQQLKT... | Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 44136
Sequence Length: 401
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular Location: Plastid
EC: 1... |
B7HB04 | MKVAIIGATGYGGIELIRLLEQHPYFSIASLHSFSQVGECITNVYPHLRNVLFHTLQEIDVKTIGKEAEIVFLATPAGVSAELTPKLVAEGLKVIDLSGDFRMIDPSSYELWYKRPAAKEEILRKAVYGLSEWKRTEIQKANLIANPGCFATATLLAIAPLIRSGMIEEDSIIIDAKSGVSGAGKTPTTMTHFPELYDNLHIYKVNQHQHVPEIEQMLTEWNSESQPITFSTHLIPISRGIMITLYAKVKQKMEIKQLQKLYEETYEQSPFIRICTQGKFPSPKEVRGSNYCDIGIAYDERTERVTVVSVIDNMMKGAAG... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 38512
Sequence Length: 345
Pathway: Amino-ac... |
Q9JY18 | MSKKIKVGIVGATGYTGVELLRLLAAHPDVEVAAVTSRSEAGTAVADYFPSLRGVYGLAFQTPDEAGLEQCDIVFFATPNGIAMKDAPRLIEQGVRVIDLSADFRIRDIPTWEHWYGMTHAAPDLVSQAVYGLSELNREAVAQARLVANPGCYPTCVSLPLVPLLRQCRLKPGMPLIADCKSGVSGAGRKGNVGSLLCEAGDNFKAYGIAGHRHLPEIRQTIAGLQDGIAEGFVFTPHLAPMIRGMHATVYLHLSDGSDPETVLRDYYRDSPFVDILPTGSAPETRSVRGANLCRISIQQAAQSDVWVVLSVIDNLVKGA... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 37214
Sequence Length: 347
Pathway: Amino-ac... |
O87890 | MGNFGRVPVGIVGASGYGGVQLVRLLMDHPEIELVYLGGESSVGKSFASLYPHLAHAVKLSIEEVDPEVIARRCEVVFLSMPNGLACQIVPTLLEKGCKVLDLSADYRFRNLTTYTTWYGVERSDRTTADTAIYGLPELYRDRISEAQLVGCPGSYPTASLLALSPLLKQGLIVPETAIVDAKSGTSGGGREAKTYLLLAEADNSLAPYSVVRHRHTPEIEQICSDLAGHEVTVQFTPHLVPIVRGILATVYATLRDPGLVGDDLTTIYTAFYRNSPWVKVCESGIYPQTKWAAGSNLCYIGVEVDPRTGRVIGMSVIDN... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 38197
Sequence Length: 352
Pathway: Amino-ac... |
Q8CUN2 | MKKAAIIGGTGYGAIELIRLLDSHPYIELAKIISQSQHGELLDETYPHLATYVTQPMQELHIQQLIEEIDIVFLATPAGVAKEIAASFLDSSIQCIDLSGDLRLSSSDYEMWYQKKPASEALLEKTAYGLTEVFQEKIKQANIISNPGCFPTAALLGLIPMLENNIIESKGIMIDGKTGISGAGKNSSAKTHFSTTNENVTPYKIGTHQHIPEIEKYLSQHVEESSVRVTLTTHLIPMTRGLMCTMYAPLQQDIDTADVIDLYKHYYEQSSFIRIRKQGEYPSTKDVTGSNYCDIGAYVDKRTNQLIISSAIDNLVKGAA... | Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 38252
Sequence Length: 346
Pathway: Amino-ac... |
Q6AV34 | MGSTALGGGAPARLGLAPKDGVFGSNLKQCGGFMLKTTPKVGSSSVRVRASVASSPQKQHSPKTSGVKSGEEVRIAVLGASGYTGAEIVRLLANHPQFRIKVMTADRKAGEQFGSVFPHLITQDLPNLVAVKDADFSNVDAVFCCLPHGTTQEIIKGLPQELKIVDLSADFRLRDINEYAEWYGHSHRAPELQQEAVYGLTEVLRNEIRNARLVANPGCYPTSIQLPLVPLIKAKLIKVSNIIIDAKSGVSGAGRGAKEANLYTEIAEGIHAYGIKGHRHVPEIEQGLSEAAESKVTISFTPNLICMKRGMQSTMFVEMA... | Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
Sequence Mass (Da): 44786
Sequence Length: 415
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular Location: Plastid
EC: 1... |
O66442 | MTYLMNNYARLPVKFVRGKGVYLYDEEGKEYLDFVSGIGVNSLGHAYPKLTEALKEQVEKLLHVSNLYENPWQEELAHKLVKHFWTEGKVFFANSGTESVEAAIKLARKYWRDKGKNKWKFISFENSFHGRTYGSLSATGQPKFHKGFEPLVPGFSYAKLNDIDSVYKLLDEETAGIIIEVIQGEGGVNEASEDFLSKLQEICKEKDVLLIIDEVQTGIGRTGEFYAYQHFNLKPDVIALAKGLGGGVPIGAILAREEVAQSFTPGSHGSTFGGNPLACRAGTVVVDEVEKLLPHVREVGNYFKEKLKELGKGKVKGRGL... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 42009
Sequence Length: 376
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4... |
Q9M8M7 | MASLSQITLPRAPSSEIGLLRRRLERPIIRTRIGFNGRIASVLTNAGDQAVSVKASVSQKVIEEEAKVIVGTYARAPVVLSSGKGCKLFDPEGKEYLDCASGIAVNALGHGDPDWLRAVTEQAGVLAHVSNVYYTIPQIELAKRLVASSFADRVFFCNSGTEANEAAIKFSRKFQRFTHPEDKEVATGFIAFTNSFHGRTLGALALTSKEQYRTPFEPIMPGVTFLEYGNIQAATDLIRSGKIAAVFVEPIQGEGGIYSATKEFLQSLRSACDAAGSLLVFDEVQCGLGRTGLMWAYEAFGVTPDIMTVAKPLAGGLPIG... | Function: Involved in the biosynthesis of citrulline (By similarity). Essential gene that modulates defense response to pathogenic bacteria, conferring susceptibility and repressing salicylic acid (SA) accumulation.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semi... |
O30156 | MDWIEREKKHILQTYTRQKVVIERGEGCYVYDVNGKRYLDLVAGIATVSIGHCNSHLVERLKEQLEKLIHISNLYYTTPQVELAEKLSEIAGMDRFFFCNSGAEAVEAALKFARRATGRKKFVSFTGDFHGRTMGALSVTHKEKFRKPFEPLVSPVEFAEFNNPESLEKVVDEETAAVIVELVQGEAGVYPADREFVKAIEELREKYGFLLIVDEVQTGFGRTGRWFAKDHYGIEPDMITMAKAMGSGVPIGCCALKEEVAEKIQVGDHGSTFGGNPLACTAALATIEVIEREGLVENSARMGEYFVKRLKESFENVIGV... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 41924
Sequence Length: 375
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4... |
Q9ZJ10 | MSSLFQTYGRWDIDIKKAKGTYVEDQNGKTYLDFIQGIAVSNLGHCHEAVTEAVKKQLDSVWHVSNLFQNSLQEQAAQKLAAHSAGDLVFFCNSGAEANEGAIKLARKATGKTKIITFLQSFHGRTYAGMAATGQDKIKTGFGPMLGGFHYLPYNDPSAFKALGEEGDIAAVMLETVQGEGGVNPASAEFLSAVQSFCKEKQALLIIDEIQTGIGRTGTRFAYQHFGLS | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 24779
Sequence Length: 229
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4... |
Q818W2 | MTSHLFQTYGRRTIEFVKGTGTKVIDNKGKEYLDFTSGIGVCNLGHCHPTVLKGVQEQLDDIWHISNLFTNSLQEEVASLLTENRALDYVFFCNSGAEANEAALKLARKHTGKSLVVTCQQSFHGRTFGTMSATGQDKVKEGFGPLLPSFLHIPFNDIKALEEVMNEEVAAVMVEVVQGEGGVIPVDLSFLKEIETLCNKFGSLFIIDEVQTGIGRTGTLFAYEQVGIEPDIVTVAKALGNGIPVGAMIGGKELGTSFTAGSHGSTFGGNYIAMAAAKEVLQVSKKPSFLKEVQEKGEYVLEKLQEELQHVECIQNIRGK... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 42060
Sequence Length: 386
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4... |
P59315 | MATEHEEKLGTEDSKWLGEYSQVHMNVFGTPLRVMDHGQGAHIWDVDGNEYLDFLAGIAVNSLGYAHPKWVKAVADQAAKVAHISNYFASEPQIELASKLVKLAGAPEGSKVYFGNSGAEGNEAALKLAKLYGRTLPGALPSIGGKPARILAMTHGFHGRTMGALSATWKPGIRKPYDPLVPNIEFVRAGDKVALHDAFAQTGLGRYGKGPVAAVILELIQGEAGVQPLGADYVKFVRELCDINHALLIIDEVQTGIGRTGKWFAFQRDDLSGGVTPDMVTFAKGVAGGFPMGGMIAFGEKLAALFTPGSHGSTFAGNPL... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 45615
Sequence Length: 431
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4... |
Q8R7C1 | MITYEKKYLMDTYNRYPIMLVKGEGTRVWDSEGNAYLDFVAGIAVNSLGHCHPALVEAIKKQAETLIHCSNLYWNEKQIELARMISENSFGGKVFFANSGAEANEGAIKLARKYASLKYGGKRYKIITAKNSFHGRTFGALTATGQEKYHKGFGPLLAGFKYVPLNDIEALYEAVDDEVCAIMLEVIQGEGGIHEATPEYVKAVRKICDENDLLFILDEVQTGIGRTGKLFGYEHYGVVPDIMTLAKGLGGGFPIGAIVAKEDKAVFKPGDHASTFGGNPLACAAGIAVLNEVTKDGFLEGVDKKGKYFREGLETLQKKH... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 43161
Sequence Length: 393
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4... |
Q9PIR7 | MDYKEQSHIIPTYKRFDIVLEKGQGVYLFDDKAKKYLDFSSGIGVCALGYNHAKFNAKIKAQVDKLLHTSNLYYNENIAAAAKNLAKASALERVFFTNSGTESIEGAMKTARKYAFNKGVKGGQFIAFKHSFHGRTLGALSLTANEKYQKPFKPLISGVKFAKYNDISSVEKLVNEKTCAIILESVQGEGGINPANKDFYKALRKLCDEKDILLIADEIQCGMGRSGKFFAYEHAQILPDIMTSAKALGCGLSVGAFVINQKVASNSLEAGDHGSTYGGNPLVCAGVNAVFEIFKEEKILENVNKLTPYLEQSLDELINE... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 43519
Sequence Length: 393
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4... |
P59316 | MNTPAINLETEKQLFFHNYARLPLDIASGKGSFLYTASGERYLDMIAGVGVNAIGYGDKRLEQAITEQASKYIHVSNLFMQKPQFDLAAKLLEISRMSKVFFCNSGTEAIEAAIKLARRFAARNGDTDKTQVLSLTNCFHGRTYGALSLTAKPKYVDGFEPLVPETGMIDFNDVEDLERKVSNRTAAVFVEFVQGEGGIHKVSEAFIAKLKELAKEHDFLIVADEIQAGCGRTGAFFSYMPFDIQPDLVCVAKPLGGGLPLGAIIGSEKVAEVFTPGSHGTTFGGNPVACAAGLAMIEAILADGLMQNALEVGSMMRTAF... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 43548
Sequence Length: 400
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4... |
Q97GH9 | MSKSYLMNTYGRFNVTFDKGEGTKLYDKDGNEYIDFVSGVAVNCLGHCNPSIVKAIEEQSSKLMHVSNYYWNENAMELTEILCKNSEFDKVFMCNSGTEAIEAGLKLARKYALLHGDENKKEIIYMDNSFHGRTMGALSVTGQPKYQESFKPLIGAVKSVKFNDLDDIKQKISSKTAAVIVEPIQGEGGIIPAKKEYLKLLRDLCDENNALLIFDEVQCGMGRVGSLFAYQKFEVVPDIVCIAKALGGGFPIGAMLAKESVASSFVPGDHGNTYGGNPLACAVAIAVLKELVDKKVVEINVNEKSKYLFDKLMTLKEKYK... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 42714
Sequence Length: 387
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4... |
P33280 | MSPSLVDNHAAAYIAAPSSAKAPMIQKPGNTFGMSSPIESKFLSQPRDLGIVAVGFSGGQCKPGVDAAPSALIESGLLTQLREELGYRLHGDDEVHLYTDLVPKEDPPHRNMKNPRAVSNVTKRIAEQVHSHAKEGRLVLTLGGDHSIAIGTIAGSAKAIKERLGREIAVIWVDAHADINTPETSGSGNIHGMPVSFLTGLASEDKEEFFGWLKPDHLLSVKKLVYIGLRDVDPGEKRILRENGIKAFSMHDIDKHGIGRVMEMALGHIGNDTPIHLSFDVDALDPMWAPSTGTPVRGGLTLREGDFICECVHETGSLVA... | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequence Mass (Da): 38265
Sequence Length: 358
Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.3.1
|
A0A509AF89 | MYECIQDYLTNHKDEKNIYVNKCISIVGSPLSAGQSLSGVNKACDNLRKFGLHDVIKAVGWGYEDIGNIGEKIPINGFLKQENIEKENDQINNNNPSYYNNIKNAEVIGKFSEKLFQTMSSELKKKNFILNIGGDHGVAFSSILSMLQTYNNLKVIWIDAHGDINIPETSPSGNYHGMSLAHALGLFKKKVPYFEWSEKLLHLKPENVAIIGIRDIDKYEKIILKKCNINYYTMFDIDKKGIYNIICEALNKIDPNKNSPIHISLDIDSVDSIYAPGTGTIAKGGLNYREIHLLIKSISDTKRVVSMDIVEYNPLLDESD... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis . May play a role in parasite intra-hepatic development during the host liver stage .
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequen... |
Q8I384 | MLDTIESYIKSHKEKENLYVKKNVSIIGSPLAAGQPLGGVQLACDDLRKLGLHNVIDVLGWKYEDIGNIDNGDNEMKQEKKTNNYINNNDNNNDNNNDNNNDNNNNCYIPNGVIKEKKHDLSNNKMNGYVNHNFYGNYEENNVISTNDKYKNNCYYDNIRNIKEIGIFSKNLFDTMSNELRKKNFVLNIGGDHGVAFSSILSSLQMYQNLRVIWIDAHGDINIPETSPSGNYHGMTLAHTLGLFKKKVPYFEWSENLTYLKPENTAIIGIRDIDAYEKIILKKCNINYYTIFDIEKNGIYNTICTALEKIDPNSNCPIHI... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis . May play a role in parasite intra-hepatic development during the host liver stage (By similarity).
Catalytic Activity: H2O + L-arginine = L-ornithin... |
P60086 | MTKTKAIDIIGAPSTFGQRKLGVDLGPTAIRYAGLISRLKQLDLDVYDKGDIKVPAVNIEKFHSEQKGLRNYDEIIDVNQKLNKEVSASIENNRFPLVLGGDHSIAVGSVSAISKHYNNLGVIWYDAHGDLNIPEESPSGNIHGMPLRILTGEGPKELLELNSNVIKPENIVLIGMRDLDKGERQFIKDHNIKTFTMSDIDKLGIKEVIENTIEYLKSRNVDGVHLSLDVDALDPLETPGTGTRVLGGLSYRESHFALELLHQSHLISSMDLVEVNPLIDSNNHTAEQAVSLVGTFFGETLL | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequence Mass (Da): 33265
Sequence Length: 302
Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
EC: 3.5.3.1
|
P00812 | METGPHYNYYKNRELSIVLAPFSGGQGKLGVEKGPKYMLKHGLQTSIEDLGWSTELEPSMDEAQFVGKLKMEKDSTTGGSSVMIDGVKAKRADLVGEATKLVYNSVSKVVQANRFPLTLGGDHSIAIGTVSAVLDKYPDAGLLWIDAHADINTIESTPSGNLHGCPVSFLMGLNKDVPHCPESLKWVPGNLSPKKIAYIGLRDVDAGEKKILKDLGIAAFSMYHVDKYGINAVIEMAMKAVHPETNGEGPIMCSYDVDGVDPLYIPATGTPVRGGLTLREGLFLVERLAESGNLIALDVVECNPDLAIHDIHVSNTISAG... | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequence Mass (Da): 35662
Sequence Length: 333
Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
EC: 3.5.3.1
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Q97GH6 | MDTIKVLNNKNITDVPYFKAIGVASGIKGNNKSDLCVIYSEKPCIAAGTFTTNKVKAAPVLLDLKHIESENIYAIVANSGNANACTGDDGYEKAYLMAECTAKHLKIKPEEVLVASTGVIGVPLPIDKVMFGIEKAFSILPKSDANKAIDAIMTTDTVQKKIFVEFMLDKKKVTICAIAKGSGMIHPNMATMLSFIVTDANITKDLLNKALKESVKDSYNMISVDRDTSTNDMALLLANGASGNTLISSENSDYEVFKKALHYVNVEISKMIAKDGEGATKLIEAKVFGASSSRDAKVAAKSVITSNLVKAAVFGSDANW... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
B2VVA8 | MSLARPNARLLSRTNRVFSSQIRTYSAPGDGVIPPAKKKYVPTSGTYPRGFKVGSAHVGVKASNTRFDDLALITSDTPCAAAAVFTKNKFQAAPVTVSRDLLKERGGQGIRAVIVNSGCANAVTGKGGIEDAKSMAKHTDACFTDSPDSPDSPYRSIVMSTGVIGQRLPIDKITSKIPTAFANLGDTHDHWLGTARAICTTDTFPKLMSKTFKLPSSDREYRIAGMTKGAGMIHPNMATLLGIICTDVPVAYFPLRRILASAANKSFNSISIDGDTSTNDTVAILANGAAGGDLIDTKFHSDFESLKQVITDFSIDLAKL... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
PTM: The alpha and beta chains are autoproteolytically processed from a single... |
Q7UUJ7 | MTDTAPQNDPTTSHVLPKGIRFAGVAAGIKASGKPDVSLIVTDRPSVMAGVYTTNQIVAAPVVLTRAKTPTSTGRVVLTNSGNANACTGDEGMQNAKTMCDLAAKLADCDSADVMVMSTGVIGKPLPMEKVRAGIEAAAGKLGDAESDFIASADAICTTDQFRKTVSETVTIRGQQFRIAAMCKGAGMIAPNMATMLGVVMTDAPIGPDAAQASLKQIAGRTFNRVSVDGHTSTNDTVMLVCTGMSVSEDAKEFNSDELKIWQEAATQVALKLAKMLVADGEGAARFFEVRVSGAADDGDAFVIAKTVAASPLVKTAITG... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
P96426 | MVQSVLSSTSHGSERADMSAASPQGFHCWTTHLGLADEGKDDFSMVISDRPCTSSVVFTKSLFAGPCVTLSKTSIEQTSPRGVLVLAKNANVATGAEGLRNASEIRASVARTVGIEPDALIMASTGVIGVQYPMDTIRAGLDGLGQGTPLDAHAVARAIMTTDTRAKVSERAVGTSTIVGIAKGVGMIEPDMATMLSFVFTDADVPQDTLNRIFRDVVDRTYNSVSIDTDTSTSDTAAVFANGSAGPVPDTEFEQALEEVCTDLVKMIASDGEGATKLIVTTVSGASSERQARVVGKSIINSPLVKTMIHGEDPNWGRVL... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
P62064 | MSSKVSPLAPTDVPAMPMIAGVRLATAAAGIRYKGRTDVLLVEMEKGTTVAGVFTTSKCASAPVEWCRDKLKGGSARALVVNSGNANAFTGKSGKQAATLTAQLAAKAIGCKPAEVFLASTGVIGEPLDATKFDGVLDALALDAGPDGWMDAAKAIMTTDTFPKVATATVKLGKAKVTINGMAKGAGMIAPDMATMLSFIFTDAPLSASCLQALLKAGVTDTFNAVTIDGDTSTSDTLLAFATGAAAENGAPKISRASDPRLKAFVKAFNAVLADLAEQVARDGEGARKLVEIIVEGAKTKVSARKIALSIANSPLVKTA... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
B9SZB6 | MYTCAPHFVSIKFPDLHSSKTLRPFGMSKREFKVFALASSVNEASNYIPAAPILIPEGPWNQIPGGVTAAKGFKAVGIYGGLRAKGEKPDLALVTCDVDAAAAGSFTTNMVAAAPVLYCKHALDISQTARAVLINAGQANAATGDAGYQDVLECADTVAMMLKVKREEVLIESTGVIGQRIKKDALLNALPTLVNSLTSSVEGAGSAAVAITTTDLVSKSVAIESQIGGINIRVGGMAKGSGMIHPNMATMLGVITTDALVQTDVWRKMVQTAVNRSFNQITVDGDTSTNDTVIALASGLSGSMSISSIDCTRAIQLQAC... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-ac... |
Q5LWL6 | MAKITKVSPLAPAAFPTLPVIDGVRLASIAAGVRYQGRTDVMLAVLDPGTSVAGVFTRSATRSAPVLDCQAKIGGASDGPAAILVNSGNSNAFTGHYGQTSVAEVTQAVADVTGVPVGRVFTSSTGVIGEPMKHERIVAKLGDLNAALSPDALEDAARAIMTTDTFAKGASRTVGIDGKMVKIAGIAKGSGMIAPDMATMLVYIFTDARVEQGALQAMLSAMTDKTFNCITVDSDTSTSDTLLLCATGASGVDAEGNAEFAAALEAVMLDLAQQVVRDGEGATKFVEIRVTGAANDVDAKVHGLAIANSPLVKTAIAGED... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-orn... |
O94346 | MQTKIFARLAGIGRARFVGTMPDKTKFISKSGTYPQGFSLNGIASGVKANGKKDLAILFSSRPCNAAAVFTKNAFQAAPVQVSRQTLNGCGGKDIHCVVFNSGCANAVTGEGGLMDAQLITAEADNLTRPHWTSWTENSEEFPSSLVMSTGVIGQRLKLDKIQSGLEHAVEDLGSTHEYWMRAAEAICTTDTFPKLVSRELSIAGKVYRIAGFAKGAGMINPNLATLLGLFVTDAPISVDAVRSILRHAINNSFNSISIDGDTSTNDTIAFLANGAAGGSEITKSSPAYKEIRDAVTDIAQQLAKLVVRDGEGATKFVTV... | Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
PTM: The alpha and beta chains are autoproteolytically processed from a single... |
A3DDM1 | MKHARQAKILEIIDKEVIETQEEIADRLKKAGMEVTQATISRDIKELRLIKVMTEDGRYKYAPFNSTDNTVFNRLMTVFSKSYVSSDYANNIVVVKTLPGMAPAAASAIDSMNYPEIVGSIAGDDTVLIVCRSEKIAKEFVEKLSKLAKSDDK | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 17065
Sequence Length: 153
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
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C1F4F3 | MSKHERHNAIRELIAQRPIASQDELRRKLVRRGFDVTQATLSRDIHELRIYKGPGGYALPNGNGHDEQDDLPDVDEVMSSFGLKVKQAQNQLVLVTTAGSAQPVALAIDHEDWPEVVGTLAGDDTVLIICPDQKRATVLAERLEKIIG | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 16369
Sequence Length: 148
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
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A6TR45 | MKYSRHAKILEIIDTMEIETQEELSEELRKIGFNVTQATVSRDIKELRLIKVLSKSGNYKYATLRSQENVLSDRLVRLFKDSILSIEYAGNIMVMKTLAGAAQAAASAIDAVDLKGVMGTIAGDDTIFVVVRDQDQMQEIEEKFRRLTK | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 16829
Sequence Length: 149
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
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Q2INH7 | MTSADRRRDAVARIIRARRIGTQEELLAALERAGFRATQATLSRDLARLGARRVSGPEGAVYELGADGADGADGGLAALRGLVSSIAANASMVVIRTHPGSAPAIARAIDLAQPPEVLGTIAGDDTIFVAPAGELRPRRLAARLAELLGTPSALAGEGGDRTH | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 16765
Sequence Length: 163
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
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Q970U6 | MRVVLIVDIVRQEEKLIAKALEENKVQYDIINVAQEPLPFNKALGRYDVAIIRPVSMYRALYSSAVLEAAGVHTINSSDVINVCGDKILTYSKLYREGIPIPDSIIALSAEAALKAYEQRGFPLIDKPPIGSWGRLVSLIRDVFEGKTIIEHRELMGNSALKAHIVQEYIQYKGRDIRCIAIGEELLGCYARNIPPNEWRANVALGGTPSNIEVDEKLKETVVKAVSIVHGEFVSIDILEHPNKGYVVNELNDVPEFKGFMVATNINVAQKLVEYIKENYSK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the ATP-dependent formation of a covalent bond between the amino group of glutamate and the gamma-carboxyl group of the C-terminal glutamate residue in LysW.
Catalytic Activity: [amino-group carrier protein]-C-terminal-L-glutamate + ATP + L-glutamate = [... |
P40616 | MGGFFSSIFSSLFGTREMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTSSEMANSLGLPALKDRKWQIFKTSATKGTGLDEAMEWLVETLKSRQ | Function: GTP-binding protein that recruits several effectors, such as golgins, arfaptins and Arf-GEFs to the trans-Golgi network, and modulates their functions at the Golgi complex . Plays thereby a role in a wide range of fundamental cellular processes, including cell polarity, innate immunity, or protein secretion m... |
Q2TA37 | MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQNLLVEERLAGATLLIFANKQDLPGALSSNAIREALELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRIFMAD | Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catal... |
P36404 | MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSSNAIREVLELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRIFTAD | Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catal... |
O08697 | MGLLTILKKMKQKERDVRLLMLGLDNAGKTTILKKFNGEDVDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSCNAIQEALELDSIRSHHWRIQGCSAVTGEDLLPGIDWLLDDISSRVFTAD | Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catal... |
A8ISN6 | MGLLSLIRGLKKKEGEARILVLGLDNAGKTTILKALSEEDITTITPTQGFNIKSLSRDGFNLKIWDIGGQKSIRPYWRNYFDQTDALIYVIDSADSKRLSESEFELTELLQEEKMTGVPLLVFANKQDLVGALAADEIASTLDLTSIRDRPWQIQACSAKQGTGLKEGMEWMMKQVK | Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Required for targeting proteins to the... |
Q1MTE5 | MGLLSILRKLKSTPDQEVRILLLGLDNGGKTTLLKQLASEDITHITPTQGFNIKSVQSQGFKLNVWDIGGQRKIRPYWRNYFENTDVLIYVIDSADRKRFEETGQELAELLDEEKLSGVPVLVFANKQDLLTAAPASEIAEGLNLHTIRDRVWQIQSCSALTGEGVQDGMNWVCKSVNAKRK | Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Required for targeting proteins to the... |
P36405 | MGLLSILRKLKSAPDQEVRILLLGLDNAGKTTLLKQLASEDISHITPTQGFNIKSVQSQGFKLNVWDIGGQRKIRPYWKNYFENTDILIYVIDSADRKRFEETGQELAELLEEEKLSCVPVLIFANKQDLLTAAPASEIAEGLNLHTIRDRVWQIQSCSALTGEGVQDGMNWVCKNVNAKKK | Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP) . Required for normal cytokinesis and cilia signaling . Requires assistance from GTPase-acti... |
Q9WUL7 | MGLLSILRKLKSAPDQEVRILLLGLDNAGKTTLLKQLASEDISHITPTQGFNIKSVQSQGFKLNVWDIGGQRKIRPYWRSYFENTDILIYVIDSADRKRFEETGQELTELLEEEKLSCVPVLIFANKQDLLTAAPASEIAEGLNLHTIRDRVWQIQSCSALTGEGVQDGMNWVCKNVNAKKK | Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP) . Required for normal cytokinesis and cilia signaling. Required for targeting proteins to th... |
P59613 | MSNKMWGGRFSERPDEIMEEINVSIDVDRHLYAQDIAASKAHAAMLATQGIITASDAKNIGKGLDTILSEIGKGGFTFKRALEDIHMNVESRLSELIGPAAGRLHTARSRNDQVATDFRLYVRDVIDETDAALAAFQQALVARALEHAGTVMPGFTHLQTAQPVTFGHHLLAYVEMAARDRGRFQDARKRLNESPLGAAALAGTSFPIDRHATAKALLFDRPMANSLDAVSDRDFVLETLSAASICAVHMSRFAEEIVIWTSPLVGLIRLSDKFTTGSSIMPQKRNPDAAELVRAKTGRVIGALNGLLIVMKGLPLAYQK... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 50418
Sequence Length: 465
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
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A6WXL6 | MSEQKSSNQMWGGRFASGPDAIMEEINASIGFDRKLYAQDIQGSLAHAAMLAKTGIIAAEDHRQIEDGLKTILKEIEDGKFTFSRKLEDIHMNIEARLADLIGPSAGRLHTARSRNDQVAVDFRLWVKQELEKTAAALKNLIEAFLERAEEHAATVMPGFTHLQTAQPVTFGHHCMAYVEMFGRDLSRVRDAIERMDESPLGAAALAGTGFPIDRHMTAKALGFREPTRNSLDSVSDRDYALEFLSLAAICAGHLSRLAEEIVIWSTPQFNFVRLSDAFSTGSSIMPQKKNPDAAELVRAKTGRINGSLVALLTIMKGLP... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 51356
Sequence Length: 466
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
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Q5ZY77 | MTNKTWGGRFKKSLDSSVNQFNASLSFDHVLFDQDINGSQVHVKQLAKQKILTEAECQEIYSALEEIRTEIKQGQYSFNERDEEDIHMFIEQLLIQKIGDLGKKLHTGRSRNDQVALDLRLYTRDKGCLINELLTRLIDCLDDLTSKHQQDLMPGYTHLQQAQPVTLGAYFNAYQCMFSRDKSRLEDWFKRMNYSPLGAGALAGSTLPLDREWVAESLGFAGIIPNTLDAVSDRDFVIELCSVAAMIMMHLSRLCEDLILWSTQEFNFVTLDDAFATGSSLMPNKKNPDVPELIRGKSGRVYGHLMAILTVMKGLPLAYN... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 46420
Sequence Length: 411
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
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Q72RA8 | MTEKEKKLWGGRFQENASSILERIGQSISFDHKLYKEDIQGSIAHARMLKQIGILNSEELSKIEIALAQIKTELEEGKFEFKSELEDIHMHIEFRLTELIGETGKKLHTARSRNDQVTQDVRLYILNQGKEILKSIINLRSSLYQKAKQSLDVIIPGYTHLQIAQPIRASQYLLSWFWALERDQEFFRFAFKASEELALGSGAMAGVNYPTDREFLKKELGLSKVSPNSMDGVSSRDHILEFLFACTQLMIHVSRICEDIILYSSQEFGILKLPDSLTTGSSIMPQKKNPDIAELIRGKSGRVIGNLNHLLVMLKGLPST... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 53352
Sequence Length: 470
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
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Q2NQZ1 | MALWGGRFSQAADQRFKSFNDSLRFDYRLTEQDIVGSVAWSRALVTVGVLSETEQQQLEDALNVTLEEVRTAPEAILASDAEDIHSWVEQCLIDKVGDLGKKLHTGRSRNDQVATDLKLWCRAQVTELLGAIHLLQQALVMTAEAHQDVVMPGYTHLQRAQPITFAHWCLAYSEMLARDESRLRDTLTRLDVSPLGAGALAGTAYAIDRDKLAGWLGFASATRNSLDSVSDRDHVLELLSYAAIGMVHLSRFAEDLIFFNTGEAGFIELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 50152
Sequence Length: 457
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
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Q024T3 | MKLWGGRFESGPGEVFERFSGSLDFDRRLIDCDIRGSQAFARALENVGILTATERAQIVEAFDSIRAESLSPAFYEGATDEDVHTLVIRKLKERAGAVADKIHTGRSRNEQVSLDTRMWLREESTDLQAQLFAVMGRLLDLAEMYPHAIIPGYTHMRRAQAVLWPHYLLAYFEMFLRDWHRFGDARRRANVLPLGSGALAGSGFPLDREAMAQNLGFEGITQNSMDVSGDRDFALDFLYACTVTMIHLSRLAEDWILYSSEEFGWLELGDGVTSGSSLMPQKKNPDSLELIRGKSGRVVGCLTSLLVTMKGLPMTYNRDM... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 50724
Sequence Length: 460
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
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A9FJ48 | MSVRLWDKGGATDAQMLRYTSRDDWQLDQRLLAYDLRATIAHVRGLARIGVLSEAERDALVRELEVLSAQNEAGELRLTEDDEDGHSAIEAALVARIGDAGKKVHTGRSRNDQVLVATRLYERDALDELAENAAAGARALLDLARREAETPMPGYTHLQRAVPSSVGYWAASFVEGLADAIDVVRATRALVDRCPLGGAAGFGVNLPLDRVGVARELGFAGVALNPLASQTSRGIIEAQILAAAWQVMAVSRRLAWDLSLFAMSELAFIRLPEAFTTGSSIMPQKRNPDVVELMRAACSVVQGALAEVQSIVALPSGYHR... | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 46412
Sequence Length: 430
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
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A0A2H3CNY6 | MDSASLAVVVWAILLVLWLRRIFGQRSSLPLPPAPPGYPVIGNLLDLANNDVHIRARHWSRNFDDDVISLKVLGKTMIILNSPTAVSDLFDKRASNYSDRPDMPMIVDFIGWDWTFALMRYGPRWKEHRRVFNNHFNIGTSGASEDRHIQLRICRELLSLMFQSPSKYLENLRHYTGHIILKRTYGHTVVDEEDPYIRLVEAASQSTSEAAVPGAFLVDLFPSMKYIPEWFPGAQFKRKAREWRKLSEAMINAPYDMAKGKFDEGNAEACFVSACLEQNKTASGQGLSEELIKDTAAVAYAAGADTSVSTLTTFILAMTL... | Function: Cytochrome P450 monooxygenase, part of the gene cluster that mediates the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols (Probable). The first step in melleolides biosynthesis is p... |
A0A2H3CSA7 | MTHASSAWFLAAVVIVTFIVVRHIRSSWRKLPPGPRGFPIVGNLLQLRNKQWLTFTELGKKYGDLMYFNVAGQPLIVINSLKVATDLLDRAKFSDRPRNIVASDIMTGGMFVAFAPYGNAWRHMRKAAHEGLNKNIVNQYHPIQIKEAVLLANDLLAEPNRWVSHVRRTAASTIMSIIYDKPPTSEQDPSIKRINDFATRLTRAAMPGAHFVESFPWMLRIPSKYAKWKRDAEGWYAKDSSMFESLFHSVKDRVAEGSNHPSFAATLIQGAGRHGLTDHENSWLAGAMYTAGAESSSAAMSWWMLAMILYPDAQKRAQAE... | Function: Cytochrome P450 monooxygenase, part of the gene cluster that mediates the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols (Probable). The first step in melleolides biosynthesis is p... |
A0A2H3CZX2 | MTRILSEEVSPIWILTAIVVVAYTTVRYLRSPWRNLPPGPRGLPLIGNLLELRGKQWLTFTELGKKYGDLMYFNVAGQPLVVLNSQKVAADLLDRRAGKYSDRPRNIVASDIMTGGNLVVFTRYGDVWRRMRKAAHEGLNKGVVYKYHPIQTAEAVLLTAGVLAEPEKWNSHIRRTAASAIMSMVYDTPPTSEQDPSVKNINDFVARLTRAAMPGAHFVEFFPWMRYIPSKYAKWKREAEESYTKDSAMFEGLFNGVKDRVAKGDERPSLASTLIQDAGRHDLTDRENSWLAGTMYAAGAETTSGVMSWWTLAMIVYPET... | Function: Cytochrome P450 monooxygenase, part of the gene cluster that mediates the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols (Probable). The first step in melleolides biosynthesis is p... |
A0A2H3CNS9 | MALFSAYALAFSLLMIPLILYILRIGRRESGLPPGPSTLPLVGNLHQLPHGGLHLQFTAWAKEFGGIFSLKFGPGTVIVATSPRAVRELIDQKSASTSDRPPSHFSNVITGGNNIGFARYSDYWRRGRRVMHSMLTKKACVNHLTIQRAEASQLMYDYLVEPKEFVAHGQRYANSVITSILAGTRSPHHTSPLVTAFFQMQHEWTHLLTPGAHPPVDMVPFLKYIPGSWKQICAKMKVSQEELYGGMIDACAKRVERGIRNGCFLEGELENKDVDRGLLRGMCSALMEGGSDSTSIYLQSFILMLVAHPEVQAKARAEID... | Function: Cytochrome P450 monooxygenase, part of the gene cluster that mediates the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols (Probable). The first step in melleolides biosynthesis is p... |
Q9H993 | MAVVPASLSGQDVGSFAYLTIKDRIPQILTKVIDTLHRHKSEFFEKHGEEGVEAEKKAISLLSKLRNELQTDKPFIPLVEKFVDTDIWNQYLEYQQSLLNESDGKSRWFYSPWLLVECYMYRRIHEAIIQSPPIDYFDVFKESKEQNFYGSQESIIALCTHLQQLIRTIEDLDENQLKDEFFKLLQISLWGNKCDLSLSGGESSSQNTNVLNSLEDLKPFILLNDMEHLWSLLSNCKKTREKASATRVYIVLDNSGFELVTDLILADFLLSSELATEVHFYGKTIPWFVSDTTIHDFNWLIEQVKHSNHKWMSKCGADWE... | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-... |
Q8MMH3 | MWSPLILPLLAQIFACAFGDAVNEGCNVDPKGIHGLWYLDEPFGVYLSAIYNGSLAYIMMKERVPAIVTTVINSLEQDNDEIVQKYGVESQEELHRIVDSLKSLKTELSTNQPLTNLPLAHDEADRDAAVWNEHLDRQREIEGPNLSYFFTRFLLAESYTFRKMAHAFALAKNVRNFDFFGKQKEHLLTNSAKSLPILAHRALLEANRSKATKDEMREELAKFLKLSLWGNRFDLAASSGHEITQAGDPIELLSSFDEDLLIDHTRVAWDILNKPHGPNDPVIVDIVLDNAGYELFNDLCLATFLVSRGLATKVRFHAKQ... | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-... |
Q6AYT5 | MAESPAFLSAQDVGSFAYLTIKDRTPQILTKVIDTLHRHKSEFFEKHGEEGVEAEKKAISLLSKLRNELQTDKPIIPLVDKCVDTDIWNQYLEYQRSLLNEGDGEPRWFFSPWLFVECYMYRRIHEAIMQSPPIHDFDVFKESKDENFFESQDSINALCTHLLQLKPITDLGEKQIQDEFFKLLQISLWGNKCDLSLSGGESSSQKADIINSLKDLKPFILVNETESLWALLSKLKKTAEPPAVRVDIVLDNSGFELVTDLVFADFLLSSELATEIHFHGKIIPWFVSDVTVRDFEWIVEHMKGSHLESMSACGAAWEAY... | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-... |
Q6DJA3 | MDPPCSLSARFEGSFAYLTIRDRLPQILTKVIDTVHRNKNKFFEDNGEEGVEAEKKALSFFSKLRNEIQTDKPVLPLTDNQSDTELWNQYLDYQKTLLNKGETPSWFKSPWLYVECYMYRRIQEGLVLSPPISEYDVFREGKTESFFQSQPAIIALCTYLQELKNNVANLSENQKKEELSKLLQVCLWGNKCDLSISGGLDNSQKFSILSSLESFMPFILVNDMESVWAVLSGSKNLESGKELMKRVDIVLDNAGFELITDFVLADALLSLRLASEVHFHAKCMPWFVSDTTKHDFNWTIKHLQAANHKWMSKCGVNWKE... | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-... |
Q04371 | MTIPGRFMTIDKGTFGEYTASTRWPIIIQNAIDDLSKHQETEKSNGTKFEQGEVIKKELKEFRQEIIDRVPLRPFTEEEIKIANVPLSFNEYLKKHPEVNWGAVEWLFSEVYLYRRVNVLFQRQCEWAKFDIFNRLKQSTFESSFYGVVELALRYENLLPQLREMKQNPGNEIDDILKVLFKEFIEISLWGNATDLSLLTNATLEDIKSIQGAKARAASESKIVVNDTEKAWEVLTKARADANSREIRVDFVLDNSGFELYADLMLAAFLLQSGLATKCIFHAKDIPYMVSDVMLKDFDILVHDLRDREFFPSGEPSTKE... | Cofactor: Phosphatase activity is strongly promoted by several divalent cations but it is suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases.
Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, inclu... |
Q9P291 | MGRTREAGCVAAGVVIGAGACYCVYRLAWGRDENEKIWDEDEESTDTSEIGVETVKGAKTNAGAGSGAKLQGDSEVKPEVSLGLEDCPGVKEKAHSGSHSGGGLEAKAKALFNTLKEQASAKAGKGARVGTISGNRTLAPSLPCPGGRGGGCHPTRSGSRAGGRASGKSKGKARSKSTRAPATTWPVRRGKFNFPYKIDDILSAPDLQKVLNILERTNDPFIQEVALVTLGNNAAYSFNQNAIRELGGVPIIAKLIKTKDPIIREKTYNALNNLSVNAENQGKIKTYISQVCDDTMVCRLDSAVQMAGLRLLTNMTVTNH... | Function: Regulates mitochondrial transport during axon regeneration. Increases the proportion of motile mitochondria by recruiting stationary mitochondria into the motile pool. Enhances mitochondria movement and neurite growth in both adult axons and embryonic neurons. Promotes neuronal survival and axon regeneration ... |
Q9CX83 | MGRTREAGCVAAGMVIGAGACYCVYRLTWGKDENEKLWDEEEEEEEEEEEKSCSDKTEKELKTNVGVGARGKPQDDSKSKVEVNVGPENGPGVKKEVHPESQSGGGLEAKAKALFKTLKEQARAKAGRGIRLPNISRNRTLTSSLPCPGGRGGGCHPGRTGSRARNRTSGKVKRKNRSKSNKAPATAWPVRKGKFSFPYKIDDILSAPDLQKVLNILERTNDPFTQEVALVTLGNNAAYSFNQNAIRELGGVPIIAKLIKTRDPIIREKTYNALNNLSVNSENQGKIKTYISQVCDDTMVCRLDSAVQMAGLRLLTNMTV... | Function: Regulates mitochondrial transport during axon regeneration. Increases the proportion of motile mitochondria by recruiting stationary mitochondria into the motile pool. Enhances mitochondria movement and neurite growth in both adult axons and embryonic neurons. Promotes neuronal survival and axon regeneration ... |
Q7L311 | MSRVRDAGCVAAGIVIGAGAWYCVYKYTRGRDQTKKRMAKPKNRAVAGTGARARAGLRAGFTIDLGSGFSPPTPVRAEAEDRAQDEASALDTVGAEAVAPAASSAEAQSGAGSQAQEADGAGVGPKAESVVGAAMASAIAPPPGVTEALGAAEAPAMAGAPKVAEAPREAETSRAAVPPGTVVPTEAAAPTEVTEGPGVAAPTKVAEAPGVASPTEAAEAPVPATPTGAAAPTGAAESPGTSGSPRTAVVPGTSAAKKATPGAHTGAIPKATSATGAVPKGGGKGVTRSRNGGKGKGKKSKVEVDELGMGFRPGDGAAAA... | Function: May regulate the dynamics and distribution of mitochondria in neural cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65683
Sequence Length: 632
Subcellular Location: Mitochondrion
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Q2NWA9 | MERGAGLWLGLLAVFFVLTYLVPLEGRLLWQPDETRYAEISREMLASGDWMVPHLLGLRYFEKPLAGYWMNNIGQWLFGSTNFAVRFASVFSTGLSALLVFTVSWTVGRQLRQSLLAALIFLSLLLVFGVGTYSVLDPMIALWLNAAMAAHVFALRADRRTTRGVAWLLLGLACGLGFMTKGFLALVVPAIAVLPVALYYRQLKATLGYGALAALLAVLVNLPWALALSRLEPDFWHYFFWVEHIQRFAAENAQHRAPFWFYLPVLALGSLPWLGLLPGAMAAGWRARRVQPERFLLLCWVVMPLLFFSVAKGKLLTYIL... | Function: Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
Catalytic Activity: 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,o... |
B4ETL9 | MLNNRASKIGAILLALFFVLTYLFPLNSRLLWQPDETRYAEISREMVVSGNWIVPHMLDIRYFEKPIAGYWINNISQLIFGHTNFAVRFGSVISILLSALLIYLLARMMWRNRQVAFVASLIYLSMFLVFSVGTYSVLDPMLALWVTASMVCCFWALKATTAKTRILAWITLGLACGMAFMTKGFLALAIPVIVMIPVTLYQKQFTRMLLYGVLAVLSAALISLPWVLAVAKAEPDYWHYFFWVEHIQRFSGDDAQHSSPFWYYIPIILLGVIPWLGLLPGALTSAWKKRRKRPELFFLLCWFVVPFLFFSIAKGKLPTY... | Function: Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
Catalytic Activity: 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,o... |
A0KGY4 | MTLTKWALPLFFLFFYLLPLDQRPLWSPDENRYAEISREMVSTGDWVVPHFLGLRYFEKPIAGYWFNSISQQLFGDTNFAVRFASAAATGLSALLIFWFALQLWQCRRKAFLASLIYLSLLIVYGIGTYSVLDAMVTLWLNAAMVSFYIIRKEGSLGSRIGGYLLFGLACGMGFLTKGFIALAVPVVVIVPYVIYQRRLLELVRFGPLAILSAVLLAAPWAIAVHLREPDYWHYFFWVEHIQRFAADNAQHKAPFWYYLPMGLLGTLPWLGLLPGALRKGWQERKISPETLYLLAWVILPLLFFSIAKGKLLTYILPCFA... | Function: Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
Catalytic Activity: 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,o... |
P12421 | MSGLAYLDLPAARLARGEVALPGSKSISNRVLLLAALAEGSTEITGLLDSDDTRVMLAALRQLGVSVGEVADGCVTIEGVARFPTEQAELFLGNAGTAFRPLTAALALMGGDYRLSGVPRMHERPIGDLVDALRQFGAGIEYLGQAGYPPLRIGGGSIRVDGPVRVEGSVSSQFLTALLMAAPVLARRSGQDITIEVVGELISKPYIEITLNLMARFGVSVRRDGWRAFTIARDAVYRGPGRMAIEGDASTASYFLALGAIGGGPVRVTGVGEDSIQGDVAFAATLAAMGADVRYGPGWIETRGVRVAEGGRLKAFDADF... | 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 + phosphat... |
Q89WF2 | MPVTGRGPCGTCAPALRSTSKDTILTHSDQPRPLQSRANGPLTGKVRVPGDKSISHRALILGALAVGETRISGLLEGEDVLNTAKSMQALGASVERTGDFAWKVQGVGVAGFAQPKAALDFGNSGTGCRLVMGAVAGCPISAVFDGDASLRSRPMRRILDPLEKMGARVVSGGEGGRLPLTLQGARDPLPITYKTPVASAQIKSAVLLAGLAAPGTTTVIESEASRDHTELMLKHFGADITSTKEGQHGRRITLVGQPELHGANVVVPADPSSAAFPVVAALIAEGSDVVLSDVMTNPLRTGLFTTLREMGASIEESEVR... | 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 + phosphat... |
C0QZK3 | MTLTIKPSEIFGSIYIQMSKSDAHRALIASSLAKTPSIIKRWIDNVSVDVEVTKNAVSNFADLEIIDDNLKVFPKKEYKKELVIDVKESGSSLRFLIPIMSAFGITCTFTGSKKLFSRPIDVYKKIWKEEGLEFIHSEDSIKISGQLKASNFKVLGNLSSQFLSGLLFALPLLDGNSNIIIDGELESEPYVMMTLKTLKAANIETLRHDNNIIEVYGNQEYSGIDYEVESDWSHAAFFAAAGALGGETTLYGLNKYSIQGDKEILNILKFMGASVSYNDDNSITIKKTNRLNALDIDMSDIPDLGPIITTLAATAKGRTR... | 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 + phosphat... |
B1GYQ3 | MEIKLKKTNYVSGVIEVPSDKSITHRAVMLSSLAEGNSIVRDYLPSDDCNRTIEAFRQMGVEIKIDNGSLYVKGAGLKLAKPQNGKYNIYAGNSGTTTRLLSGILAGQDFETVITGDDSLSKRPMRRVILPLSQMGANIKSNDGLLPLIIKGRNPLKELNYESDKSTAQVKSAILFAGLFADGATTYKEPVKSRDHSERMLKAFGVNIKVNGNFVTVYPAEKLIAQDITVPGDISSAAFFIAAALIVPDSNLTIRNVGVNPTRDGLIEVLKQMGADITLANMREISQEPVCDIVVKYSKLKAADIDASLVPRMVDEIPVF... | 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 + phosphat... |
Q749Y6 | MVSLSSHPARALRGEIAVPGDKSISHRSIMLGSIARGVTTVSGFLRGEDNIATLDAFRAMGVQVHDDGETLRIEGKGLHGLTEAEDVIDCGNSGTSIRLLTGLMAAQRFYTVLTGDRYLRRRPMRRVVEPLSRMGACIHGRDNGEKAPLAIVGRPLTGIAYDSPVASAQVKSALMLAGLYADGATRVTEPHLSRDHSERMFRHFGARLETDAAGVTVYGGHELDGRDIVVPGDISSAAFFLVAALIVPGSELLIRGVGVNPTRTGILDILAAMGGSVELLDQREVSGEPVADLLVRSSALKGIEIGGDVVPRAIDEFPVI... | 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 + phosphat... |
Q7NLT3 | MGQAFSITPARRLSGEIAVAGDKSISHRALMLAALAEGESVIEGLLPGDDPRSTAACLRALGAEISGIDGPSVRVRGVGLGRLHEPADVLDMGNSGTTMRLMLGVLAGQPGLFCTLTGDRSLRSRPMLRVVSPLRQMGARIWGREEGGRAPLAVWGEQLRAIDFVSPVASAQVKSAVLLAGLLAEGLTSVSEPVRSRDHSERMLRAFGAEVLVDGTTAAVRGPARLRAQSLRVPGDISSAAFWLVAGSIVPDSQLLLSGVGVNPTRTGVLDALAAMGADIAVENRREVCGEPVADLRVRSAPLKACTIGGEWIPRLVDEI... | 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 + phosphat... |
Q5FTC0 | MQVSRPLTVSASPKGLSGRTRVPGDKSISHRSLMFAALASGRTYVTGLLEGEDVLRTADAMRALGATITREGADWVIEGRGVGALTEPADVLDMGNSGTAARLLSGILSSHAFNSIMTGDASLRSRPMRRVTVPLAANGSEFLTREGGRLPMAIRGTGEAKPIEYRLPVASAQVKSAILLAGLNAHGTTVVEEPVATRDHTENMLRHFGVEVDVSRIDAGGRRIALTGPVQMTARDVTVPGDPSSAAFPIVAALLVPGSDIWIEGVGLNPLRTGLFTTLIEMGASLSIENERVEGGEPVGDLHVRYSKLKGVDVPPERAP... | 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 + phosphat... |
A4FNI0 | MTQFWPAPAASGAVRATVPVPGSKSITNRALVLAALAEGPSTLRGPLRSRDTELMATALRALGADLQDGPEGSWQVAPGPLRGPAEVDCGLAGTVMRFLPPVAALAEGRITFDGDPRARERPLDAVLNALRALGADISGDSLPFELQGTGKLAGGAVTIDASASSQFVSGLLLSAPRFEQGVTVTHTGEPVPSLPHIDMTVSMLRAAGVEVDDSKRDVWHVAPGPIRALDLDVEPDLSNATPFLAAAAVTGGTVTVPGWPERTDQAGDAIRDILARMGATVELGPDGLTVTGPAELAPLDIDLHDVGELTPTVAALAAFA... | 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 + phosphat... |
Q980I5 | MIVKIYPSKISGIIKAPQSKSLAIRLIFLSLFTRVYLHNLVLSEDVIDAIKSVRALGVKVKNNSEFIPPEKLEIKERFIKLKGSATTLRMLIPILAAIGGEVTIDADESLRRRPLNRIVQALSNYGISFSSYSLPLTITGKLSSNEIKISGDESSQYISGLIYALHILNGGSIEILPPISSKSYILLTIDLFKRFGSDVKFYGSKIHVNPNNLVEFQGEVAGDYGLASFYALSALVSGGGITITNLWEPKEYFGDHSIVKIFSEMGASSEYKDGRWFVKAKDKYSPIKIDIDDAPDLAMTIAGLSAIAEGTSEIIGIERL... | 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 + phosphat... |
Q2S4R9 | MVQTIDQAASLRGTVSLPADKSISHRSALLSALGTGRSRVYNFPDSADPQSTLDCVRTLGIEAGRNDEGVLAIHGRGLGGLHPPSEPLDCGNSGTTMRLLSGMMAGQEFGSVLTGDESLQQRPMERIADPLQAMGARIDLRSGHAPIRIRPQRSDGLRPLEYRLPVASAQVKSCVLLAGLYASGRTVVIETTPSRDHTERMLGLEVQEVGGERHIIVEEDHTVPAVDWSVPGDFSGAAFFLVAGTLVPDSELHLDDVGLNPSRTALLDVLDGMGADITVENERVQGSEPVGDITVRSASLSGIDIGGRLIPNLIDEIPVI... | 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 + phosphat... |
A3DDJ2 | MIKLNVNLQDRSYPIYISTDYSQIGKCIQSAKLTGKMVLITDTNVDKYQAEECVKAFSDAGYEVSKFVIPAGEENKNLDTTRDIYKYLLGLKLDRSATLMALGGGVVGDITGFAAATFLRGINFVQIPTTLLAQSDSSVGGKVGVDFEGTKNIIGAFYQPKFVYINVNTLKTLPERELKAGLAEVVKHGVIMDEEFYEYIDYNVHKILNHDEAVLQYIAKRNCSIKASVVEKDEKEGGLRAILNFGHTIGHAIETVMNFELLHGECVSLGMVGAMRMALYLEMIDEQSVNRVKNTLDKIGLPTRLEGIDVDKVYNQMFYD... | 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): 4... |
Q6F7E5 | MQTLHVELGDRRYPIFIGSQLNPQNLLAPYIKGRQVMIVTNTTLEQLYLQHYQDALHALDKQVAVCVLPDGEKYKNIEHLNLIFDALLKAGFNRDCTVLALGGGVIGDMAGFAAASFQRGVYFVQIPTTLLSQVDSSVGGKTGINHPLGKNMIGAFKQPEVVMADMSQLKTLPPRELSAGLAEVIKYALLGDIEFLGWLETHMDGLIAGDETLLAEAVYRSCAHKARIVANDEKEQGERALLNLGHTFGHAIESYLGYGEWLHGEAVATGMVMAADLSHRLGWISSGDLERTKKIIQRANLPISCPPIPLDEFLSYMSHD... | 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): 3... |
C1F548 | MRTIQVTTPGVQYPVYLGSGLLPQVASRLRKLTAPNSRIFIVTSPEIWALWGKKLLSGFGKSSPEVLFLPAGEAHKRMASVEKLATALSESGADRSSLLIAFGGGILGDLTGFLAAIYMRGIDYVQIPTTLLAQVDSSVGGKTGANLSTGKNLIGSFHHPRAVFADVDVLHTLPPRELRAGLQECVKAGIIRDAALFSYMERNAETILAADDAALTRVIAAAVRMKADVVQQDEREGGLRMILNYGHTLGHAIETVTHYRGLLHGEAVGWGMLAATELSRMRGLLTAAQSERMQRVILAYGPLPRFRAKAEALLEATARD... | 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): 4... |
Q88XU0 | MTNIEVKTRVKQYQIKIMINSLHHLGTLVTKVWCARQVAVVTDTNVGPYYAKLVTDELTAAGFKVRVMTVPAGEESKSWSQVQSLIDQLSAAHFSRSDGVLALGGGVVGDLAGFVASIYMRGIALIQVPTSLLAQVDSSVGGKTAIDLPTGKNLVGSFYQPDLVVIDPAILVTLPPRMLAEGYGEIVKCAALVGGDFWQSLHQITSVAAILPAAPDLIAASVAFKARVVMADEHEQGQRQLLNFGHTIGHAVELLADGQLMHGEAVAIGLVQVCRLFAAHGLAPTSLTSTLKARLMAVGLPTELPPIAPQAVAAVMQHDK... | 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): 3... |
Q38X86 | MPTISVNLTTQKYQIKIENGLATSIGREVQRVWSVRKIALVTDTIVGPLYQAQITEQLTQAGFQVTVLTIPAGESAKSLEQAMSLYEALLTANFNRSDGLIALGGGVVGDLTGFVASTYMRGLPFIQIPTSLLAQVDSSVGGKTAVDLPAGKNLVGTFYQPELVLIDPQMLETLPQRQLVTGYAEVVKIAALVGADFWNLVQQIESPTAILDKAPELIARSIAYKAQIVMADVQESGQRRLLNFGHTIGHAVESLADGELTHGEAVSIGLIAISRLFEQPTQIAAQLQTVLERVGLPVTHPLLQSPALFEKIAHDKKNQG... | 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): 3... |
Q5ZX00 | MAKFELYAEVDVSISGHQYPIIICRNGLIDPELINRFITSKQVLIVTNRTVAPLYLGHLQSVLPSKQCDVVILEDGEEHKNQRSLFTIYDSLIQNKHHRDTSIIALGGGVIGDMAGFAASTYQRGVRFIQLPTTLLAQVDASVGGKTAINHPAGKNMIGSFYQPQAVIIDLNTLKTLPEREFRAGIAEMIKYALLVGGSFFERIQEALQQGLTVHSPELPLLIAECCQVKAKIVEQDERESGLRALLNLGHTFAHALETYTDYKKWLHGEAVAIGLYCAAVLSEKKGLLDKPIVDQVEKMLIHAGLPHKIPNSIDLIQLR... | 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): 4... |
Q75FW3 | MSLIETVPVNTEHKSVPVHLHSNLSGLSEEIAKLPGVTSVFLITEKSIHSIYSKYLERELSSLPIKTIYIKGGEKSKHINRTGEVYNQLIEYGADRKSLILAFGGGVVGDFAGFIASTYLRGIRFVQIPTTLLACVDSSVGGKVAVNADFGKNMIGSFYQPEFVFAPLSVLSTLPDREWKCGQAEIIKHSLLSGGEYWEKVKTHSFKDLNVDSTILPYLIAESVRFKANVVSSDEKETGLRKILNLGHTTAHAIESVTKYKKYSHGEAVAIGLVTALLLSEQHSELDPVTTKETIESLKNYGLPFQTKLKSKQLAKHMLH... | 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): 3... |
B1MYC9 | MTVITVSLEKKQYQVKIDRRLHQEIGQAVSLVWTPRRIALLTDSHVGPLYLTAVQQQLEMSGFEVLPLQVPAGESSKSLKTVGELIGKMAEKGFTRDDGLIALGGGVIGDLGGVVASLYMRGIALIQIATSLTAQVDSSVGGKTAINLSHTKNIAGTFYQPDLVLVDPTYLDTLADRDLVEGYAEVVKTSVLAGGSFFDLTGRIYGVTDIRDNAEELSTRAVAYKAQVVMADEKEAGQRQFLNFGHTIGHAIELLAHGELRHGEAVAIGMIAMSSRMTRDGLTPASLTAALRARLETVDLPTTSDLIGTPAFFKHMVNDK... | 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): 3... |
Q8Y5X6 | MPEITVRAKSKTYPVYINEFALEDIREKWTKSLAKFSHVFVLTDGHVAELHKAKLDAVLADLPVVTYYVAPNGEEAKTFRVYEDVMTKMIETGLDRKAVLIAFGGGVIGDLGGFVAATYMRGIPFYQVPTTVLAHDSAVGGKVAINHPLGKNMIGNFYQPEAVIYDTQFFATLPERELRSGFAEMIKHALISDLTLLRALMDTFTEPKDFYTKDLTPFLQRGIEIKANIVAQDETEQGVRAYLNFGHTFGHALEAYGNFGKWLHGEAITYGMIYALTMSETIYGLDFDLAEFKTWLEQLGYDTTFDASVPFSKILENMRH... | 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): 4... |
Q67N10 | MELGEERYPIYVGAGLMAQLGALVRRHLPETRRALLVTDANVAPLYGEAARAALEQAGITTARVTVPAGEASKSLSQAYSLYSSCVRAELDRTSAVVALGGGVVGDLAGFVAATYLRGIPLVQVPTTLLAQVDSSIGGKTGVDLPQGKNLVGAFHQPSLVVADVETLKSLPRRELSAGMAEVVKHGVIRDEEFLKYVEVQVGNVLAGDPAVLERVVAESCRIKAEVVAADPREKGLRAILNFGHTVGHALEAAIGFRWLHGECVAVGMVAAAHIARHSGIAQEGRLELRLTRLLERLDLPTTLPEGMDPKDLEPFLRRDK... | 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): 3... |
Q3A2N6 | MKLKRMVVGLGERSYPIWIGGGIFSRLPEALQEVNFPKKIAVVSNPLVQSLYGQALADALQSSGYDHHFISIPDGEEHKNWTTLQTIYDGLIAKGFDRHCGLIALGGGVTGDMGGFAAATFLRGIPYIQVPTTLLAQVDSSVGGKTAINHPQGKNLIGAFYQPRHVHIDVDTLQSLDAREFATGMAEVIKYGIIKDKAFFDWLYTHREALQRRDTEALISAVKRACQIKANIVEVDEKEQALRAILNFGHTFGHAIENLSGYQTYRHGEAVAIGMMVAAHVSRRMDLCTADEVGAIERLLQVFDLPVTPPDYSLEAYLEA... | 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): 3... |
P56122 | MNTLGRFLRLTTFGESHGDVIGGVLDGMPSGIKIDYALLENEMKRRQGGRNVFITPRKEDDKVEITSGVFEDFSTGTPIGFLIHNQRARSKDYDNIKNLFRPSHADFTYFHKYGIRDFRGGGRSSARESAIRVAAGAFAKMLLREIGIVCESGIIEIGGIKAKNYDFNHALKSEIFALDEEQEEAQKTAIQNAIKNHDSIGGVALIRARSIKTNQKLPIGLGQGLYAKLDAKIAEAMMGLNGVKAVEIGKGVESSLLKGSEYNDLMDQKGFLSNRSGGVLGGMSNGEEIIVRVHFKPTPSIFQPQRTIDINGNECECLLK... | 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... |
Q0I3U1 | MAGNSIGQLFRVTTFGESHGIALGCIVDGMPPGLALSEDDIQPDLDRRKPGTSKYTTPRREEDKVQILSGVFDGKTTGTSIGMIIKNTDQRSQDYGEIKDRFRPGHADFTYQQKYGLRDYRGGGRSSARETVMRVAAGAIAKKYLREYFGIEVRGYLSQIGEIKIDPQVVADVSKIDWAKVNSNPFFCPDESAVEKFDELIRELKKAGNSIGAKLTIVAEHVPVGLGEPVFDRLDADLAHALMGINAVKAVEIGDGFAVVEQKGTEHRDEMTPEGFCSNHAGGILGGISSGQPIIATIALKPTSSITVVGRSVNLNNEPV... | 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... |
A8A9W1 | MGGNTIGKMFSVTTWGESHGKAIGAVIDGCPAGLPLSEEDLLVELSLRRPGRRFTTPRREPDVPEILSGVFNGKTTGMPISIIIRNRDVISSYYEKIKETPRPGHADLAYIKKYGYEHWDYRGGGRASGRETAARVAAGAVAKKLLGCLGVVVSGYVVELGGVEFPSAEDAEESLRSRLSPFRVLCCEEKAEEVLKEALERRDSVGGVVEAVAWNAPAGLGEPVFDKLKADLAKAMMSIPASVGFEVGWGFKLARLRGSEARDKIVSSAGEATVEGDKAGGMLGGISVGAPIRIRVAFKPTSSIMIPEKTVNIHTLEETE... | 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... |
Q5KWX7 | MEKVYGLIGFPVEHSLSPLMHNDAFARLGIPARYHLFSVEPGQVGAAIAGVRALGIAGVNVTIPHKLAVIPFLDEVDEHARRIGAVNTIINNDGRLVGYNTDGLGYVQALEEEMNITLDGKRILVIGAGGGARGIYFSLLSTAAERIDMANRTVEKAERLVREGDERRSAYFSLAEAETRLAEYDIIINTTSVGMHPRVEVQPLSLERLRPGVIVSDIIYNPLETKWLKEAKARGARVQNGVGMLVYQGALAFEKWTGQWPDVNRMKQLVIEALRR | 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): 30427
S... |
Q74D29 | MPFTGATRVLGIIGQPVSHSLSPLMQNAALQAMGLDYAYVPFAVEEDCLADAVRGLAALGVVGFNVTIPHKSAILPLLDRLSPEAELIGAANVVKREGSDLVGYNTDGTGFIQSLSEDLGFTPAGCRILVMGAGGAARAAVASLAGAGAASVVIANRSIARGEELSAAFRRHFIGTQFAAIPLDPENLNRCVQNFDLLVNTSSVGMGGTAFPGMDLSRMGPHGAVYDMVYVPAVTPLLAEAERCGIRYANGIGMLAAQGECALELWTGVRPPEGLMKACLMAALMS | 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): 29606
S... |
Q5FPK1 | MIDGHTKLAGVMGWPVEHSRSPLMHNHWCRVNGVNGAYVPLPTHPHGFDQALRGLAAAGFQGVNVTIPHKEAAMLACDELTPTAKRAGAVNTICFVAGRIIGDCTDGTGFCDNLSAHDVAIAGRAMVLGAGGAARAVAAALLDRGCEVVIANRTLERAEALVEALGGGEAVAWYEWPSLLSGCSLLVNATSMGMGGKAGLDWDAALREAAPGLCVTDIVYTPRETPLLLAAQARGLRTVDGLGMLVHQARAGFRAWFGVDPQADRTTFDLLAASLRTDA | 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): 29117
S... |
P43876 | MDLYAVWGNPIAQSKSPLIQNKLAAQTHQTMEYIAKLGDLDAFEQQLLAFFEEGAKGCNITSPFKERAYQLADEYSQRAKLAEACNTLKKLDDGKLYADNTDGIGLVTDLQRLNWLRPNQHVLILGAGGATKGVLLPLLQAQQNIVLANRTFSKTKELAERFQPYGNIQAVSMDSIPLQTYDLVINATSAGLSGGTASVDAEILKLGSAFYDMQYAKGTDTPFIALCKSLGLTNVSDGFGMLVAQAAHSFHLWRGVMPDFVSVYEQLKKAML | 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): 29760
S... |
Q5V450 | MDVYGLIGNPVGHSLSPPMHEAGYEALGLDARYVTFEPPADAGAEAIEAAETLGVDGLNVTIPFKQDVLDAVDPAPLAERIGAVNTVDFTGGTPTGYNTDAVGAVRALDHHDVSLSGTAVVVGAGGAGRAVAFGLADEGLSVRIANRTESKADALADEVPDASGHGLDSLSDLLANADILVNCTSVGMEEDKTPVPADALHSDLAVLDAVYTPIETRLLQDAAAAGATTVDGAWMLLYQGVEAFERWTGEDAPVDRMNGRLREHL | 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): 27384
S... |
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