ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A9HKR8 | MSESQSEFPGGGTTGDIVRTMQEAQERAAVLAQALPFLRRYAGDTIVVKYGGHAMVDDSLSNAFGHDIALLKLVGVNPVIVHGGGPQISAMLTRLQIPSTFVDGLRVTDAAMVDVIEMVLAGKVNKQVAGLINQAGALAVGISGKDGGLITARRLQRTTRDASGQERALDLGFVGEPTHIDPRVLYALSGSGLIPVVAPVGIGEAGETYNINADTAAGAIAGAVHATRLLMLTDVPGVLDETGALIPELTAEEARRGIASGMISGGMIPKVETCLEAVRSGARAAVILDGRVPHACLLELFTEAGPGTLIRGE | 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): 32287
Sequence Length: 313
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
|
Q6B8Z0 | MLNNFERVQILSDALPFVQRFHGRTLVVKYGGSAMKNVYLKSKIIEDILFLSYIGIKVVIVHGGGPMINHWLKQVNIQPKFFNGIRVTDKDTMELVEMVLVGKVNKDLVTLLNRSSNLAVGLSGKDANLVVASSFFPDQKDNYTGKVQQVNIEIVNLLLSSGYIPVVASVASDLNGQAYNINADSVAGAIAECLNAEKLILLTDTPGIMSDINDPSSLIKYLNISQLEELKSQKIILGGMIPKVDCCIKALQGNVSSAHIIDGSVEHALLLEILTSAGIGSMLVL | 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): 30879
Sequence Length: 285
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Plastid
EC: 2.7.2.8
|
Q7VMS6 | MNQTTTFDKLCNYSAACLANWQGKTIVVKYGGNAMISAELKQTVMQNILLLNQYGINVVLVHGGGPEISLGMKLLGKEPQFINGLRVTDQDTIDVVLQMLAGKVNKRLVALLKGKGIGLCGIDGGLIQCEKLEAELDYGLVGNIVQVDITVLQMALAANLIPVIAAVAVDQQGIIYNVNADTVASEIAVALGADKLVLMTDIAGLLADRNDERSLMSRVEVSQVETLIAQGIISDGMIPKVASCTRFINAGGIEAHIIDGRIKHAILLSILSDKQNGTRFYKEK | 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): 30388
Sequence Length: 284
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
|
Q9K8V4 | MGDIVVIKCGGSVLDSLSDSFFTSVRRLQAEGAKPIIVHGGGPAINGMLAKLEVETTFVDGLRKTTDSVLSVAEMVLCGQTNKKVVRKLQKAGVKSIGLSGSDGELVRVKAIDEAILGYVGEPVHVNGELLHMLVADGFVPVLAPIGVNDEFEPYNVNADTVAGAVATALQAKELIFVTDVAGILKDDELVPALTPEEVESLIEEGTIYGGMIPKVRSAIHSLTGTLEAVSIVNGNDVFFAESGKLIGTTIKKQVIHSQG | 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): 27247
Sequence Length: 260
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
|
Q31ED4 | MNLNKAQAQNIASVLAEALPYIQRFSGKTIVVKYGGNAMTEEALKNGFARDIVLMKLVGMNPVVVHGGGPQIGHLLERVGKQSEFIQGMRVTDSETMDIVEMVLGGMVNKEIVNLIHQHNGNAVGLTGKDGNLIRAKKMEMTAFNEDLNAPELIDLGHVGEVERINTKVLDMLIQDDFIPVIAPVGVDEQGHSYNINADLVAGKVAEALHAEKLMLLTNTPGLLDKQGELLTGLNAESVAALIEDGTIYGGMLPKIQCALDAVQNGVESSHIIDGRVEHAVMLEVFTDEGVGTLITSH | 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): 31990
Sequence Length: 298
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
|
B8HGC5 | MNTQTRETTSMSDAQDKAATLIEALPWIQRFAGTTMVIKYGGNAMVNDELRRAFAEDIVFLHHVGIHPVVVHGGGPQINSMLGRLGIESEFKGGLRVTTPEAMDVVRMVLTGQVGRELVGLINSHGPYAVGMSGEDGGLLRAVRTGTVVDGEDVDLGLVGEVVGVDPAGIVDILDAGRIPVISTVAPEIVDGGDSVPGAARFQPTGQVLNVNADTAAAAVASALGASKLVILTDVEGLYANWPDKSSLISSLTASELRDMLPRLESGMIPKMAACLKAIDEGVERAHIVDGRLAHSMLLETFTTAGIGTQVVPDEETNA | 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): 33369
Sequence Length: 319
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
|
A7I2W9 | MKKIGIIGVSGYTGLELIKIILNHSGFKLSYLAATSEGEISEIFPQLAGVLNMKVEIADAKEAAKRCDLVFLALPHEKAMEFAREILEFNSTKVVDLSADYRLSLKLYEKNYTKHLDPKNLSHAVYGLVEINREKIKKARLVANPGCYPTCSILAIAPFVNFIDKNIGVFIDAKSGVSGAGKGLKTTSHFVSANENLNAYSPITHRHADEIKEQIGILAGSEIDTIFVPNLVSITRGMSVSVFAVLKEKIDADKILKEFYKDEEFIRFRDEPVQIKNVVGTHFCDIFVRTACNKIFINSAIDNLLKGASSQAVANANLMLDEPENSALPKIAYGI | 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): 36898
Sequence Length: 335
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.2.1.38
|
Q9PIS0 | MKIKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPNTPLNLCFENKNLDELELDLLFLATPHKFSAKLLNENLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANPGCYTTCSILSLYPLFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKITLQFTPHLVPMQRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVLGAIDNLIKGAAGQAVQNMNLMFDFDEDEGLKFFANL | 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): 38896
Sequence Length: 342
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.2.1.38
|
Q9A8H5 | MANAPKVFIDGEAGTTGLQIRERLVGRTDLQLISIDPDKRKDADARAEMLNSADAVILCLPDDAAKEAVSLVSNPNTVIIDASTAYRTAEGWAYGFAELDSEQRGKIAASKRISNPGCYPTGAIALTRPLVSAGILPAELPVSYNAVSGYTGGGKAMIAQFEDESAADHTRAPYFIYGLSLSHKHVPEMQKHGGLLTRPIFTPAVGRYAQGMIVEMPLHLSTLNGAPSLADIHAALVKHYKGEAFVEVASLDEAKALTTLDPEGLNGTNRLKLFVFGSDAGGQARLVALLDNLGKGASGAAVQNLNIALGLDEAAGL | 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): 33278
Sequence Length: 317
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.2.1.38
|
Q6DAR1 | MLNTLIVGASGYTGAELALYLNRHPQMNITALMVSAQSVDAGKLISDLHPQLKGIIDIPVKPLTDAEEAAKGVDVVFLATDHKVSHDLAPIFLAAGCTVFDLSGAFRVQDAEFYRRYYGFEHQHTDWLAKAVYGLAEWRAESVKQAQLIAVPGCYPTAAQLALKPLLDAQLLNSAQWPVINAVSGVSGAGRKASLTSSFCEVSLQPYGIFNHRHEPEISTHLGTPVIFTPHLGNFARGILETITCRLQPGVTQQDVAEAYHNAYHDKPLVRLYDKGVPALKSVVGLPFCDIGFAVDGEHLIVVATEDNLLKGAAAQAVQCMNIRFGFPETQSLI | 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): 36171
Sequence Length: 334
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.2.1.38
|
A6KXY5 | MIKAGIIGGAGYTAGELIRLLINHPDVDIKFINSSSNAGNKITDVHEGLYGETDLVFTDELPLDEIDVLFFCTAHGDTKKFMDSHNVPEDLKIIDLSMDYRIKSDDHDFIYGLPELNRRAICHSKHVANPGCFATCIQLGLLPLAKHLLLNEDIMVNAITGSTGAGVKPGATSHFSWRNNNMSIYKPFSHQHVPEIKQSLKQLQNSFNAEIDFIPYRGDFPRGIFATLVVKCKVELEELVKMYQDYYAEDSFVHIVDKNIDLKQVVNTNKCLIHLEKHGDKLLVISCIDNLLKGASGQAVHNMNLMFNLEETVGLRLKPSAF | 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): 36012
Sequence Length: 322
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.2.1.38
|
A2BWM0 | MNVAIVGATGYGGIQSVNLLKDNKNYKISYLGGYKTSGTKWSDNFPFIKLDSNNLIEKISIDRIADKADVALLCLPNGISSTLTRGLLEKGVKVIDLSADYRYKSLEQWKRIYSNEAAKYKRDDDDLCKEAVYGLPEINNKDISKARLIACPGCYPTSALIPLIPFLSQGIIDNEGIIIDSKSGTSGGGRESSQKLLFSECGDGLSAYGLINHRHTSEIEQIASFISGNDIELLFTPHLLPMIRGMHSTIYGRLRDPGLTSSDCRIILENFYRNYSNIRVLPVDIYPSTKWVKNTNEIHLSVKVDNRNGRIILLSVIDNLLKGQTGQAIQNLNLISGLPLNNGLEMINHYP | 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): 38887
Sequence Length: 351
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.2.1.38
|
Q7V7N1 | MSQVRGSRVAVIGATGYGGLQTIRLLEDHPHLHVTYLGGERSAGRRWSELCPFLPILDDPEVQSPDPDKIAEFADYAVLSLPNGLACQLAPQLLKRNVRVVDLSADFRYRSLEQWKQVYVHEAQNLNRDDVQLCREAVYGLPEWKGPEIAVANLVAAPGCFPTASLLPLLPFLKQGLIENDGLIIDAKTGTSGGGRVAKEQFLLAEASESIMPYGVVGHRHTSEIEQLASEVAGQPIELQFTPHLVPMVRGLLATVYGRLRDPGLTAEDCTTVLKAVYRHHPCIDVLPVGTYPATKWVKYSNKAVLSVQVDNRNSRLVLMSAVDNLIKGQAGQGVQCLNLMAGLPPTTGMSLLTFYP | 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): 38981
Sequence Length: 357
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.2.1.38
|
Q58131 | MSQENWIDLEKKYHLQIYGRLPVVLVEGKGMEVYDIDGKKYLDFLAGIGVNNVGHCHPKVVEAIKKQAETLIHTSNIYYTIPQIKLAKKLVELSGLDRAFFCNSGAEANEGAIKFARKYVSKVLGREGGEIISMYNAFHGRTLTTLAATPKPKYQDGFYPLPPGFKYVPFNDIEALKEAITDKTAAIMIEPVQGEGGIHVADKDYLKAVRDLCDDKNIVLIFDEVQCGMGRTGRMFAFEHYGVEPDILTLAKALGGGVPIGAVVLKEEIAKALSYGDHGTTFGGNPLACSAALASVEVIEELIKDDKVIEKGKYFIRKLENLIEKYNFIKEVRGLGLMIGAELEFNGADIVKKMLEKGFLINCTSDTVLRFLPPLIVEKEHIDALINALDEVFTEIKK | 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): 44065
Sequence Length: 398
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular Location: Cytoplasm
EC: 2.6.1.11
|
Q8TUZ5 | MDARELIDKYHMNTYSRFPVTLVPGEGARVWDDEGNEYIDLVAGIAVNVLGHCHPAVVEAVKEQVERLIHCSNLYYNEPQAEAARLLAEAAPKDLNKVFFCNSGTESVECAIKLARKFTGCTKFIAFEGGFHGRTMGALSATWKPEFREPFEPLVPEFEHVPYGDVNAVEKAIDDDTAAVIVEPVQGEAGVRIPPEGFLRELRELCDEHGLLLIVDEVQSGMGRTGQFFAFEHEDVLPDIVCLAKGLGGGVPVGATIAREEVAEAFEPGDHGSTFGGNPLACAAVCAAVSTVLEENLPEAAERKGKLAMRILSEAEDVVEEVRGRGLMMGVEVGDDERAKDVAREMLDRGALVNVTSGDVIRLVPPLVIGEDELEKALAELADALRASG | 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): 42025
Sequence Length: 389
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular Location: Cytoplasm
EC: 2.6.1.11
|
O27392 | MDSEEIIELERKFIMQTYTRQPIVLSHGKGATVWDIEGNSYIDCFAGVAVNSIGHAHPKVALAICHQAQRLIHSSNIYYTREQVELAKLLTAISPHDRVFFANSGAEANEGAIKLARKFTGKSEIIAAENSFHGRTLATVTATGQKKYSEPFRPLPEGFKHVPYGDIGAMADAVGDETAAIILEPVQGEGGVIIPPEGYLKDVQELARQNDVLLILDEVQTGFGRTGAMFASQLFGVEPDITTVAKAMGGGYPIGAVLANERVAMAFEPGDHGSTFGGNPWGCAAAIATIEVLMDEKLPERAAKMGSYFLGRLRQVLHGCDAVRDIRGVGLMIGIEIDGECAGVVDAAREMGVLINCTAGKVIRIVPPLVIKKEEIDAAVDVLGHVISDL | 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): 41763
Sequence Length: 390
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular Location: Cytoplasm
EC: 2.6.1.11
|
A0QYS9 | MTLQSRWEAVMMNNYGTPPLSLVSGEGAVVTDADGREYLDLLGGIAVNLLGHRHPAVIEAVTTQLDTLGHTSNLYATEPGIALAEALVGQLGTQARVFFCNSGTEANEVAFKITRLTGKTKIVAAEGAFHGRTMGSLALTGQPSKQAPFEPLPGNVMHVPYGDVAALEAAVDDQTAAVFLEPIMGEGGVVVPPAGYLVAAREITSKHGALLVLDEVQTGVGRTGAFFAHQHDGIVPDVVTMAKGLGGGLPIGACLAVGATGDLLTPGLHGSTFGGNPVCTAAGLAVLKTLAAEDLVARAGVLGKTLSHGIEELGHPLVDKVRGKGLLQGIVLTVPSAKAVETAARDAGFLVNAAAPEVVRLAPPLIITEGQIEAFITALPAVLDTAAEDS | 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): 39796
Sequence Length: 390
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular Location: Cytoplasm
EC: 2.6.1.11
|
P59318 | MTALSQSEPSLSASSDSSTDALVQKAKRHLLQNYKQPPFVLARGQGARVWDMDGREYLDLIGGIATCALGHCHPEVVAAAKAQLDSLWHVSNVFYSQPQIDLAAQLTEWSGLSRAFFCNSGAEANEALLKLTRKVMKDRGTPERFEVISFDSSFHGRTLATVTATGQAKYQKGFEPLPAGFTHVPYGDLEAVRKAVGPATAAILVEPIQGEGGVRMAPLGFLVGLRALCDEHGLLLLVDEVQTGMGRTGKPFGFMHEGIVPDGISVAKALGNGLPIGAMLCKEELGASLTPGTHGSTFGGNPVAAAAANAVVRILRRPGFLDEVQEKGAYLLARARELQGRLPAGRIQAVRGQGLLVGVQLDHKVAPVIAQVHEEGLLVNPAGDRTMLFAPPFIVTVRELD | 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): 42652
Sequence Length: 401
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular Location: Cytoplasm
EC: 2.6.1.11
|
Q9P3I3 | MAFRTALRRVAAVNAAPATRLAGAGAGAATAARRSYATASQLTHPDPTEDSPSGKMVREHVPYMVTTYSRPPPVFVKGKGSYLWDLEDRKYLDFTSGIAVNSLGHCDEEFSKIIAEQAQELVHASNLYYNPWTGALSKLLVESTKASGGMHDASSVFVCNSGSEANEAGIKFARKVGKVLDPSGSKVEIVCFQNAFHGRTMGSLSATPNPKYQAPFAPMVPGFKVGTYNDIAAIPSLVTEKTCSVIVEPIQGEGGVMPATEEFLVALGKRCREVGALLHYDEIQCGLARTGTFWAHSSLPKEAHPDILTTAKAIGNGFPIAATIVNEHVASKIKVGDHGTTFGGNPLACRLAHYIVGRLADKQLQEGVKAKSEVFLRGFEKLRNKFPSLVKEVRGKGLILGLQLSEDPTPVIKAARERGLLVITAGTNTLRFVPSLLVTEGEIEEGLKILEESFEAVMVKA | Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 49408
Sequence Length: 461
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.11
|
Q8CUM9 | MSSTTKVSSAVMQTYNRFPITATKGKGSFLWDDNGEKYLDYTSGIATCNLGHVPDNVQHAISNQLKDLWHCSNLYHIPSQEKLAALLTEYSCLDQVFFCNSGAEANEAAIKIAKKYAKDKGYDDRTEIITFEQSFHGRTGSTMAATAQEKIHQGFTPLTEGFRYLPFNNKESLSEIDNGKTSAVLLEVIQGEGGIHTAEKDWLKQLAAICKQADILLMIDEIQTGIGRTGSLFAYQPYGIEPDVITVAKGLGSGFPIGAMLAKQHIAASFSPGTHGSTFGGNPVAAAAGIATLKEILSDGFLENCKEGQEELFNQLKSIKEISPLIKDIRGKGYLMGIEVMNQASAWIEKLREKQILVLPAGEKVVRILPPLTTTKEELQICIQALKEVALELGGNTNG | 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): 43410
Sequence Length: 399
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular Location: Cytoplasm
EC: 2.6.1.11
|
Q7VAS9 | MVDAPHSKCGTFGFVGSSPTAPTFLLDTYKRLPLKIVKGNGCWLWDETGKKYLDAVAGIATCSLGHSDKKLSKVLSQQLRKIQHVSNLYRIPEQEDLAQWLVNQSCADSVFFCNSGAEANEAAIKLARKYGQIKRGIKRPIILSAKSSFHGRTLAALSATGQTKYQKGFEPLVEGFEFFSFNDSNSVQDLYENLEKDEPRVAAILIEPIQGEGGLNLGDQKFFYFLRDYCNKNNILLLFDEVQSGMGRTGKLWGYEHFNVEPDAFTLAKGLGGGHSIGALLVKENASIFEPGDHASTFGGNPFACKAGLTVAKEIQNRNLLENTYCRGNQLREGLQKLINNYPHHLEEVRGIGLMLGLAIKKNSNLTSQKIVELAIKEGLLVIGAGEKVIRMLPPLIITKREIETLLTRLNACFRKLNN | 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): 46354
Sequence Length: 419
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular Location: Cytoplasm
EC: 2.6.1.11
|
Q7VSW3 | MAVNLQIPSESEILPVAGVEIGVAEAGIRKAGRRDLTVFRLAPGSAVAGVFTRNRFRAAPVQVCEAHLAQGGPIRALVVNTGNANAGTGAPGLKNAQDTCAALGKLLDVPAEQILPFSTGVILEPLPMDRLTAGLPAAVADLRADGWYGAAHGIMTTDTLPKIHSRRVNIGGKTVTITGISKGAGMIRPNMATMLGFLATDAGIAQPLLRQLAIELADVSFNRITVDGDTSTNDSFILIATGQAGVTVDSAGDAAYAALRDALAAAATDLAQKIVRDAEGATKFMTIRVEEAGNTEEALKVAYAVAHSPLVKTAFFASDPNLGRILAAIGYAGIDDLDVSRLRLWLGDVLVAVDGGRNPDYQEADGQRVMKQAEILVRIALGRGQVADTVYTCDFSHEYVTINADYRS | 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-ornithine = L-ornithine + N-acetyl-L-glutamate
Sequence Mass (Da): 42685
Sequence Length: 408
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Subcellular Location: Cytoplasm
|
Q8CK24 | MSVTAAKGFTAAGITAGIKESGSPDLALVVNTGPRRSAAGVFTSNRVKAAPVLWSEQVLKSGEVTAVVLNSGGANACTGPKGFQDTHATAEKAADVLGTGAGEVAVCSTGLIGVLLPMDKLLPGVEAAAGQLSEHGGEKAAIAIKTTDTVHKTSVVTRDGWTVGGMAKGAGMLAPGLATMLVVITTDADLETEALDRALRAATRVTFDRVDSDGCMSTNDTVLLLSSGSSGVTPEYDAFAEAVRTVCDDLGQQLIRDAEGASKDIKVEVVNAATEDEAVQVGRTIARNNLLKCAIHGEDPNWGRVLSAIGTTDAAFEPDRLNVAINGVWVCKNGGVGEDRELVDMRYREVHIVADLAAGDATATIWTNDLTADYVHENSAYSS | 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-ornithine = L-ornithine + N-acetyl-L-glutamate
Sequence Mass (Da): 39512
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Subcellular Location: Cytoplasm
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Q3A246 | MVKVNGFSFVARSAGIRKSGKPDLGLIFSTVPARCAGVFTTNKVQAAPVLVTAPRIAAGECQAVLVNSGNANACTGEVGMQDALRCGQLAAKSLGIDEQLVAVSSTGVIGHPLPMPLLEKTIPGMSEGLSETAVDDVANAMMTTDSFAKVASRQAGDSAPYTILGVAKGAGMIHPNMATMLSFVMTDACVDQHFLQQALRQAVEGSFNIITVDRDTSTNDMVLVLANGESKTPEIVADSAEGQEFAELLRGVLLDLAKMIVRDGEGATKLVHVCVNGAADDGDARKVAYNVATSNLVKTAFFGEDANWGRIIAAVGYSEAQVDPSRIAIFFDGVPVVQKGLGTGPELEAQATDVLKQAEFSVTIDLGLGDGRGEYYTSDLTYEYVKINADYRT | 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-ornithine = L-ornithine + N-acetyl-L-glutamate
Sequence Mass (Da): 41236
Sequence Length: 393
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Subcellular Location: Cytoplasm
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B8BVB6 | MMFTKSTALALAAIVALSNVNAFSTSIHQPITSKAAHITSSSSLQAANNGLDTDTTLPSFSTKEEYTSYLQKAGRLPSGFAVGTAKGTFVSVEAPALGPLPIKATVIHLTEGPTDSWAAVFTKQSGCPVKVGKARLSGGHPLQALVINNKVSNVCPGGDGIAAAESVCAAVASSLNLPGGANSVLPSSTGVIGWRLPAKELAEDVAPRAIEALQTESAYAAAEAIMTTDRYPKLRSKTLSDGVRVVGVAKGAGMIEPNMATMLGYIMTDATIEKSKLQTMLTEACNRSFNSISVDGDESTSDTVVAIASGLKPLSSEDELKDALFEVCEGLSADLVRNGEGTGHVIRVTISNFPGSEYDARRMGRHLVNSPLVKCAISGNDPNTGRIAGAIGSFMGKFFPTESVAEMSLTLGGRTIFNNGQFVLEGDAVEKELSGHMSDAQLGEHDDFPKHQKFVEIGVDFGGSGSDVIVLGSDLTKEYVEVNADYRS | 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 precursor protein within the mitochondrion.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
Sequence Mass (Da): 50928
Sequence Length: 488
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Subcellular Location: Mitochondrion matrix
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Q9Z4S1 | MFVPRGFSYAGVHCRIKRKRKDLGIIFSEVPCTAAGVFTTNVVKAAPVIYDMEILGKNPSGIRAITVNSGVANACTGEQGMINARRMAEKTAKELNIPVESVLVSSTGVIGVQLPMEKVESGIEEAVKNLSKDPVPFAEAIMTTDTKIKIHSKKVTIEGKEITVLGIAKGSGMIHPNMATMLSFITTDANVSEDALKKLLKISVDDSYNMIDVDGDTSTNDMVIILANGLAGNAPIQEETDGFWKLYEAVHEVNQVLAEKIVEDGEGATKVIEVEVRNAPDRNSARLIARAIVSSNLVKTAIYGEDANWGRVIAAAGYSGAQFDPDRLDLFFESAAGRIKVAENGQGVDFDEDTAKKILSEKKVKIILDMKQGKELARAWGCDLTEKYVEINGRYRT | 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-ornithine = L-ornithine + N-acetyl-L-glutamate
Sequence Mass (Da): 43043
Sequence Length: 397
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Subcellular Location: Cytoplasm
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B8ZRK7 | MTHGASKTTPETTRAGRQARIVAILSSTSVRSQSELATLLADDGIDVTQATLSRDLEELGAVKLRGADGGVGVYVVPEDGSPVRGVSGGTARLSRLLSELLVSADSSANLAVLRTPPGAADYLASAIDRAALPYVVGTIAGDDTVFVAAREPMTGSELATVLESLNR | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 17120
Sequence Length: 167
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
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B2HR31 | MNGAKQAPEISVNRAGRQARIVAILSTESVSSQSELAALLAVQGIEATQATLSRDLEELGAVKLRGADGGVGVYVVPEDGSPVRGVTGGTGRLARLLGELLVSSDASANLAVLRTPPGGAHYLASAIDRAALPYVVGTIAGDDTVFVAAREPMTGAELAIALEKLK | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 16872
Sequence Length: 166
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
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P9WPY8 | MSRAKAAPVAGPEVAANRAGRQARIVAILSSAQVRSQNELAALLAAEGIEVTQATLSRDLEELGAVKLRGADGGTGIYVVPEDGSPVRGVSGGTDRMARLLGELLVSTDDSGNLAVLRTPPGAAHYLASAIDRAALPQVVGTIAGDDTILVVAREPTTGAQLAGMFENFGKESHVRARHPGLFRRSGHLGGDQLDRQGDRP | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 20802
Sequence Length: 201
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
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Q5YYF4 | MSVSTPERGGAEQGKGPAIARTRAGRQSRIVELLSAHAVRSQSELAALLAAEGIETTQATLSRDLDELGAVKLRAADGGAGVYVVPEDGSPVRGVTGGTDRLSKLLGDLLVSTDASGNIAVLRTPPGAAGYLASALDRAALPYVVGTIAGDDTIAVIAREPLTGAELAAKIEELA | Function: Regulates arginine biosynthesis genes.
Sequence Mass (Da): 17681
Sequence Length: 175
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Subcellular Location: Cytoplasm
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Q6PFJ9 | MDSDEGYNYEFDDEEEECSEDSGEEETADDTLELGEVELVDPVVAGGERDDCGETGGSGLGPGQDEEDYRFEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLDKLFSECHVINPSKKSRTRLMNTRSSAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWGDYLTTKIIEEGMGQTISCPAHSCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLRKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRSTLMFTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVLLQHVHEGYDKDLWEYIED | Function: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 ube2l3. Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets. The initial ubiquitin is then elongated. E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 61654
Sequence Length: 527
Domain: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.31
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Q94981 | MDSDNDNDFCDNVDSGNVSSGDDGDDDFGMEVDLPSSADRQMDQDDYQYKVLTTDEIVQHQREIIDEANLLLKLPTPTTRILLNHFKWDKEKLLEKYFDDNTDEFFKCAHVINPFNATEAIKQKTSRSQCEECEICFSQLPPDSMAGLECGHRFCMPCWHEYLSTKIVAEGLGQTISCAAHGCDILVDDVTVANLVTDARVRVKYQQLITNSFVECNQLLRWCPSVDCTYAVKVPYAEPRRVHCKCGHVFCFACGENWHDPVKCRWLKKWIKKCDDDSETSNWIAANTKECPRCSVTIEKDGGCNHMVCKNQNCKNEFCWVCLGSWEPHGSSWYNCNRYDEDEAKTARDAQEKLRSSLARYLHYYNRYMNHMQSMKFENKLYASVKQKMEEMQQHNMSWIEVQFLKKAVDILCQCRQTLMYTYVFAYYLKKNNQSMIFEDNQKDLESATEMLSEYLERDITSENLADIKQKVQDKYRYCEKRCSVLLKHVHEGYDKEWWEYTE | Function: Atypical E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 Ubc10 . Controls the subcellular localization and morphology of muscle nuclei (myonuclei) by regulating the protein levels and distribution of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex . Functions by mediating the monoubiquitination of the LINC complex subunit koi leading to its subsequent proteasomal degradation . Appears to function, at least partially redundantly, with the RBR E3 ligase family member park in nuclear localization and morphology . Likely to function in metamorphosis by regulating the proteins levels of EcR isoform A (ECR-A) and its heterodimeric partner usp, via the ubiquitination and subsequent degradation of ECR-A .
PTM: Autophosphorylated.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 58932
Sequence Length: 503
Domain: Members of the RBR family are atypical E3 ligases. They interact with E2 conjugating enzymes such as Ubc10 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate.
Subcellular Location: Cytoplasm
EC: 2.3.2.31
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Q9Y4X5 | MDSDEGYNYEFDEDEECSEEDSGAEEEEDEDDDEPDDDTLDLGEVELVEPGLGVGGERDGLLCGETGGGGGSALGPGGGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRSSAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRATLMYTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVLLQHVHEGYEKDLWEYIED | Function: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 . Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets . The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2 . E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes . Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear . According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest . According to another report EIF4E2 ubiquitination leads to its subsequent degradation . Acts as the ligase involved in ISGylation of EIF4E2 . In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, nuclear subcellular localization and nuclear morphology .
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 64118
Sequence Length: 557
Domain: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger . The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate .
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.31
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Q22431 | MDDEDMSCTSGDDYAGYGDEDYYNEADVDAADDVAVTPTHSEEADYECLSVNQVERVFIDGVNSLVSRISINEKFARILLQANHWDVDKIARLVRNDRNDFLRKCHIDAKPEPKRKLSSTQSVLAKGYCSVCAMDGYTELPHLTCGHCFCEHCWKSHVESRLSEGVASRIECMESECEVYAPSEFVLSIIKNSPVIKLKYERFLLRDMVNSHPHLKFCVGNECPVIIRSTEVKPKRVTCMQCHTSFCVKCGADYHAPTSCETIKQWMTKCADDSETANYISAHTKDCPQCHSCIEKAGGCNHIQCTRCRHHFCWMCFGDWKSHGSEYYECSRYKENPSVAAEANHVKARRALEKYLHYFERFENHSKSLKMEEELRDKIRKKIDDKVNEHNGTWIDWQYLHKSVSLLTKCRYTLQYTYPFAYFLSATPRKNLFEYQQAQLEKEVEELAWAVERADGTARGALEAHMHRAEHKRQTLLHDFFF | Function: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBC-2/UBE2L3, and then transfers it to substrates.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 55808
Sequence Length: 482
Domain: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate.
Subcellular Location: Nucleus
EC: 2.3.2.31
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O76924 | MDSDIEMDMESDNDGEYDDDYDYYNTGEDCDVERLDPKRADPEYFEYECLTVEDIEKLLNERVEKLNTILQITPSLAKVLLLEHQWNNVAVVEKYRQDANALLVTARIKPPSVAVTDTASTSAAAASAQLLRLGSSGYKTTASATPQYRSQMCPVCASSQLGDKFYSLACGHSFCKDCWTIYFETQIFQGISTQIGCMAQMCNVRVPEDLVLTLVTRPVMRDKYQQFAFKDYVKSHPELRFCPGPNCQIIVQSSEISAKRAICKACHTGFCFRCGMDYHAPTDCQVIKKWLTKCADDSETANYISAHTKDCPKCHICIEKNGGCNHMQCFNCKHDFCWMCLGDWKTHGSEYYECSRYKDNPNIANESVHVQAREALKKYLHYYERWENHSKSLKLEQQTIDRLRQRINSKVMNGSGTWIDWQYLFNAAALLAKCRYTLQYTYPYAYYMEAGSRKNLFEYQQAQLEAEIENLSWKIERAETTDLGDLENQMDIAEKRRTTLLKDFFPVDA | Function: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 58627
Sequence Length: 509
Domain: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate.
Subcellular Location: Nucleus
EC: 2.3.2.31
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O95376 | MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEARVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVGVSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQEPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKCNICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQAREALKKYLFYFERWENHNKSLQLEAQTYQRIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKCRYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAEQRRRTLLKDFHDT | Function: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 . Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (By similarity). The initial ubiquitin is then elongated (By similarity). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex . Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination . May play a role in myelopoiesis .
PTM: Ubiquitinated. Ubiquitination promotes proteasomal degradation.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 57819
Sequence Length: 493
Domain: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.31
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Q8U9X6 | MADGTDQKSSNQMWGGRFASGPSAIMEEINASIGFDKKLYAQDIRGSIAHATMLAEKGIISQEDKEKIVHGLNTILSEIEAGTFEFSRKLEDIHMNIEARLATLIGTAAGRLHTARSRNDQVALDFRLWVKEELQKTEGMLTALIAAFLDRAEENADTVMPGFTHLQTAQPVTFGHHCMAYVEMFGRDRARVRHAIEHLDESPIGAAALAGTGYPIDRHMTAKALGFREPTRNSIDTVSDRDFALEFLSIASICATHLSRLAEEIVIWSTPQFGFIRLSDAFSTGSSIMPQKKNPDAAELVRAKTGRINGSLVALLTVMKGLPLAYSKDMQEDKEQVFDSAESLELAIAAMTGMIRDLEVRKDRMRAAAGSGYSTATDLADWLVREAGLPFRDAHHVTGNAVALAEKKGCDLADLSLEELQAIHPDITNGIFDVLSVEASVASRTSFGGTAPSEVRKQIAWWRGRN | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 50989
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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Q5WHY3 | MVGRLKESPSQEMIDLLFKPSIRSDLKHHYSYLLKINSVHLFMLKSEGIISDEAASKIHSVLTHLQVTGKEALSINPALEDLYFNVEAYIIEQTGPEIGGQMHTGRSRNDILATVTRMRIREEMLEIYELVCTLRRTLIDLATEHTSTLMTGYTHLQPAEPITFAHYLSALLHGFERDFTRLYNCYAHINKSPLGSCALASTTFSINRKFTMELLGFADLLENSLDGIASRDYALEALSALSIFSNSLSRFAQDLYTWCSYEFGYLEVGHSVAVISSIMPQKKNPVTLEHIKAKAGHIQGALVSSLSVLKNTLYSHSRDTSMESMKYTWEAINETKAAIRLMIKTLQTLTVHKDNMAATTRQNFSTVTELANALVRHYHFSFRTAHHIVAEIVNETLNQGLGSDKIEASTVERAIKQVTAKTVSVTKEFVEQALDPERNISLRTVRGGSAPVEVARQLQQLEQTLASDHQKISDLKQALQSADQLYKHYAAELERGAQ | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 55866
Sequence Length: 498
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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Q8U705 | MADINPRQSDTSKFPDPVYKETVLRPLFDGAKNHHVDGFRRIDRAHLVMLRETGILDAETAAKIAGALEDIDRTIEPSELVYTGEVEDFFFLIEKELKARIGVDVAGRLHTARSRNDIDHTLFKIGLKDKIDTLTAKARVLLKALIDAAERNQSTLIVAYTHGQPAQPTTFGHYLSAAIEVLIRDIERFTEARHIVDLSPMGAAAITTSGFPIDRARVAELLGFAAPLRNSYSCIAAVDYTTATYGAIELMFLHLGRLIQDFQFWTSFEVGQIYVPNSLVQISSIMPQKRNPVPIEHLRHLASQTFGRARTMLDVMHNTPFTDMNDSEGETQSMGYEAFASAGRVLDLLASLVGQISIDPERVDQNIRRSCITITELADSLVRIEDLSFRQAHEIAATVAKSVVALKGDLPNDGYQPFLGAFSGLTGRETGIDEEKFRQIVSPEHFVAVRSRFGGPAPEPMREAFAAYRGKLGAFEAEAQRSTNHEAAKAAELAEKFTALTGAR | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 55699
Sequence Length: 504
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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Q981V0 | MEPIPLEAEKPGSCPEPFGGSLMNRGSFLFVESNTTGTGELLMKRARLLGFETYLVTRNPARYPFLRDSVAQLIEAETRSPDELVGVATKLSGLAGIYSSSDYFVEAASSAAMAMGLPAANARAIATCRNKWKQATELQRHSIPIPETWLATSIRDVENILAHGTLPVVVKPVSGSGSSGVRLCDSAAAAIAGFNSAKSVLQDQVDLPSPDILIQQYVEGKEYSAEIIAYDGKLHCLGILAKHKGPPPCFVEVGHDFPAPLLEPSLQELASFASGAVSALGLEFGPAHVEFVITESGPVIIEVNPRLAGGMIPVMLSHALGTSILDMVIRLYAGEGFTPPRGSARAGAIRFRLAPTSGKLKSLGFSRNPDPTVPEAGLLKSEGGDVQIKGDFRDRVAYAVGVADELDAAAAAADRMIDSLVIDIETAADESDKQDPGPGEGRWALHPEAMKLLAPPIEISRDGRLLQHQAAIDEAHLVMLADQGLVSQAAAADLLKHILDLQDEGFQSLEGRDAPRGVYLAYEAELAARAGPEKAGWLHLARSRNDLNATISLLVLREAACSISQQIGIAQGALLQRVEEASSLVAPLYSQYQIALPGSPGHYLLGVFFALGRERQRLHSLLEDIRNCPMGAGAGGGTSMPIDPLKTASLLGFEEPSFNSLDAVASRDHHLHGLSIFASISTLLSRVAQDLQVWTTREFALIDVPRNLAGGSSMLPQKKNPFLLEHIKGSASTVIGAYVSAATATCKAPFSNSIEVSNYGCSPLRLSEEALQRALILTSLIVKGMSFNVRSMRDHLEDGSSMTAIAAERMASRGIPFREAHTQIGEIAQRLSQDDCATQRRSELASQLAGVFPVSLEECRDALQFGGGPGKRSTDDQLSVAKTHFREMELKCAEISERWAHAEAHCKGRVKELIDKHRSTCRSGVCG | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 99126
Sequence Length: 927
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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Q92VM6 | MTEPTQLWGGRFKSGPSEALANLSRAPRSYFRLYKEDIAGSRAHASELKRAGVLDESEFSAIRAALEGIEADVGAGREEPIAADEDLHTFLERLLMARLGTLGGKLRAGRSRNDQTANNTRLYLRRMARELSQGVIAIEEALTEQASRHTETVMPGFTHLQPAQPVVLGHHLMAHAQSLLRDLQRFADWDRRFDRSPLGAAALAGSGIARRPDLSAIDLGYSAACENSIDAVAARDHVAEFLFICSLVAVDLSRLAEEICLWSSKQFSWVRLHDSYSTGSSIMPQKKNPDVAELTRGMSGTLIGNIAGFLATMKAMPLAYNRDLAEDKRSLFETIDVLELVLPAFAGMVGTLEFDVEKLREEAPKGFTLATEVADWLVGRDVPFAEAHEITGAVVRFCEERGHDLAGLTAEDLPGIDPRLHPEMLAALVLEKALASRNGYGATAPEKVREQIARFETALAECCAFAGGPIGGGAFAGAKDGAEEARRR | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 53037
Sequence Length: 488
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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Q182I5 | MKLWGGRFRKAENQLMEEFNKSFGYDCVLYKKDIEGSVAHVHMQVKCGLLTEEEGKSITEGLKGILEDVENGKLVLDGEYEDIHSFTEINLIQRIGDVGKKLHTARSRNDQVAVDMRLYAKEKANDLVGLISEFKATIKDVADKNPVMMPGYTHLQRAQVVTFKHHLMAYYSMFDRDEKRIKNAIEILDESPLGCGALAGTTHDIDRSITCEQLGFKKVVDNFMDGVSDRDYLLELMSDFSIIMMHLSRLSEELILWSSQEFGFVEIDDLYTTGSSIMPQKKNPDGAELIRGKTGRVYGNLFGLFTVMKGIPLAYNKDMQEDKEGFFDSVHTLEMCIQIMDRMIATLKVNEDKMKQAVKNGFLNATEVADYLVKNNVAFRDAHGIVGSIVIYCEDNKKAIEDLTLEELHKFSDAFKEDIYDFIDYESILNKGIKKNLK | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 49853
Sequence Length: 438
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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B9E0B2 | MKLWGGRFKKSESKLMEDFNSSLSFDRQLYKEDIEGSMVHVKMLAKCNILSSEESKAILSGLESILKDIEEGKLEVEGDYEDIHSFVEINLIERIGQVAKKLHTARSRNDQVALDFRLYAKRKALEVVENIEYLQDVIENLGDKNNVIMPGYTHLQRAQVVTFKHHIMAYYHMFKRDRERILNAICIMDESPLGCCALAGTTYNIDRNFTAQELGFKKPVDNFLDGVSDRDYVIELISDFSIIMMHLSRLSEELILWSSKEFDFIRIDDEFSTGSSIMPQKKNPDAAELIRGKTGRVYGSLVSLLTTMKGIPLAYNKDMQEDKEQLFNSLDTVLSCLKIMSGMLSTLKVNEKNTFNAVKKGFLNATEAADYLVNKGMAFRDAHKVIGEIVLYCEDKNRAIEDISLDELKKFSSLFEEDVYDFIDYENTINRGIKRNLK | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 50221
Sequence Length: 438
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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Q3IME1 | MTGDADEGRDVVRRDRFSGGPARGFLSSLAADERIFEADLAVDRAHVVMLDEQDIIGTDDAAAILGALDDVEAAGHGSLTDGEDVHAAIETAVIERVGDRGGKMHTARSRNDEVAACIRYRLREDVLAAVEATLEAREMLLDVAGDHTETVMPGFTHLQPAQPTTVAHYLHSYASALARDTERLLDAYGRINRSPLGAAAFAGTPFDIDRERTAELLGFDGVVRNSMDAASARDFLVETTAAAAGLATTLSGLAEDLVVFSKAGYVELDDAYASTSSIMPQKKNPDTMELVRATAGDTAAGLNALLTILKGLPRAYNRDLQRAHPHAFEALDAVTEATEVAAGAVATADWKEPALSEAAGEGFSTATGVADLLAMEGVPFRTAHELVARAAEAGGDYAALSAAAEDILGGPLSEHVDKAAVEAALDPESSVASRDSLGGPAPESMAAALSAAGQRLDADAEALRERRGALATAADERERVVSSYDSTAPE | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 51179
Sequence Length: 490
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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B2A8E3 | MSKLWGGRFSKQTDQLVDEFNASIEFDNRLIFYDLLGSQAHVKMLFQQGIIDTTDYKQITEGLDIIWKEAEQDKLEFNLSDEDIHMSIEKRLIELKGEVGKKLHTARSRNDQVAVDMNMFLCDKAIKLVNELLQNMSVIKELSEQHTKTYMPGYTHLQRAQPTTLGHHMLNYFWKFQRDASRLIDFRNRADLSPLGSGAFAGTGFNISRRSTRKDLGFTQQFENSMDAVSSRDLSLEFIFCLSSIMINLSRLAEELILWSTKEFDFIELDDAFATGSSIMPQKKNPDVPELIRGKTGRVVGHLTALATTYKGLPMAYNKDFQEDKEGLFDSLDTVESSLKLTSKILSTMTIKTKNMEKALYQDFSNATDIADYLATQGIPFRDAHAVVGQLVKHCQEHNKLFYQLTEQELDISFKQIADSLEENSQQILTQMDTTKILNIMDPIKCVHNRNSRGAPAPEALQFQLGQAQKYFHSLTEQVKTYQSFLP | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 55671
Sequence Length: 487
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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A9A331 | MYRSRLGNDLSDITLDYVSSIDDDAAITFYDIVGSQAHVLMLYQQKIITKSDAKKILSSLESLKDETFDSSSGAEDIHELIEALVIKRAGMSSGGKMHTARSRNDQVVLDIRMKIRDDINIICNCLLDTIEALVSVAKNHQKTIMPLYTHLQQAQAGLFSHYLLAHADVLSRDFQRLYGTFERINQSPLGAGPVGGTSISIDRRSTAKMLGFDDVVENSIDATSTRDFVAEYVSMVSILMTNLSKIAEDFVIWSTSEFSFIELSDEFTSPSSVMPQKKNPDILELTRGKTSEVIGNLTAILTTVKGLASGYGRDLQQIKSSIWSTSKISISALLIFKSMLLTLKVNEKQMKKVTESSNLIALDIAEKLVQEGIPFRVTHKIAGSLTQLAHLSKKPISKLTPSDIKKSVADTKVDPKLVLEIISSITVVSSLKERKSYGSSGYDEQKRMISDRLKKINDFRTDLTHRENKINSSLEDLKKQIDEII | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 53923
Sequence Length: 485
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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Q4J8F0 | MLYRRWGSDKDFVISYTSSNESDKEIVEEVKLTLKAHVIELYLSNYISKDTAKKIIRAINSFKDYPSSGYEDVHEALEDYIIKNIGEEGGWVGLGRSRNDHVATALRLRTREYIFDIMEELYLLRKSLIEQAKKNLNTIMPSYTHFQPAQPTTLAHYFMYLEEELNTPWEALFNSLKLINRSPLGSGAIVGSNVKIDRKREAELLGFDDVLYNTISSTSSRIDFINAISSLTLLMLVLSRFAEDMILLSSMFVNIIKLPDSHVSTSSLMPQKRNSVTMEILRTKVGECYGDLSSLMMIYKGLPSGYNLDLQEMNKHYWNCIKHVIPSIHITRDIIQNIQIKNFGEIQGLTATDLAEEMAISGIPYRKAYIDVANKIKAGTFVAGISYTKSIENKKVIGSPNPSLLTQEIEIKEKRLNNQHEKFKQYKESVIEKMGQLGVIEDGLLQQ | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 50950
Sequence Length: 447
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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Q2LT96 | MKDSTEKSKPWGGRFQEPTNELVEAFTASISFDRRLYRYDIEGSIAHARMLVRQEIINRKEGFAIVEGLKEIQRDIETGSFEFSPGDEDIHMAIEKDLIRRIGDAGAKLHTGRSRNDQVALDVRLYLRAEIKEILEFMKVLKGAFLELAKKEAETILPGYTHLQKAQPVLLAHYLLAWREMLDRDESRLRDCYRRVNVLPLGAAALAGTSLPIDRAYVARLLKFPEISRNSMDTVSDRDFVAEFLFASSLIMMHLSRFCEDLILWSSGEFNFVEISDAFTTGSSIMPQKKNPDVAELIRGKTGRVYGNLIALLTLLKGLPMTYNRDLQEDKEPLFDTVDTVKACLQILAEMIRNMKFNREKMRQEAEGGFSTATDLAEYLVMKGIPFREAHGIVGKLVSFCIECKKELAQLSMEEFQRFCPVINEDIHDRLSVSNSVRSRKSYGGTACRQVMEQIRQIEEGAYPSTRRRKEA | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 53888
Sequence Length: 472
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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Q9Z4S3 | MSEKLWEKGYTVDEEVEKFTVGDDYIVDMRIIKYDIKASIVHSKMLQRTGLLTQEEQKKIEEALNELLHLVEEGKFQIKPEDEDCHTAIENFLVKKLGETGKKIHTARSRNDQVLTALRLMYKDELKKIKDLVVELQKSLDGFIERFGQIKFAGFTHTRKAMPTDFATWAGALRDALQDDLKLLETVYDIIDQSPLGTGAGYGVPIEVDREFTAKELGFSRVQWNPIYTQNSRGKFEYLLLHVLSQISYDLNRFASDIIFFSLPEIGFLKLPKELCTGSSIMPHKINPDPLELVRAYHHFVVSRMVMAVSLPSNLILGYHRDLQLLKKPVIESIDVVKNILRIMKIIFDRIEVDREKSEDSITEEVLATHRVYELVKKGIPFRDAYRMVAEKYGREKD | Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Mass (Da): 46000
Sequence Length: 398
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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Q6D2F1 | MKAIVFAYHDIGCVGLEALALAGYEIQAVFTHSDAPGENHFYASVAKTAAGMDVPVFAPEDINHPLWVNRIRELAPDVIFSFYYRTILSDDILQLPSFGAFNLHGSLLPRYRGRAPVNWVLVNGETQTGVTLHKMVSRADAGDIVAQSVVAIDDEDTALTLHGKCRTAAATLLAQQLPLIRSREIALTPQDDSQASYFGRRTAADGLIDWQKSAHEINNLIRAVTEPYPGAFTFLGERKVIIWRARVVKNNRVNVNHPHGGDAGSIISTSPLVVSCGEDALEIVSGQSEAGLYMSGSRLAAEMGMVPQARLGNLASRVQRRRTRVLILGVNGFIGNHLTERLLRDDRYEIYGLDISSDAIARFLGDPRFHFVEGDISIHNEWIEYHIKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLKIVRDCVRYNKRIVFPSTSEVYGMCDDKEFDEDTSRLIVGPINKQRWIYSVSKQLLDRVIWAYGAKNGLRFTLFRPFNWMGPRLDTLDAARIGSSRAITQLILNLVEGSPIKLVDGGAQKRCFTDIHDGIEALFRVIENRNGQCDGQIINIGNPHNEASIRELGEMLLTSFNAHPLRDRFPPFAGFIDVESSSYYGKGYQDVAHRTPSIRNAKRLLEWEPTVKMEQTVAETLDYFLRTVDVPHTADATDTQG | Function: Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
Catalytic Activity: NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose
Sequence Mass (Da): 75223
Sequence Length: 673
Pathway: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3.
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A4WAL9 | MMGYFWALMSVLLVSGAQLMMKWAMVSLPPVGQTDALMSAFMSVTPGAVALVIGLFAYVFSMGCWYMALRRIALSKAYPLLSLSYVLVWAAAIGLPWLHEPFSVGKLAGVSVIFVGLLLVCLPDKKS | 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): 13752
Sequence Length: 127
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
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B2VBI5 | MGLLFALGSVVLVSAAQLLLKWAMIQLPDISQLPQFLSSLSQFPLPTAALFLGLLAYALSMLCWLLALKRLPLSRAYPLLSLSYLLVWLAALWLPGLNEVFRWGKLAGAGLIVSGLLLICWPAAKTR | 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): 13862
Sequence Length: 127
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
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Q6D2F5 | MTNKGYFWVVASLVLASAAQVLMKSGMLALPSISMTHWPSLSTLMAGWPVVAVLVGIICYGLSMVCWFMVLRYLPLSRAYPLISLSYAVVYLAAVFLPWLNEPMSLRKNLGVLIILLGVWLVSRDAQATK | 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): 14336
Sequence Length: 130
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
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B4ETM1 | MKTGYLWAIASALLVTVAQLLLKIGMSELPDLQLEKQWFDLHWLWANIIPISVVFVGLIGYVLSMVCWLLTLRTIPLNKAYPLISLSYVFVYILAVVLPWFQETLSWSKTIGIIFIMLGVWLISQKTEQTTSH | 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): 15226
Sequence Length: 133
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
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Q9HY59 | MNALRGWLAALGSVLLASAAQLGMRWGMSRLPLPEAWAGQTPERAALLAVALAVAAYAASLLCWLAALRHLPLGRAYSLLSASYALVYLLAASLPAFDETFSTSKTLGVGLVVLGVLTVNARRTAAAPAHHPSRKAP | 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): 14273
Sequence Length: 137
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
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P23281 | LTAAVAVAGGNSRYVLDGVPRMRERPIGDLVDGLKQLGAEVDCFLGTKCPPVRIVSKGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIIDKLISVLYVEMTLKLMERFGISVEHSSSWDRFVVRGGQKYKSPGKAYVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEQMGAEVTWTENSVTVKGPPRNSSAMKHLRAIDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPEKLNVTEIDTYDDHRMAMAFSLAACADVPVTINDPGCTRKTFPNYFDVLQQYSKH | 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): 36319
Sequence Length: 338
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Subcellular Location: Plastid
EC: 2.5.1.19
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A3DK03 | MLLKVRKSKASGNVRIPGSKSHTIRALFFASLAEGKSEIQSPLISDDALSAVEVCRALGAKIEKEDDKYVVEGFGGNPEVPEDVINVGNSGTTLRFGIMTAALGDGCSVFTGDRQIRQRPLGPLLCAINNLGAEAFSTRNNGRAPVVVKGKLKGGRTEIDSVTSQYLSSILINSPLIPLDTEVIVTRLNEVPYVDMTLWWLDKLGIKYENHDYKTFYIKGGQRYRPLNVTIPGDFSSATFFAVQAAISGEEFVLDNLDMTDPQGDKMVFSILEDMGAKVKVEGKSVRIKGCELVGREIDMNAIPDALPAMAVAGCFAKGETKLLNVPQARIKETDRIHVMCEQLKKMGADITELEDGLVIRESRLKGCKLEGYGDHRVVMSLAIAGLNAEGETVIDTAEAVNVTFPDFVNFLSRCGADISTCE | 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): 45916
Sequence Length: 423
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
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A5FUH8 | MEHAATLPQTSRRPATPLTGTITVPGDKSISHRALMFAGLAVGETRISGLLEGEDVLRTAAAMRALGATVERTGPGAWRASGPGIGGLQSPDDVLDMGNSGTAARLLCGILASHDIFAVMTGDASLRRRPMRRVIDPLGATGAVFAAREGGRLPLSVRGAAEAMPLSYRLPVASAQVKSALLLAGLNARGITEIEEPEPTRDHSENMLRHFGAEVEVAAHGTGKLIRLRGQPELRGADVVVPGDPSSAAFPIVAALIVPGSRVTIGGVGLNPLRTGLFLTLREMGAAIEIVNAREAGGEPVGDLIVTASDLRAVDVPAERAPSMIDEYPILAVACAMARGSSRLRGLAELRVKESDRLAATLAMITANGVKAQVDGDDLIIEGGGARGGATVATHMDHRLAMSALVMGLATETPVTIDDARFIDTSFPGFLPLMRGIGAAIEAAA | 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): 45982
Sequence Length: 445
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
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B7J781 | MTRYLVRPGSRLAGRFPVPGDKSISHRAVILGALAEGVTEVEGLLEGADVLATIAAFRSMGVQMEGPDKGHLRIHGAGLQGLRAPVVPLDCGNSGTAMRLLAGVLAGQPFPSTLVGDASLQKRPMGRILNPLRAMGAEIAAQDGRAPLHIHGRPLHGIDYALPVASAQVKSAVLLAGLYADGQTCVTEPAPTRDHSERMLQGFGQPVERHGPRACLRGGGRLCGQALQVPGDISSAAFFLLGATIAPGSDLTLEGVGINPTRTGIIEILTRMGARIDLTALREVGGEPVADIRVRYAPLQGIAIPPRLVPLAIDEFPALFIAAACAKGQTVITGAEELRVKESDRIAVMAGGLRALGATVEERVDGAIISGSALLGGRVDSHGDHRIAMAFAMAALVAQGDMEILDCANVATSFPSFPALAQQAGLLLEVASA | 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): 44810
Sequence Length: 433
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
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Q9YEK9 | MVWLRAPDRVVVHPSTVEGRVEAPPSKSYTHRMLFLALLARGRSVVRRPLVSNDTLATLNAVALLGGKPRLGRGVAEVEGGEVRGGAVVYAAGSGTTIRIAMGVAAHSAEATLLYGDESLNRRPVHPLSEALRSMGARVCDTGGNPPVKVSGPLRRASVEVDAAISSQFATSLLIAGSRLGEFELSAARLSSRGYVDITLESLSMFGVRVEREGYRLFRLRGTPKPVDAAVPGDYSSASFMLAAGAIAGRVEVEGLRPVDPQPDRRIVELLRSMGARVRVEGGVVAVESTGPLEPVDVDLDGSPDLAPVAAVLAAYARGVSRLRGLERLKYKESDRLSAIAWNLARLGVEARVRGGILEIRGGGVEGGVARSWGDHRIAMAMAVAGLGARRPVAVEGFSRVPDSYPGFLEDLARLGARVEAVKGGGV | 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): 44971
Sequence Length: 427
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.19
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Q9R4E4 | MSHGASSRPATARKSSGLSGTVRIPGDKSISHRSFMFGGLASGETRITGLLEGEDVINTGKAMQAMGARIRKEGDTWIIDGVGNGGLLAPEAPLDFGNAATGCRLTMGLVGVYDFDSTFIGDASLTKRPMGRVLNPLREMGVQVKSEDGDRLPVTLRGPKTPTPITYRVPMASAQVKSAVLLAGLNTPGITTVIEPIMTRDHTEKMLQGFGANLTVETDADGVRTIRLEGRGKLTGQVIDVPGDPSSTAFPLVAALLVPGSDVTILNVLMNPTRTGLILTLQEMGADIEVINPRLAGGEDVADLRVRSSTLKGVTVPEDRAPSMIDEYPILAVAAAFAEGATVMNGLEELRVKESDRLSAVANGLKLNGVDCDEGETSLVVRGRPDGKGLGNASGAAVATHLDHRIAMSFLVMGLVSENPVTVDDATMIATSFPEFMDLMAGLGAKIELSDTKAA | 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): 47588
Sequence Length: 455
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
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B2UN97 | MNLHSHSISSLQGALTVPGDKSISHRAAILGGLAEGVTEVDNFLCSEDCLNTLRAMEQLGAKVDVLEERQGYGPVRFRITGVAMSPKAPERPIDCGNSGTGMRLLAGMLAACPFDSEMFGDASLSSRPMGRIMQPLEQMGARIEARGAKPGCAPLSIHGGRVHPISYTLPMASAQVKSAILLAGMFADGTTTVRQPAVTRDHTERLFRHFGVPCTVDGLTVGTCGPALPVAHDLTVPADISSAAFWMVAAASRPGSRLTLRQVGLNKTRNAVISALQRMGARMDIVPTSPEDAGEPYGDITVYGSDSLHGTSLLPEEIPNLIDEIPILAVAGALGRGDFIVRNARELRVKETDRIATTAANLRLMGVDVEEFDDGMVVHGGTPLKGTELSSYGDHRIAMSFLVAGLSAQGETVVTDAECINTSYPGFERDLAQFL | 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): 46106
Sequence Length: 435
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
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Q8KB71 | MSTFQGEVTTLPPDKSISHRAALIGALAEGTTEISNFSGGYDNQSTLSVLRDAGISIRQEELSAGDGRIERRVVIESNGLWSFREPSVPLMCNNSGSTMRMMAGIMAAQPFRSELVGDASLMKRPMKRVADPLRQMGAEISLSDAGTAPVVIHGTKALKTIEYRLPVPSAQVKSLVAFAALHADGQSKIIEPIRSRDHTELMLGLATIDRPDGVREIIIDGRKPIAAKPFKVPADPSAACFMIALGLLGERSEIVLRNVCLNPTRVAYIDVLQEAGAGLGIENVRSEGGEPVGDIVVRSCSGLKPLRISDHGVVAGVIDEVPMLAVLSAFASGEFELHNAAELRTKESDRIDALVVNLQRLGFECEQYADGFVVKGRKTVASEEVEIECFDDHRIAMSFTIAAEAAGASLRLSDRDVAGVSFPNFFALIDSLRQ | 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): 46626
Sequence Length: 434
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
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O84371 | MVSSNQDLLISPSIPYGEIAVPPSKSHSLRAILFASLSKGTSIIENCLFSPDSQAMLTACEKMGAHVRRIGDSLHIQGNPDPHHCHPRYFHMGNSGIALRFLTALSTLSPTPTLITGSHTLKRRPIAPLLSSLKQLGAHIRQKTSSSIPFTIHGPLSPGHVTISGQDSQYASALAITAALAPYPLSFSIENLKERPWFDLTLDWLHSLNISFLRDQDSLTFPGGQSLESFSYSVPGDYSSAAFLASFGLLSSSSKPTILRNLSSQDSQGDKLLFSLLKQLGAHILIGKHHIEMHPSSFSGGEIDMDPFIDALPILAVLCCFAKNPSRLYNALGAKDKESNRIEAIAHELQKMGGSVHPTRDGLYIEPSRLHGAVVDSHNDHRIAMALAVAGVHASSGQTLLCNTQCINKSFPYFVIAAQTLHANVRHYQADFPLRSSFCR | 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): 47787
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
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Q8U0A0 | MLRIVPPKEIQGEVIAPPSKSYTHRGYFLSLLADEKSIVERPLISDDTLATIDAIRAFGADLIEEVVYPPEELRPNYIFARDSGTTARISIIVSSLAKGVSVIDGREQLRRRPMEDGVSSLRMIGVEAIGKRLPVKVFGRGRISAKEVSIVAEKSSQFATGFLILAAKIGLKVEIVKPVSKPYIEMTLKTMEEFGVKYDKAQENERLVIFVDPGVKGTKFKVPGDYSSAANFLVAGALYGKIRVRNLMRDDVQADKEILNILREYGAKVKVKDEYVEVESNERNPLNVDCSNFPDLFPLLAVLAAYAEGKSVIRGRQLRIKESDRIHAMAVNLSRAGIRVRELSDGLEIWGGQPKGFRGKTFNDHRITMALAILALGAKGESIIPETKSIAKSYPNFFEDLMRVIK | 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): 45068
Sequence Length: 406
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.19
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C0ZX05 | MDHVSLSLWSAPRAQAPVDAVVTLPGSKSITNRALILAALADGPSTITGALRSRDADLMIAALRDLGIGVEEAGDPTTLRITPGPLRGGEVDCGLAGTVMRFLPPLAAMADGIVRFDGDEQARTRPLGTILEALRGLGARIEGDALPFTVTGTGSLRGGTVTIDASGSSQFVSGLLLSAAAFEEGVTVHHDGKPVPSMPHIDMTVEMLRQSGVSVTTPATGGDADTWRVAPGPVRAVDWAIEPDLSNATPFLAAAAVTGGTVSVPMWPSSTTQPGDAIRGILASMGADVTLADGVLTVRGPEKLRGIDIDLHDVGELTPTVAALAALAEGTSHLRGIAHLRGHETDRLAALADEINKLGGSVTETDDGLTIVPAELHGGQWLSYADHRMATAGAIIGLVVDGVDVDDVGTTAKTLPGFENMWIDMLESSPATPKASF | 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): 44918
Sequence Length: 437
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
|
Q9YEJ9 | MAQAAVERRVFRLSVDEETVVAAGVGALSEAPRAAGGTAYIVHEEALSAEAARLARILEARGVEVLGAVAGGGERVKSLDWVTRLWDLMLQAGVERSTTVYIIGGGALLDAAGFAASTLMRGLSTVNIPSTTLAAFDAAAGGKTGVNLRGKNMVGTFHNPRMVLVEPGIVAGQPDEGYRDGFAELVKHVALSGDREPAASLLPQALARRPAPLARLAFWSLGYKMQVVAGDPRERGLRRILNLGHTIGHALEAASSYTLSHGRSVSIGLAGELELSRRLAGLPRGEAEDVLDMLSTAGLPLEPPPGLAGEAAGLVGLDKKREGGSIVMPLLERLGRPRLSRVPVETVSRLMVELWGGG | 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): 37446
Sequence Length: 358
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
|
Q5WGS7 | MFVDIHTSSKQYKAEVGSGILREAGKTIEALAPASSYLIVSDENVANRYLDVLVSSFSKEPHTFVVKAGEQSKSFHVYEQLAAFCLEKQLDRQSVIIAFGGGVVGDLAGFVAGTYMRGVRFIQVPTTLLAHDSSVGGKVAVNLPAAKNMIGVFHQPEAVLFDTELLATLPEHEWRSGFAEIVKLGFIADASFLAWLRETVPALTSIKADNLQKMVAKAIAIKADIVGKDEKEHGIRAHLNFGHTLAHAIEAELGYGKITHGEAVAIGMRFAFRLSLRFTKEDLRLADYEEWFSALGYDLRLPAGLSAQRLLARMKSDKKTNAGKIVMVLLAQLGAAYTKTVDEHLLLELLEEELGGRS | 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): 39100
Sequence Length: 358
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
|
A6TL07 | MEKLYINLDENSYWIYIGKGLLPTLGKHVAGADKILLITDENVEKYYGDQITQIVEGRILEKVILRPGEPTKNLGNVGHLLEIMLEKGLTRSSKVIALGGGVIGDIAGFTASIYMRGIDFIQVPTTLLAQVDSSVGGKTGVNLEQGKNMVGSFYQPKVVVIDIDLLKTLPHRELISGLGEIIKYGIIYDGEFFDYINENLWNLLALEETVVTKIIKRCCEIKAAIVSQDEQEMGVRKILNFGHTIGHGIEALTHYEKYTHGEAVILGMYYEAQIAKNRGYIDESYFRDIEMIIRKTGLDLNISQFILTDLLDAMTKDKKNKGGKISFILPRGKGNVQEVLLTPEELATFLYTYLYV | 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): 39846
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
|
A8MH15 | MLETKINLGKVTYPLYMGRNLLDNLDVLIEDHIEGKTVFLLTEDNVFKYYGNPLLEKLKSSRFKYHIIESGETSKSIDTYGEIIHELTENKQDRDTIILALGGGVIGDLGGFVASTYMRGVDLIHIPTTLLAQIDSSIGGKTGINFGAIKNLLGTFYHPRAVYMDLSTLDTLPKREYIAAFGEIIKYGLIGDYDLLLDLDQHHRAYLDRTRSVDDLILKCIRMKENIVLKDERDSGMRQVLNLGHTFAHGLESSTNFQKFLHGEAVALGLIFASNLSLKLKFIAEEYHQFVNQLIYKYFSDRYILQLDTEGIVEAMTMDKKNKEHRITFILPVDKEKVEIFKNIPIEIVEESLEEIKYGFRCK | 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): 41473
Sequence Length: 363
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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A0JX82 | MSSESTVIKVTGKSAADNYDVVVGRGLLGRLPELLGERVKRVLVIHPRALRLTGDTVRDELASAGFTALTAEIPDAEEGKHIQVAAFCWQVLGQNDFTRSDAVVAVGGGAVTDLAGFVAATWLRGVKVIHMPTSLLGMVDASVGGKTGINTAEGKNLVGAFHPPAAVLADLDTLSTLPKNELISGMAEVIKCGFIADPAILDLVEKDPSAVTDPQSAFLRELIERAIAVKADVVSEDLKETGRREILNYGHTLGHAIELVERYSWRHGAAVSVGMMFAAELARSVGRLSDADADRHRTILETLGLPITYRRDRWQGLLDGMRRDKKSRGDLLRFVVLDGIARPGILDVPDTSLLFAAYQEIAS | 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): 38981
Sequence Length: 363
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
|
A0Q706 | MISKLSVSPTFSPSYNIIVDSVLDFSHILEYVTNKQVLIVTNTTVAKLYLTKFLAALVDDLDVNTCILEDGEQYKSQQSLDKILSTLLENNFTRNSTVLVALGGGVIGDITGFAAAIYQRGVDFIQIPTTLLSQVDSSVGGKTAINHQLGKNMIGAFYQPKVVYTSIEFYKTLPQREYIAGMAEVVKYAFISKDFYLWLDSNRDKILAKDSVTLIEMVKRSCQIKAQVVAMDEKELTGARAILNFGHTFGHAIEKCQNYRGLKHGEAVGVGMAQAIDFSHYLGLISQQQAKDFKDFIVSFGISIDFPKDICQKEFLEAMLLDKKNSNKELKFILIENIGSLSLQKQSKNELEQFLDISR | 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): 40092
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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Q8RF47 | MKKIFDDIYVGSNIISKLNDYTEDFDKILIFSNETIADLYFEKFKSTLNEKDKVFYFAIKDGEEYKNIESILPVYDFMLENNFSRKSLIISLGGGVICDMGGYISATYMRGIEFIQVPTSLLAQVDASVGGKVAINHPKCKNMIGSFKNPYRVIIDVEFLKTLPKREFKSGMGELLKHSFLTKDKSYLEYIENNVEKIKNLDNEVLENIVEQSIRIKKHYVDIDPFEKGERAFLNLGHTYAHALESFFDYKAYTHGEAVSKGIIFDLELSLLRGQIDKEYLERARNIFKLFDIDTDLIYLPSDKFIPLMRKDKKNSFNKIITILLDSEGHLSKTEVKEDEIVKIIDKYKNNFLRASIDIGTNSCRLLIAEVEKDNENITFKKEIYKDLEIVKLGEDVNKNKFLKEEAIERTLKCLKKYRKIIDKYSIEEKNIICFATSATRDSTNKDYFIKKVFDETKIKINCISGDKEAYINFKGVISSFDRDFKDNILVFDIGGGSTEFTLGNMQGIEKKISLNIGSVRITEKFFLNNKLYNYSEENRIKAKDWVKENLKELEDFKKLNFSLIGVAGTTTTQVSVREKMEVYDSEKIHLSNLTSKEINDNLSLFIKNINKQEIKGLDPKRKDVIIGGTIILKEILDYFGKDFIIVSENDNLMGAILEGVENK | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 76592
Sequence Length: 664
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
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Q74BL6 | MTIETLRVELGERSYDIRVGSAIIGTIGAVCRDAVAGRRVAVVTNTTVGPLYADGVVDSLTAAGFTVLRIDIPDGEEHKTSVTLTSVYDELIKGGLTRDSLLVALGGGVVGDLAGYAAATYLRGVPFVQVPTTLLAQVDSSVGGKTGINHPLGKNLIGAFHQPRAVLIDVDTLATLPQREYLGGLAEVIKYGVVLDGKFFAFLEQNVSALLGRDRQTLVRAITRCCALKAWVVEQDERETGLRAVLNYGHTFGHAVEALTGYTAVLHGEAVAIGMVRAAVLAEARGHSSAGDTRRIRALVEALGLPTELPSFDADSYRDVLLRDKKARDRGLDFVLNRGIGGHEIVRIENLSEVFGICGVGE | 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): 38488
Sequence Length: 362
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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P43879 | MLCVNVELQERRYPILIGSGLLQDERSYPIKRGDRVMIVTNPTVAQFYLDTVIYALEKRGCVVDHVLLPDGEKYKTLESLNLIFTALLQGNHGRDTTIIALGGGVIGDVAGFAAASYQRGVRLIQIPTTLLSQVDSSVGGKTAVNHELGKNMIGAFYQPSMVIIDTLTLNTLPKREVNAGLAEVIKYGAILDYEFFEWLEQHIDELVALHPEALQHCISRCCQIKADVVARDETEKGDRALLNLGHTFGHAIETHLGYGNWLHGEAVSTGMMMAAALSEELGDISIADVSRLEKLLARANLPTVSPDTMQPEDYLPHMMRDKKVLSGKLRLVLLKSLGQAYVANDTEHTLVLNAIRRCTQTD | 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): 39919
Sequence Length: 362
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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Q5XAW2 | MPQTLHVHSRVKDYDILFTDHVLKTLADCLGERKQRKLLFITDQTVYHLYQTLFEEFAQQYNAFVHVCPPGGQSKSLERVSAIYDQLIAENFSKKDMIITIGGGVVGDLGGFVAATYYRGIPYIQIPTTLLSQVDSSIGGKVGVHFKGLTNMIGSIYPPEAIIISTIFLETLPQREFSCGISEMLKIGFIHDKPLFQQLRDFQKETDKQGLERLIYQSISNKKRIVEQDEFENGLRMSLNFGHTLGHAIESLCHHDFYHHGEAIAIGMVVDAKLAVSKGLLPKEDLDSLLQVFERYQLPTSLERADVSATSLFDVFKTDKKNSEQHIIFILPTETGFTTLAINKDDHQFVEKLDSLL | 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): 40343
Sequence Length: 357
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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Q8R9A6 | MRYLTAGESHGEALIAIIEGLPSNLFIDAEFINKELERRQKGYGRGGRMAIEKDEIHIISGVRDGKTTGAPLAMEIKNRDYKNWKDKKVPPVTRPRPGHADLPGSIKYNQRDIRNILERASARETAARVAVGSVAKLLLKELNISLKSRVLEIGGAKREEKWKRLIEKAKKEGDTLGGIIEIVIEGVPVGLGSHAQWDRKLDALLAYHVMSVQGIKGVEFGLGFEAARLPGSLVHDDIYYKENEGFYRKTNNAGGIEGGMSNGNPIVIRAAMKPIPTLLRPLDSVDIATKEETKAIYERSDVTAVEAAACVLEAVCAWVIADECLKKFGGDSVEELKRNYDTYLAYVRSF | 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): 38673
Sequence Length: 350
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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B9KE09 | MNSFGIRFKFTSFGESHGQAIGCVIDGMPAGVKFDFDFLQEMLDKRKPGQNKFSTPRKEEDKAQVLSGVFEGYTTGTPISVLVYNENTRSKDYEKDVFRPAHADFTYYHKYGIRDYRGGGRASARESIARVAAGALAQMLLKEFDIEIMSGVFGVGSIDSKLSNDEFDFNCAKNSEVYALDKNLEQSFKDEILKAKKAKDSIGARVFTRVKNPIKGLGEPLYDKLDSKLAHAIMGVNAVKAIEIGSGIQSSYMYGSQNNDELKDGVFLSNHSGGILGGISNGGFIDIKTYFKPTPSIFLPQQTQNIQGENIIRELKGRHDPCVGIRGSIVVNAMVAICMADALLLNASSNLQNLQRVYGKNK | 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): 39824
Sequence Length: 362
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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Q05FR1 | MNNSYGEIIKISTFGESHGLIIGALIDGFFSNLYISEKFIQKNLNLRKPFTSLFSTQRREQDKVKIFTGIFKNKTTGAPVLMLIKNNDKQSSDYNNISLNFRPGHADYTYFLKYKFRDYRGGGRSSARETACRVASGCVFKNLIYNKGVIVRSYIKKIGFLKINFKYWNYTLNRFFSNLLFINEIKDIINNCKNSCNSLSSEIVIIINGLEPSLGDPLYKKINSTISNYLLSINATKSICFGFNFKNKNSFQVKDEIKNSGFTSNNNGGILAGITNGQPLVIKILFKPTSSTSRKIKTINEKLKNITNKTYGRHDPCVGLRAVPVIESMLYTILINKILKKKIYE | Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Mass (Da): 39214
Sequence Length: 345
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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P36923 | MKPVIVKNVRIGEGNPKIVVPIVAPTAEDILAEATASQTLDCDLVEWRLDYYENVADFSDVCNLSQQVMERLGQKPLLLTFRTQKEGGEMAFSEENYFALYHELVKKGALDLLDIELFANPLAADTLIHEAKKAGIKIVLCNHDFQKTPSQEEIVARLRQMQMRQADICKIAVMPQDATDVLTLLSATNEMYTHYASVPIVTMSMGQLGMISRVTGQLFGSALTFGSAQQASAPGQLSVQVLRNYLKTFEQNK | Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids (AroAA). 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): 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
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Q5KY94 | MNISPKAIKVRNIWIGGTEPCICAPVVGEDDRKVLREAEEVCRKQPDLLEWRADFFRAIDDQERVLATANGLRNIAGEIPILFTIRSEREGGQPIPLNEAEVRRLIEAICRSGAIDLVDYELAYGERIADVRRMTEECSVWLVVSRHYFDGTPRKETLLADMRQAERYGADIAKVAVMPKSPEDVLVLLQATEEARRELAIPLITMAMGGLGAITRLAGWLFGSAVTFAVGNQSSAPGQIPIDDVRTVLSILQTYSR | 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): 28564
Sequence Length: 257
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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A8MCY4 | MHVFGLIGYPLNYTLSPQIHNYVFKRLRIDAAYVPLRVASKRLLHFIEFSRDALSGFNVTIPHKVAVAKLIDELNDDADTIKSVNTVVNSNQKLIGYNTDYVAVEESLIERGYKGEEALLIGAGGAARAVVLALSKTGCRAIKVLNRSRERAVELCGLANGLGLDCSVVDIGGNYGKPHVIINATPLSSEEYWLLNLGELGTMLLLDMAYKPNTETDLIKRARELGIQVIDGVEILVRQALAADKLWLGDFNEPSASEVIKYIKGINPS | 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): 29480
Sequence Length: 269
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
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Q8RAG2 | MKIDSTTKVFGLIGHPVKHSLSPLIHNSSFEKLNFNGVYVVFDVAPELLENAVKGLKALGIKGFNVTVPHKESVMNYLDFVTEEAEKIGAVNTVVNENGILKGYNTDVQGFIDSLKELKEDVRGRKAFVLGAGGASKAICFALAREGVESIVIANRTLNKAKALAEYIREEFKMKCDYCSIEEVEKFNEIDILINTTSVGMHPEVGNSPVSEEVVAKANFVYDLIYNPSETLFLKYARKNGVKSANGLSMLVNQASYAFYLWTGEFFDKDFVYEKIRGEM | 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): 31107
Sequence Length: 280
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
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Q3AEF5 | MRINGETKLTGIIGYPLKHTLSPQMHNEAFKALNLNFLYLPLEVAEESLPQAIYGLKAFNFRGINVTIPYKEKVFPFLDEVATEAKTIGAVNTIVHDRGRLIGYNTDAPGFLLSLKENDVEVTGKKVLLLGAGGAARAVAYALLTAGAELIIANRTIDKAKELAKDFQGVGKISEILELGDKPISLAPYHMAVNTLPLGMHPYENQMPAVDFTGVTSDFVAYDLIYNPAETKFLKASKEKGARTINGLSMLLWQGVLAFEKWTGVSPPVKVMKKAIGLSC | 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): 30495
Sequence Length: 280
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q9AC57 | MTNAITGAAIVGGVCGQPIKHSMSPVIHNAWIAAAGLDAAYVPFAPAADRFETFVDGLRGGAVRGLNVTIPFKERALAVADTASDLARMAGAANLLVFNEDGSVHADNTDGPGLLGAIAIQAPGFDVTAAPVVILGAGGAARGAVAALLLAGAPRIAVVNRTVARAQDLADTFGEKVVAKGEDALPALLPEAGLIINATSLGLGGGAGPSADLTLTPKTAVVMDMVYKPLRTEFLRRAEAAGRRTVDGLEMLLRQAIPTFETIYGQAPSPKIDVRVLALKLLGEV | 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): 29015
Sequence Length: 285
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
B3PGZ3 | MTDLYAVFGNPINHSKSPSIHRMFAEQTGQDLHYTKQLVDVDKFAQTADAFFAQGGRGLNITVPFKQEAFRYAHSLTPRAERAGAVNFLVQLSDGSIRGDNTDGIGMVHDMHNLDWNIAGKRVLLLGAGGAVRGVLQPLLEEHPAQVVIANRTLSKAEELAKNFLDLGNVEAKGYDQLNGAHFDIVINGTSASLHGELPPLPDNLLNPGACCYDMMYGAEPTVFLQWAQQQGAAHTADGLGMLVGQAAEAFYLWRQIRPEVVPVLTALRRQLHEKK | 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): 30195
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
|
Q3IYG9 | MTELTRIPLAGVIGSPIAHSRSPALHGYWLKRYGLKGHYIPMDVAQADLRDVLAAMPRMGFVGCNVTIPHKESVIGLADIVTDRAALIGAANTLIFGKDGKIHADNTDGTGFTANLRQNAPAWQPQSGPAVVWGAGGAARAVIAALIEVGVPEIRLANRSRARADALRSDFGAKVHVHDWVQAGNILEDAMTVVNTTSLGMVGKPEFRVPLDALNPKAVVTDLVYAPLRTRLLVEAEAAGCRTVDGLGMLLHQAAPGFERWFGVRPEVDEETRAAVLAT | 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): 29715
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
|
Q8KBH8 | MSNSQSKKIFGLIGKHVDYSWSPLIHNTGFEALGLPCVYTIFNIPSPEMIGDALKGSRALGIAGFSVTIPYKKTVVPFLDELSPEALSIGAVNTIVNDNGRLLGYNTDIDGFAAPLLPMAESIRNRPVCIFGNGGAALAAVEAFRLRFNPSSVLLVVRDTQKAEDMLEEYAYRDLVTIHAGREIDQPACSKLIRDCRVLVNATPVGTAGRNDHIHSILPTGHGLLHDGQIVYDMVYNPPETPLLAEARAAGATVIAGIEMLIAQAARAFSIWTGQELPVDLVRKTVLAAIEKSEG | 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): 31734
Sequence Length: 295
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q7NS40 | MTDRYAVIGNPISHSQSPFIHEEFARATGQDISYERLFADIGRFNDVVGEFVASGGKGLNITLPFKGDAFRYASELTERARAAEAVNTLTFRDGKVYGDNTDGVGLVRDIVENLDYPIVGRRVLILGAGGAVRGVLEPILEQKPASLTIANRTVIKAEALAHHFARYGKVEAVGYAALEGRSFDIVINATSTSLNNEMPPLPHGVFTPRTLAYDMVYSTGLTPFLQRAQGENAGMLADGLGMLVEQAAESFSIWRGAQPETRKVTNMLREVLA | 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): 29650
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
|
A2BZ92 | MITSNTSFLALIGNPVSHSLSPIMQNAAIKYLGLDLIYIAIPCKNEDLEIVVNSLKKMNCKGLNITIPFKKKVFDLCSEISPVAKKIQAINTLKLKNDNNWSGTNTDIEGFIYPLKNLNLTNKNSIILGSGGAARSVIQGLIDLKLSKITIISRNNNSLNELITLFKNDIKIEGILNTNDEIGNLIEETDLIVNTTPIGMSQTSDNDAIPFGQSSWETIDSNTIVYDLIYNPSPTPFLKFCDRKGCMTIDGTQMLIAQGAKSLSFWTNGLEVPFEVMHDALKKYL | 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): 31448
Sequence Length: 285
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
B4F1M1 | MEKYVVMGNPIEHSQSPFIHQLFSKQSGIDYEYGRLLVPLGEFDKVATQFFSQGGRGANVTVPFKEDAFRFVDKLTQRAQACGAVNTILKLDDGTLLGDNTDGQGLILDLARLDFIIPGKILSVLVIGAGGATRGILLPLLNYNCDITLTNRTVEKAQQLAQEFSQFGTIRASAPQNVTDKHYDLIINASSSSMTDDIPPIPDSAYGFKTACYDLYYKAGMTSFLYHALKNGSTRLSDGLGMLVGQAAYAVELWYERVPDINPTINILRENLNK | 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): 30127
Sequence Length: 274
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
P43904 | MDRYCVFGNPIGHSKSPLIHRLFAEQTGEALVYDAQLAPLDDFPGFARRFFEQGKGANVTVPFKEEAYRLVDELSERATRAGAVNTLIRLADGRLRGDNTDGAGLLRDLTANAGVELRGKRVLLLGAGGAVRGVLEPFLGECPAELLIANRTARKAVDLAERFADLGAVHGCGFAEVEGPFDLIVNGTSASLAGDVPPLAQSVIEPGRTVCYDMMYAKEPTAFNRWAAERGAARTLDGLGMLVEQAAEAFFLWRGVRPASAPVLETLRRQLATV | 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): 29485
Sequence Length: 274
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q3IDI6 | MDKYAVFGNPIKHSKSPAIHKQFAISLGEQIDYRAILAPIDNFEKTVSNFFAQGGKGANVTMPFKEQAFAMADELTPLAKIVGAVNTLKKQADGTLLGDNTDGIGFVSDLLANNVSITGKRILIIGAGGAARGVVLPLLDHQPQEVVIVNRTAEKAQNLAKLFAQHGNVSGYGFNNLPENDYALIINSTSSSMNDELPALDQKHITNCEVAYDMFYSLQNTIFMNWVAQYNSKTKLLDGSGMLVGQAAQAYYVWRNKMPAILPVVNALKQGALT | 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): 29680
Sequence Length: 274
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q4FVE5 | MTQHFIVIGNPIAHSKSPEIHTLFGAHAGLDICYQCQYCPDDPASFTAVIEAFFHGGGVGANVTVPFKQVAYECCAARGGLSEHAKIAGAVNTLSLNQALLASGVSRAEALYGDNTDGQGLVNHMQRLGWPLNGARIAIIGAGGAARGVVLPLIEAGIEALTIANRTLSKATELVNELSTASVVIHNQQIQTCCTADLSGDFDIIVNATSIGLSGETLPLADELNCQYAYDMMYGRELPFLQHFAARGAQTSDGYGMLIGQAALSFECWTGHAIDVTQATAALEKSSI | 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): 30240
Sequence Length: 288
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q8ZW89 | MYFAVIGAHVRGKSASPAMHTASFKALGINAVYIAVDVPKEELGCFAQIARLNFRGFNVTIPHKEEVVKFLDALSAEARAIGAVNTVLVERNLMVGYNTDAHAVYKLAGGHMEGAEVLILGAGGAARAALFAAIKAGAKKIYVKNRTAERAEALAREFREKFERPIEAIPWSGAVKADVVINATPIHDAVIADLTGASLYVEFVYTPTPRTKMVEEAERLGVKVVDGVDLLVEQGAQAEKIWLGVEPDRAVMKKAVLEFLGL | 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): 28185
Sequence Length: 262
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
|
Q75W16 | MALATNSAAVSGGAAAAASSAPQPRLAATFLPMRRRTVSAVHAADPAKSNGPVQAAAKASSPSTVAAPEKKPVGLGKWTVDSWKAKKALQLPEYPSQEELDSVLKTIETFPPVVFAGEARHLEERLADAAMGRAFVLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVVKVVGRMAGQFAKPRSDSFEERDGVKLPSYRGDNINGDTFDEKSRVPDPQRMIRAYAQSVATLNLLRAFATGGYAAMQRVTQWNLDFMDHSEQGDRRYRELAHRVDEALGFMTAAGLTVDHPIMTTTDFWTSHECLLLPYEQSLTREDSTSGLFYDCSAHMLWVGERTRQLDGAHVEFLRGVANPLGIKVSDKMNPRDLVKLIEILNPSNKPGRITIITRMGAENMRVKLPHLIRAVRNSGQIVTWITDPMHGNTIKAPCGLKTRPFDSILAEVRAFFDVHDQEGSHPGGIHLEMTGQNVTECIGGSRTVTFDDLSDRYHTHCDPRLNASQSLELAFIIAERLRRRRMRSGVNSNLPLPPLAF | Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Mass (Da): 59334
Sequence Length: 539
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
|
Q9UT09 | MSPVFLPSGETYDQEHLDDNRVLGYNPLVPAALVQQEIPVSETSRKVITDSRKEIQAILNKQDDRIIVVVGPCSIHDPKLAMDYAKLLKPKADELQDALCVVMRCYLEKPRTTIGWKGLVNDPNLDGSFAINKGIRMARQMYCDVTNFGIPLASEMLDNISPQFFADLLSFGAIGARTTESQLHRELASALSFPVGFKNGTDGTVGVAIDAIGATAHPHTMLGVTKQGLAAITMTRGNKDTFIILRGGKKGPNYDAEHVAAVRKDLEKANLPPRIMIDCSHGNSSKNHLNQPKVSKSIAEQIRNGDSSIVGVMIESHINEGRQDAPIRPGVKDTLKYGVSITDACVSWEQTAPMLDDLAEAVRARRQNQKSN | 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): 40638
Sequence Length: 372
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Subcellular Location: Cytoplasm
EC: 2.5.1.54
|
P32449 | MSESPMFAANGMPKVNQGAEEDVRILGYDPLASPALLQVQIPATPTSLETAKRGRREAIDIITGKDDRVLVIVGPCSIHDLEAAQEYALRLKKLSDELKGDLSIIMRAYLEKPRTTVGWKGLINDPDVNNTFNINKGLQSARQLFVNLTNIGLPIGSEMLDTISPQYLADLVSFGAIGARTTESQLHRELASGLSFPVGFKNGTDGTLNVAVDACQAAAHSHHFMGVTKHGVAAITTTKGNEHCFVILRGGKKGTNYDAKSVAEAKAQLPAGSNGLMIDYSHGNSNKDFRNQPKVNDVVCEQIANGENAITGVMIESNINEGNQGIPAEGKAGLKYGVSITDACIGWETTEDVLRKLAAAVRQRREVNKK | 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): 39749
Sequence Length: 370
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
|
P19080 | MMIRGIRGATTVERDTEEEILQKTKQLLEKIIEENHTKPEDVVQMLLSATPDLHAVFPAKAVRELSGWQYVPVTCMQEMDVTGGLKKCIRVMMTVQTDVPQDQIRHVYLEKVVVLRPDLSLTKNTEL | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 14517
Sequence Length: 127
Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.4.99.5
|
P00887 | MNRTDELRTARIESLVTPAELALRYPVTPGVATHVTDSRRRIEKILNGEDKRLLVIIGPCSIHDLTAAMEYATRLQSLRNQYQSRLEIVMRTYFEKPRTVVGWKGLISDPDLNGSYRVNHGLELARKLLLQVNELGVPTATEFLDMVTGQFIADLISWGAIGARTTESQIHREMASALSCPVGFKNGTDGNTRIAVDAIRAARASHMFLSPDKNGQMTIYQTSGNPYGHIIMRGGKKPNYHADDIAAACDTLHEFDLPEHLVVDFSHGNCQKQHRRQLEVCEDICQQIRNGSTAIAGIMAESFLREGTQKIVGSQPLTYGQSITDPCLGWEDTERLVEKLASAVDTRF | 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): 38735
Sequence Length: 348
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
|
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