ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B8D2C6 | MFDNSTQVVGLMGYPLGHSMSPAMHNRAYKDLGINYVYLPLEIKPDFLKEGIEGLRAFNFRGVNVTIPYKEKVIPYLDEIDRLAGEIGAVNTIVNNGGKLKGYNTDALGFKKMLEDDCSFEIKGTKAVIIGAGGASRAVGAVLAREGASEIFLLNRTLKKAAKLVGIWNKTYPGIKTVALPLDEDKYLPVVKRCDVIIDTTPVGMAPGIKGGPVIAKEAITRDTLVVDLVYNPPETTLIKAGRQVGARTMNGFPMLIYQAAYAFKLWTGIKPELFIKPVREAISPDFFA | 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): 31542
S... |
A0LLU7 | MIKPVQTELYAVIGNPVAHSLSPVMMNAAFRSMNVPATYLALQADELPEDLETLARFGFRGLSVTLPHKELAYRLADHVDDMARTIGAVNTLMREGSAWIGCNTDWLGATKALRRVTELEGREALILGAGGAARAVAFGMKREGARVTIANRCVEKGKALAKSFRCDFIPLAILDRARFDRHFDVVVQCTSVGLQGTIPTVLVSDSFFEPGMVVMETVYRPLRTPFLNAAKRAGATIVHGTDMLVYQGVAQLEWWLSRPIPEFPCVAAMKQAIHEVLSKEKNAQDD | 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): 31400
S... |
Q0AZJ6 | MPLDIKTELMGLIGYPLQHSLSPLMHNLTLKKMGLNCIYLALEIEEGKLPEIPSAIRTLNFRGLNVTIPYKEKIIPFLDELSPEAAAFGAVNVIKNKNGHLHGYNTDGRGFVEALREEGIDPGERALFIGAGGAARSVAFALAGLGVSRLDFLDLDFSRARQLAEFITSRSSSLASAFLMNTLEFQRLSRTASIIINCSPVGMFPDTGKSPVSKEDLRGSRAVLCDLIYNPLQSRFLSLGQELGLETMNGLGMFVQQGALTLEILLGQKPPLDYMKEVVQNQLEKRVDPD | 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): 31793
S... |
P74591 | MPSITGKTKLLGVIGYPVGHSLSPVMHNAALQAMASDYAYVAFPIAPEDLTIAIAGLGASGVQGLSVTIPHKQVVMPLLTQITETARQVGAVNTLWRDGHGWQGTNTDVEGFLAPLLELKQDWSGRTAVILGYGGAARAVVVGLTQLGCPEIIVVGRSQEKLAQFANSWTDPKIKQALQVLPWEALSTVIPKASLLINSTPVGMAPHPKQSPLDQSLVEKLPPTAIAYDLIYTPRPTRFLQHAQERGLVTIDGAEMLVQQGAAALKIWLQQEVPVDVMRQALLHHLEKSA | 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): 31099
S... |
Q9HLE4 | MNGNSIIGLIGHPVSHSIGQILYNRIFQDMGIDAFYLAMDVHMNVLPAFLKNSFFLKAFNVTIPHKVSIIPFLDDLDEIASQTRSVNLVIREQSRMKGYNTDYYGLDYALSFNQVEIEEKRIVIAGSGGIARTVIRYMLDHGAHRVDVLTRNAQNARRNLDIPGIGLHENIDEDYDIYVNCTPLGTLGDGDPFSTVDFRSGRTGIDLVYNPPDTPFLKRMRNAGGRTVSGLDVFIGQGLRTLELVFGIRPDSIFREYAVEALNEIRKG | 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): 30013
S... |
Q5JFT1 | MADAETRLYGVIGFPARHSLSPVMHNAAFRALGINAVYLAFEVPPEELGEAIGGAKALGISGLNVTMPHKEAVIHFLDSLSEDSGEIGSVNTVVNRKGRLEGHTTDGLGARRALERAIELGGRRILIIGAGGAGKAIAYELSRDNEVVVLNRTPEKAKALERFGITGDALNRENLGEYLEWAEVLINATSVGMNSWETPVPAELLRRDLVVMDIVYKPLKTRLLTEAELRGCKTVDGLWMLVYQGIESFRLWTGFKPDEGLMRGAALEGISE | 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): 29522
S... |
Q9WYI1 | MKFCIIGYPVRHSISPRLYNEYFKRAGMNHSYGMEEIPPESFDTEIRRILEEYDGFNATIPHKERVMRYVEPSEDAQRIKAVNCVFRGKGYNTDWVGVVKSLEGVEVKEPVVVVGAGGAARAVIYALLQMGVKDIWVVNRTIERAKALDFPVKIFSLDQLDEVVKKAKSLFNTTSVGMKGEELPVSDDSLKNLSLVYDVIYFDTPLVVKARKLGVKHIIKGNLMFYYQAMENLKIWGIYDEEVFKEVFGEVLK | 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): 28889
S... |
Q5SJF8 | MLRFAVLGHPVAHSLSPAMHAFALESLGLEGSYEAWDTPLEALPGRLKEVRRAFRGVNLTLPLKEAALAHLDWVSPEAQRIGAVNTVLQVEGRLFGFNTDAPGFLEALKAGGIPLKGPALVLGAGGAGRAVAFALREAGLEVWVWNRTPQRALALAEEFGLRAVPLEKAREARLLVNATRVGLEDPSASPLPAELFPEEGAAVDLVYRPLWTRFLREAKAKGLKVQTGLPMLAWQGALAFRLWTGLLPDPSGMEEAARRALGV | 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): 28284
S... |
Q8DLA6 | MPKISGQTQLLGVIGDPIEHTLSPAMHNAALEYLGLNYVYVPFWVKPQQLGVAIAGLEALNVVGFNVTIPHKETILPYLADVSDLAQQVGAVNTVYRSEKGWVGTNTDVHGFLAPLRQQSCLWSEIAVLVLGYGGAARAVVTACYDLGCRQIYISGRQRERLGAFVASWPQITLHPLLWSERATCLAKISLVVNTTPIGMSPHTGATPLTAEDLAKLPATAIVYDLIYKPRPTLLLQLAMARGLQTFDGLAMLLHQGAAALEYWLGQPAPTAIMATALETALGTEK | 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): 30796
S... |
Q978S5 | MMPPDYVFGLIGHPVSHSIGQIVYNRYFQKKGLNAIYLSIDIFPETLKYFMSYASKMDGFNVTIPHKISIMDYLDQIDWEARSIGSVNLVKTEDGLLKGFNTDYYGIEYMFKKGGVDVSGKSIVVAGSGGIARTVIHYLIKNNAKSVTVKARDVKLAKNKLNAYDVDIKEYANNDYDIYINCTPLGTEAVGDPFPEVQFGKGKIAVDVVYNPPVTPFLKRAGISGSKTLSGLDLYIGQAIKTLDILTSGCDIDTLINSVRVAVNEVR | 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): 29461
S... |
B5YJ55 | MITGKTKIIGIFGDPIEHTLSPLIHNEAFSYLGLDYCYVAFNVKKDKLKEAVEAIRALNIRGVNITVPHKETVIQYIDELSDEVKNIGAVNTILNNEGILKGFNTDVNGFILSLKDEGISMKNKNFLILGAGGAAKAIVYGILKEGGKVYIYNRTPSNALAIKEKFKKFGFIEIVEMDKSVTEKIDVIVNATSLGLKKDDPMPLNPELIKPEHVYCDIVYPETPLMREAERIGCKVVGGIGMLLWQAAFAFKIWTEVEAPIEIMKKTLNKLLTKD | 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): 30561
S... |
B8GTG2 | MDKYAVIGHPIGHSKSPRIHALFAGQTGQDMAYEAVFAPLDGFADTVRRLVAEGYRGFNVTVPFKGEAFKLADALTDRARCAGAVNTLKVQDDGTLLGENTDGAGLVTDLVNNLGVAIAGRDLVVLGAGGAVRGVLAPLLALGPASLHIANRTGARAEQLARDFADLGPVTGGDLDSLMGRQAHVLINGTSAGLDDEVPPLPDDLLHADGGCYDMMYGDRPTAFLRWAAAHGAAWTADGLGMLVEQAAESFALWRGVRPQTGPVIQILRPVQP | 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): 28540
S... |
B9MKD6 | MKNIVLTGFMGSGKTTIGKLIAEKLDIELIDTDSEVIKEFGMTIDKIFEVHGEKKFREVETKVIERVSKLENVVISTGGGVVLNPENVKLLRENGVIYFLYAPAESILKRLKDDDTRPLLKNGDKLSNIIRLLNMRMPFYKNCDFEINTDILTPELAAEKIISIHLAKESKR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19480
Sequence Length: 172
Pathway: Metabolic intermediate biosynthesi... |
Q8RAE8 | MKNIVLTGFMGTGKTTVGKKVATTLHFNFIDTDKLVEKMAGMSVAEIFEKHGEEYFRKLEKAAVIKASRLKNHVIATGGGVVLNPSNIVQLRKNGVIILLKARPEVILRNISKTKDRPLLAVEDPEKRIRELLEEREPFYRFADYTIDVSDKTIEEVAEEVIRAYIKLKGR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19369
Sequence Length: 171
Pathway: Metabolic intermediate biosynthesi... |
A4XLN3 | MKNIVLTGFMGSGKTTIGRLVAEKLNIDLVDTDSEIIKEFKLTIDQIFEIHGEKKFRECEKRVIERVSKLENVVISTGGGVVLDPENVNLLRKNGVIYFLYASPENILKRLKDDNTRPLLKNGDKLSNIIRLMNIRMPFYKNCDFEINTDILSPELAAEKIISIHMAKESKR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19637
Sequence Length: 172
Pathway: Metabolic intermediate biosynthesi... |
Q9A435 | MTETDQTPDTAPEAAPEVAPIVSDDLAPLRAKTIVLVGLMGVGKSSVGRRLANVLGLPFRDADNEVEAAAGRSISEIFAELGEPAFRDGERRVIARLLDEPPHVLATGGGAFVNAETRALINEKAVSVWLKADVELLARRVSRKDNRPLVRGKDPVKVLTELAEARYPAYAEAQVHVETGDTPHMVAVEAILTALRQAHA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 21439
Sequence Length: 200
Pathway: Metabolic intermediate biosynthesi... |
Q3J2I9 | MKVGAEVRRRGNREDGRQVMARLKKTVVMVGMMGAGKTAVGSALARGLNVPFLDSDEEIERAANRTIAEIFARDGEPFFREKESQVLARLLRGSPCVLSTGGGAFMAEGNRRMIREQGVSVWLKADLDVLWHRVRHKATRPLLRTPNPRETLRALLEARDPVYAQADLAVESGEGTVEQMAVRVREALATRPDVLETDE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 22077
Sequence Length: 199
Pathway: Metabolic intermediate biosynthesi... |
B3EPX3 | MKHPSLIFLTGFSGSGKSTIGPLLANSLGYDFLDLDKEIERQADKPITRIFAEEGEDHFRERERAMLESIVGRKELVVSLGGGALQNNDCFSLIISSGTMVYLHSSPLILAKRMSHKTDRPLMKGENGERLSSEEIEKKILALLEHREPRYKTAQIMVETDTKRIGTTVEELTRKIERYVRRAEKNQNSHSQTKKQSRK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 22643
Sequence Length: 199
Pathway: Metabolic intermediate biosynthesi... |
Q9Z6M1 | MTIILCGLPTSGKSSLGKALAKFLNLPFYDLDDLIVSNYSSALYSSSAEIYKAYGDQKFSECEARILETLPPEDALISLGGGTLMYEASYRAIQTRGALVFLSVELPLIYERLEKRGLPERLKEAMKTKPLSEILTERIDRMKEIADYIFPVDHVDHSSKSSLEQASQDLITLLKS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19631
Sequence Length: 176
Pathway: Metabolic intermediate biosynthesi... |
Q8KCL0 | MKHHSLIFLTGFSGSGKSTIGPLLANSLGFEFIDLDREIELTAGKSINRIFAEDGEAAFRSLELRTLEKIGQQERMVVSLGGGVLENDRCFELIRSHGTLIYLKSSPEILTLRLQHKTDRPLLKGPDGRKLTREEIQQRIAELLKKREPRYLKADLVLFTDSKKIGASVEELTRKIERHIRRASKNNTNEK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 21695
Sequence Length: 191
Pathway: Metabolic intermediate biosynthesi... |
O84372 | MPTFDTTKQIFLCGLPSVGKTSFGQHLSQFLSLPFFDTDHLLSDRFHGDSPKTIYQRYGEEGFCREEFLALTSVPVIPSIVALGGCTPIIEPSYAHILGRNSALLVLLELPIATLCQRLQHRSIPERLAHAPSLEDTLSQRLDKLRSLTSNAFSLRAETSSEAVMRDCQSFCLRFLSTKESSYA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 20512
Sequence Length: 184
Pathway: Metabolic intermediate biosynthesi... |
Q8XV61 | MSVSNVFFVGLMGAGKTTVGRAVARRLDLPFFDSDHEIEARCGVRVPVIFEHEGEMGFRDRETQMIDELTARHGVVVATGGGAVLRPENRAFLRERGTVIYLRANPHDLYLRTRHDKNRPLLQTENPRARLEELHAIRDPLYREVAHFVIETGKPTVAQLVNMVLMQLEVAGIVVPPAASSPTSQVSRQS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 21220
Sequence Length: 190
Pathway: Metabolic intermediate biosynthesi... |
Q98FY0 | MNAHQANPPGESLAALLGRLGSRSIVFVGLMGAGKTAIGRKVATMLSLPFIDSDQEIESVSRMTVPELFERYGEAEFRALEQRVILRVLENGPQVLSTGGGAFMNAQTREAIAGHGVSVWLKAELDLLMDRVSKKQNRPLLKSADPRAVLERLMSERYPVYATSDVTVPTRDDRKEVIAAEVLNALCRHFGIDEIAATGEIES | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 22161
Sequence Length: 203
Pathway: Metabolic intermediate biosynthesi... |
Q32JD7 | MTQPLFLIGPRGCGKTTVGMALADLLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTAPSTVIATGGGIILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEEDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNEPSQVISEIRSALAQTINC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19177
Sequence Length: 174
Domain: The LID domain closes over the acti... |
Q46065 | MAKSNEGLGTGLRTRHLTMMGLGSAIGAGLFLGTGVGIRAAGPAVLLAYIIAGAIVVLVMQMLGEMAAARPASGSFSRYGEDAFGHWAGFSLGWLYWFMLIMVMGAEMTGAAAIMGAWFGVEPWIPSLVCVVFFAVVNLVAVRGFGEFEYWFAFIKVAVIIAFLIIGIALIFGWLPGSTFVGTSNFIGDHGFMPNGISGVAAGLLAVAFAFGGIEIVTIAAAESDKPREAISLAVRAVIWRISVFYLGSVLVITFLMPYESINGADTAAESPFTQILAMANIPGTVGFMEAIIVLALLSAFNAQIYATSRLVFSMANRQD... | Function: Permease that is involved in the active transport across the cytoplasmic membrane of all three aromatic amino acids, phenylalanine, tyrosine and tryptophan.
Catalytic Activity: H(+)(in) + L-phenylalanine(in) = H(+)(out) + L-phenylalanine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): ... |
C4Z158 | MKILVMNGPNINFLGIREKGIYGEQNYEALVSMIQKKAEELGADVEVFQSNHEGAIIDKIQEAYYNDVDGIVINPGAFTHYSYAVRDALASVAAIPKIEVHISNVHTREEFRHTSVTVPVCNGQVVGLGLKGYLYAMEAVVDLAMKK | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16213
Sequence Length: 147
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step... |
B1XX46 | MNILVLNGINLNMFGKRDPKQYGTITLAQIDEQLDALGAELGATVQHFQSNHEGEMAERIHQAHVDNVDAVLINAGAWTHYSYGIRDALAILKCPIVEVHMSNIHAREPFRHHSVIAEIARGQIAGFGVDSYLMGLRAAVNLVNAAKAG | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16249
Sequence Length: 149
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step... |
Q0AQ78 | MTQPIHILNGPNLNLLGTREPDVYGTLSLKEIEQACARHARDLGYEILFRQSNHEGELIDWLHDANVNACAVVFNPAAFTHTSVALHDAVRAIEPPVIEVHLSQTAAREAFRHHSYIALAARGSITGLGLQSYLLGINAAITSLGN | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 15884
Sequence Length: 146
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step... |
B1LXE5 | MNDTVLVLNGPNLNLLGKRQPEIYGRETLADVEALCRETAAGFGLAVDFRQSNAEHALIDAIHEFRVGSAGIVINAGAYTHTSVALLDALNTCEVPVIECHISNVHRREAFRHHSYISLAATSVLAGFGTHGYALAIRHLAHLRAGRPA | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16059
Sequence Length: 149
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step... |
Q2RI90 | MKILVINGPNLNLLGNREPETYGRTTLATIEAELRRQASQAGVEIEFFQSNHEGALIDCLHAARGRVDAAVINPGALGHYSIALRDALAAVDYPAVEVHLSNIYRREEFRHHTVTAAVVAGQISGFGPLSYRLGLEAAIELARRRREAPPDGGSNG | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16879
Sequence Length: 156
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step... |
P0A4Z7 | MSELIVNVINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSVALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHVGT | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 15790
Sequence Length: 147
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step... |
O66908 | MRIILFSGKGGVGKTTISAATGYKLSQLGKKVIVVSLDPAHSLADSFDVPEEERRKAKGLPIKINENLEIQEIDIQEEIERYWGEVYRFIELLFHTTGLHEILADELAILPGMEEITSLLYVNKYYREGNHDVLILDLPPTGESIRFVSMPTVMKWYMKKIFKTERLIMKVARPTVGRMTDVPLPDEEYFKALETFYERLKGVDEILINPDITSIRIVSNPEKMVLKESQRAFLYFLLFGVNVDAVIVNKVIPEEVIQQENCSFLEKWLNIQKKYVKEIESYFSPVPVFKVPLLEEEVVGLERLEKLAQLIYGDEPPDKI... | Function: Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da): 45683
Sequence Length: 396
EC: 7.3.2.7
|
P08690 | MQFLQNIPPYLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFSQTIGITIQAIASVPGLSALEIDPQAAAQQYRARIVDPIKGVLPDDVVSSINEQLSGACTTEIAAFDEFTGLLTDASLLTRFDHIIFDTAPTGHTIRLLQLPGAWSSFIDSNPEGASCLGPMAGLEKQREQYAYAVEALSDPKRTRLVLVARLQKSTLQEVARTHLELAAIGLKNQYLVINGVLPKTEAANDTLAAAIWEREQEALANLPADLAGLPTDTLFLQPVNMVGVSALSRLLSTQPVASPSSDEYLQQRPDIPSLSALVD... | Function: Anion-transporting ATPase. Catalyzes the extrusion of the oxyanions arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents.
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da):... |
O66674 | MRVFFFGGKGGVGKTTASSAFAVKLSEQGKKVLLLSTDPAHSLSDVFNTELQGETKLSENLTVKEIDLNEELKEYRSRVFKLAEATLRKETLRELEGIIHSLEESPGIEDVVIFEALSKEVVYRENEYDYIVVDTAPTGHTLGLLKTVRNLGNFLEEIVKLKEKVYELKKLSGKSVHEEALEYLKERKERFKKFSEIIYDKSYFFAVLTPEKLPFEETKRLVNSLKHYGIRVKALIINKVLPENPQDEFLKARKEVEKKFLKEIENYFMDIEKISIPYQKEEVVGYEKLKEFSKFLPLG | Function: Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da): 34559
Sequence Length: 299
EC: 7.3.2.7
|
P52145 | MKFLENIPSYLFFTGKGGVGKTSISCATAIRLAELGKRVLLVSTDPASNVGQVFDQTIGNTIQPVTAVSGLSALEIDPQDAAQQYRARIVDPIIGLLPDDVVNSISEQLSGACTTEIAAFDEFTGLLTDASLLTRFDHIIFDTAPTGHTIRLLQLPGAWSSFIESNPDGASCLGPMAGLEKQREQYAHAVEALSDPERTRLVLVARLQKSTLQEVARTHDELSAIGLKNQYLVINGVLPASEEKRDALAAAIWQREQEALANLPAGLSDLPTDNLYLQPLNMVGVSALKGLLNEHAEITSLPEQSPQNKPENMSLSVLVD... | Function: Anion-transporting ATPase. Catalyzes the extrusion of the oxyanions arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents.
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da):... |
O50593 | MKLLQNIPPYLFFTGKGGVGKTSISCATAIHLAEQGKRVLLVSTDPASNVGQVFDLAIGNTIRPVTAVPGLSALEIDPQEAARQYRARIVDPIKGLLPDDVVNSISEQLSGACTTEIAAFDEFTGLLTDASLLTRFDHIIFDTAPTGHTIRLLQLPGAWSSFIESNPDGASCLGPMAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAEHDALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLATRSEALPLPVTNILYTPENLSLSGLVD... | Function: Anion-transporting ATPase. Catalyzes the extrusion of the oxyanions arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents.
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da):... |
Q08DD1 | MEALWTLTLALAAGLAAASPPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGLYPGVLEPSSRGGLPLDEVTLAEVLAAQGYLTGIAGKWHLGVGPEGAFLPPHHGFHRFLGIPYSHDQGPCQNLTCFPPATPCEGICDQGLVPIPLLANLSVEAQPPWLPGLEARYVAFARDLMTDAQHQGRPFFLYYASHHTHYPQFSGQSFPGHSGRGPFGDSLMELDAAVGALMTAVGDLGLLGETLVFFTADNGPETMRMSHGGCSGLLRCGKGTTFEGGVREPALAFWPG... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Hydrolyzes cerebroside sulfate.
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification ... |
Q46366 | MRILTFTGKGGVGKTSVSAATAVRLSEMGHRTLVLSTDPAHSLSDSFNIQLGAEPTKIKENLHAIEVNPYVDLKQNWHSVQKYYTRIFMAQGVSGVMADEMTILPGMEELFSLLRIKRYKSAGLYDALVLDTAPTGETLRLLSLPDTLSWGMKAVKNVNKYIVRPLSKPLSKMSDKIAYYIPPEDAIESVDQVFDELEDIREILTDNVKSTVRLVMNAEKMSIKETMRALTYLNLYGFKVDMVLVNKLLDAQENSGYLEKWKGIQQKYLGEIEEGFSPLPVKKLKMYDQEIVGVKSLEVFAHDIYGDTDPSGMMYDEPPI... | Function: Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da): 45848
Sequence Length: 405
EC: 7.3.2.7
|
O52027 | MTATQTPAKEVVEPNSEDTEFVFFSGKGGVGKSTVSCATATWLADNDYDTLLVTTDPAPNLSDIFNQDIGHEVTAIDDVPNLSAIEIDPDVAAEEYRQETIEPMRALLGDEEIQTVEEQLNSPCVEEIAAFDNFVDFMDSPEYDVVVFDTAPTGHTIRLMELPSDWNAELEKGGSTCIGPAASMDDKKADYERAIDTLSDESRTSFAFVGKPESSSIDEIERSASDLAELGISSQLLVVNGYLPESVCEDPFFEGKRADEQAVIDRVESTFDQQALATYPLQPGEIAGLELLSDVGGVLYDGEEATVDVDAATRRATNED... | Function: Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity). Involved in resistance to arsenite and antimonite but not to arsenate.
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da): 70532
Sequence Length: 644
EC: 7.3.2.7
|
P15289 | MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPG... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Hydrolyzes cerebroside sulfate.
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification ... |
Q58542 | MLSKIKDSINSLRGITEKKLEKKDGTKYIMFGGKGGVGKTTMSAATGVYLAEKGLKVVIVSTDPAHSLRDIFEQEFGHEPTKVKGYDNLYVVEIDPQKAMEEYKEKLKAQIEENPFLGEMLEDQLEMAALSPGTDESAAFDVFLKYMDSNEFDVVIFDTAPTGHTLRFLGMPEVMDKYMTKLIKLRKQMSGFMKMMKKLLPFGGKDEDIDYDKMLEELEKMKERIVRARNILSDPERTAFRLVVIPEEMSILESERAMKALQKYGIPIDAVIVNQLIPEDVQCDFCRARRELQLKRLEMIKEKFGDKVIAYVPLLRTEAK... | Function: Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da): 39919
Sequence Length: 349
EC: 7.3.2.7
|
O27555 | MAFKDLFKFNKGKTTFVFIGGKGGVGKTTISAATALWMARSGKKTLVISTDPAHSLSDSLEREIGHTPTKITENLYAVEIDPEVAMEEYQAKLQEQAAMNPGMGLDMLQDQMDMASMSPGIDEAAAFDQFLRYMTTDEYDIVIFDTAPTGHTLRLLSFPEIMDSWVGKMIKIRRQIGSMAKAFKNILPFMGDEEEEDRALQDMEATKKQINAAREVMSDPERTSFKMVVIPEEMSIYESERAMKALEKYSIHADGVIVNQVLPEESDCEFCNARRKLQQERLKQIREKFSDKVVAEVPLLKKEAKGIETLEKIAEQLYGE... | Function: Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da): 36544
Sequence Length: 324
EC: 7.3.2.7
|
P50428 | MALGTLFLALAAGLSTASPPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAEGGLRFTDFYVPVSLCTPSRAALLTGRLPVRSGMYPGVLGPSSQGGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPDIPCKGGCDQGLVPIPLLANLTVEAQPPWLPGLEARYVSFSRDLMADAQRQGRPFFLYYASHHTHYPQFSGQSFTKRSGRGPFGDSLMELDGAVGALMTTVGDLGLLEETLVIFTADNGPELMRMSNGGCSGLLRCGKGTTFEGGVREPALVYWPGH... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Hydrolyzes cerebroside sulfate.
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification ... |
Q55794 | MRVILMTGKGGVGKTSVAAATGLRCAELGHKTLVLSTDPAHSLADSFDLELGHEPRLVKENLWGAELDALMELEGNWGAVKRYITQVLQARGLDGVQAEELAILPGMDEIFGLVRMKRHYDEADYDVLIIDSAPTGTALRLLSLPEVGGWYMRRFYKPLQGMSVALRPLVEPLFRPIAGFSLPDKEVMDAPYEFYEQIEALEKVLTDNTQTSVRLVTNPEKMVLKESLRAHAYLSLYNVSTDLVIANRILPETIDDPFFQRWKSNQQVYKQEIYDNFHPLPVKEAPLFSEEMCGLAALERLKDTLYKDEDPSQVYYKENT... | Function: Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).
Catalytic Activity: arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate
Sequence Mass (Da): 44626
Sequence Length: 396
EC: 7.3.2.7
|
P08691 | MLLAGAIFILTIVLVIWQPKGLGIGWSATLGAVLALASGVIHIADIPVVWNIVWNATATFIAVIIISLLLDESGFFEWAALHVSRWGNGRGRLLFTYIVLLGAAVAALFANDGAALILTPIVIAMLLALGFSKSTTLAFVMAAGFISDTASLPLIVSNLVNIVSADFFKLGFTEYASVMVPVDIAAIIATLVMLHLFFRKDIPPTYELARLKEPAKAIKDPATFRTGWVVLLLLLVGFFVLEPMGIPVSAIAAVGAAVLFAVAKKGHGINTGKVLRGAPWQIVIFSLGMYLVIYGLRNAGLTDYLSDVLNELADKGLWAA... | Function: Involved in arsenical resistance. Thought to form the channel of an arsenite pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45599
Sequence Length: 429
Subcellular Location: Cell inner membrane
|
P45946 | MKRLSFLDRYLTIWIFLAMALGIGLGFIFPSFVGGLNKLQVGTTSIPLAIGLVLMMYPPLAKVRYEEIGRVFKDIKVLILSLVQNWIIGPTLMFILAIIFLPDKPEYMIGLIMIGLARCIAMVIVWNDLSKGDTEYAAGLVAFNSIFQMLFFSVYAYIFVTVIPQWLGMEGAVVNITMAEVAKSVFIYLGVPFIAGMVTRYIFVKVKGKEWYEKVFIPKISPITLIALLFTIIVMFSLKGDVIVSLPLDVVRVAIPLLIYFVLMFFVSFFLGKKIGANYAVTTTLAFTAGSNNFELAIAVAVGVFGIHSGAAFAAVIGPL... | Function: Seems to confer resistance to arsenite by allowing cells to extrude this compound. Could be part of an arsenite extrusion pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38312
Sequence Length: 346
Subcellular Location: Cell membrane
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Q9XJ29 | MESIAAATFTPSRLAARPATPAAAAAPVRARAAVAAGGRRRTSRRGGVRCSAGKPEASAVINGSAAARAAEEDRRRFFEAAERGSGKGNLVPMWECIVSDHLTPVLAYRCLVPEDNMETPSFLFESVEQGPEGTTNVGRYSMVGAHPVMEVVAKEHKVTIMDHEKGKVTEQVVDDPMQIPRSMMEGWHPQQIDQLPDSFTGGWVGFFSYDTVRYVEKKKLPFSGAPQDDRNLPDVHLGLYDDVLVFDNVEKKVYVIHWVNLDRHATTEDAFQDGKSRLNLLLSKVHNSNVPKLSPGFVKLHTRQFGTPLNKSTMTSDEYK... | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a su... |
B8N0E7 | MRFRQQVETCLNYWPAEGPVQRELILGTVGAYRRPIDSRPVLIQDVRGQEGTFTLDIHGFQFIKHISQHVASFDEASVLKDNMTALEAEHLLKTRWAIVNIWRPLKPVPRDPLAVSDARSFHDKDLLEIYGRVPGRQAKKDYDAATKGSGFGMLYGKYSPGQQWFYMSDMKPDEALLIKCYDSKDDGRTARRTPHTAFVDPRTRDVKVARESLELRCLVFFEDQPLA | Function: Hydroxylase/desaturase; part of the gene cluster that mediates the biosynthesis of aspergillic acid, a hydroxamic acid-containing pyrazinone with aliphatic side chains that originates from leucine (Leu) and isoleucine (Ile) . Aspergillic acid has antibiotic properties and was shown to be lethal to mice . The ... |
B8N0E8 | MSIFSSISSLGLEACYRHHVRTSPNATAVVDGDQSMTYRELETRVNDLASILGRENIEEEEPIGILVPMGIAHVVAQAAVLRLGGSCVPMDLSFPDQRINDLLRALKTRIVLTVESEKARFAEFQTILVDSKYANLHQNGYHEDTIPAVETGRNHRTHILHTSGTTGLPKPVEIMSKGITRMAFNTQCVEFKSTDRVAQISAPSFDAALFEIWTTLARGAAIVLLPKNVVIDPVALHDSLRKYRITSILVTTALLNHVVSAIPNAFEDLDYVLTGGEAANPSVMQVILENGPPKKLVHAYGPTECTIITTYHLTTLEEVR... | Function: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspergillic acid, a hydroxamic acid-containing pyrazinone with aliphatic side chains that originates from leucine (Leu) and isoleucine (Ile) . Aspergillic acid has antibiotic properties and was shown to be lethal to mi... |
B8N0E9 | MGFFIQHGLTKPEILYPFLFGIFAVASLCIATLLFPASFSAASRVISWVLSIYLEVKNPIRHTETGRNIPGPSYVWPNGQGDIEKYVQGRSRSEQWQRKYGNVYRIWAGMTPEVVLTRPEQLHAIFKDSDKHTKATNSDSGYFMSRILGQCLGLMAGPRWKLLKGIAAPPFMHPTAVRSIGRIQEHVRAHFHDLETNGNLREGRIHPVQDLKMLPFFIVAEANYGSLTPAMKSELDSLAPARENLMKFVLFGGLARFNISRFFPTEANRQLRRFRSQWRAFNRAAYERAREKHPSAMVVQMYDAVHKGVLTEEQVAQTMD... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspergillic acid, a hydroxamic acid-containing pyrazinone with aliphatic side chains that originates from leucine (Leu) and isoleucine (Ile) . Aspergillic acid has antibiotic properties and was shown to be lethal to mice... |
B8N0F1 | MDRSRTSSQGRDVLPPRGDEGRISPSLDKEKSPGPEDQPDAPPDGGLTAWLVVVGAWCTSFCSFGWVNSVGIFQNYYESHLLKHLSSSTISWIPSLQIFFMFAMGPIVGKLYDTFGARYLIIGGTFFHVFGLMMASISTQYYQLLLSQGICSAIGAAAIFQPALSAVSAWFNRKRGIAFATLSTGSSVGGVIFPIMVDRLIAKVGFGWSMRISAFMILFLLGIAIVTVKARRPPPQGPKPSGVQLLQPFKEPVFIVTLLGYMLLTYGVFIPINYVIVQAVASGMNADLASYLVPMLNGASLFGRLGAGFMSDRYGRYNIF... | Function: MFS transporter; part of the gene cluster that mediates the biosynthesis of aspergillic acid . Probably involved in aspergillic acid metabolism and transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47346
Sequence Length: 442
Pathway: Secondary metabolite biosynthesis.
Subcellular ... |
Q9H1I8 | MPALPLDQLQITHKDPKTGKLRTSPALHPEQKADRYFVLYKPPPKDNIPALVEEYLERATFVANDLDWLLALPHDKFWCQVIFDETLQKCLDSYLRYVPRKFDEGVASAPEVVDMQKRLHRSVFLTFLRMSTHKESKDHFISPSAFGEILYNNFLFDIPKILDLCVLFGKGNSPLLQKMIGNIFTQQPSYYSDLDETLPTILQVFSNILQHCGLQGDGANTTPQKLEERGRLTPSDMPLLELKDIVLYLCDTCTTLWAFLDIFPLACQTFQKHDFCYRLASFYEAAIPEMESAIKKRRLEDSKLLGDLWQRLSHSRKKLM... | Function: Ubiquitin-binding protein involved in DNA repair and rescue of stalled ribosomes . Plays a role in DNA damage repair as component of the ASCC complex . Recruits ASCC3 and ALKBH3 to sites of DNA damage by binding to polyubiquitinated proteins that have 'Lys-63'-linked polyubiquitin chains . Part of the ASC-1 c... |
Q91WR3 | MPALPLDQLQITHKDPKTGQPKTSAALNPEQKADRYFVLYKPPPKDNIPALVEEYLERANFVANDLDWLLALPHDKFWCQVIFDETLQKCLDSYLHYVPRKFDEWVAPTPEVADMQNHLHRSVFLTFLRMSTHKESKDHFISPSAFGEILYNNFLFDIPKILDLCVLFGKGNSPLLQKMIGNIFTQQPSYYTDLDETIPTILQVFSNILQHCGLQGDGTSTTPQKLGERSPLTPSDMPLLELKDIVLYLCDTSTTLWAFLDIFPLACQTFQKHDFCYRLASFYEMAIPELESAIKKRRLEDSKLLGDMWQRLSHSKKKLM... | Function: Ubiquitin-binding protein involved in DNA repair and rescue of stalled ribosomes. Plays a role in DNA damage repair as component of the ASCC complex. Recruits ASCC3 and ALKBH3 to sites of DNA damage by binding to polyubiquitinated proteins that have 'Lys-63'-linked polyubiquitin chains. Part of the ASC-1 comp... |
Q66DP5 | MSLNVKLHPSGIIFTSDGTSTILDAALDSNIHIEYSCKDGTCGSCKAILISGEVDSAENTFLTEEDVAKGAILTCCSKAKSDIELDVNYYPELSHIQKKTYPCKLDSIEFVGEDIAILSLRLPPTAKIQYLAGQYIDLIINGQRRSYSIANAPGGNGNIELHVRKVVNGVFSNIIFNELKLQQLLRIEGPQGTFFVREDNLPIVFLAGGTGFAPVKSMVEALINKNDQRQVHIYWGMPAGHNFYSDIANEWAIKHPNIHYVPVVSGDDSTWTGATGFVHQAVLEDIPDLSLFNVYACGSLAMITAARNDFINHGLAENKF... | Function: Participates in the conversion of CDP-6-deoxy-D-glycero-L-threo-4-hexulose to 3,6-dideoxy-D-glycero-D-glycero-4-hexulose together with CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase (E1) in two consecutive steps. The detailed mechanism of E3 is not yet resolved.
Sequence Mass (Da): 36033
Sequence Length... |
A0A455RAK9 | MAFGVEPPEHVTPWFKPVYEATFQFGGVAWTLCYILIAREGMRTKSYGMPLFALANNFAWEMVYALWVVDNAFEKTAMTIWMLIDTPIIYSILKHGVLEWQHAPMVSRNLKSILVGLIALCAAAHWSWQSWWIGNEMGKRDDLEGADLTQMAYWAVSMCQFLVSTMSLAMLCVRGHSGGVSWMIWLSRFLGTLIGLNMNYAWAYYTWPEAHEYFMSAPAVFVWGVTTVCDIIYGFVLYHVKSNERELSDGRKVAAEADDEQVGGWSKMKTGKN | Function: Terpene cyclase; part of the asc-1 gene cluster that mediates the biosynthesis of both ascochlorin and ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis . The first step in the pathway is performed by the non-reducing po... |
A0A455R4X0 | MGSLLFDSPVGRFVASFPALSAAAGLIVAISFIYIRFIKTPKLDLPVVGNPGDKWDAQKHIVAGARKYPDTPYILPMDPPIVVLPIKIQDEVRNLPENVVSFTKEHQRNFFAQYTGIGDHRPEMITAIRQDLTRHIVSTIPGLQEEVRYGFDKEFGDCKDWTPFPLYMKVLRIVALTSGRVFVGRPLSREEEWLQRTISYTMDCVKARNAIREYPWWKRRWVTSSLPEIAKLTEHRTRGGVLLKPIMDAQLAKDSKREKIINEETGDEEGNFIEWLLKHTPGDLKMDPENLALNQMVLAFASVHTSSMSVTHAILELVTR... | Function: Cytochrome P450 monooxygenase; part of the asc-1 gene cluster that mediates the biosynthesis of both ascochlorin and ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis . The first step in the pathway is performed by the n... |
A0A0H3G0N3 | MTDIPDRKEAVISLWPEFAKAIVSGKKTVEFRRRIPLPALSARIWIYATRPVKSVIGFAYLEAIVQGDVNTLWSRYGREAFLSEQQYRDYFEGTEKATAFLLRDHQPIRPINLDQLKEIRANFQPPQSLTWLRKEETQKLVSLTSQVE | Cofactor: Active in the presence of Mn(2+) or Ni(2+) ions. No activity detected with Zn(2+) or Co(2+).
Function: Shows sequence-specific endoribonuclease activity towards single-stranded RNA (ssRNA), with a preference for the bond between pyrimidine and adenine nucleotides. May also have 5'-exonuclease activity.
Sequen... |
A0A455R624 | MGLSLGYSPDRGSIGSWICAAPLILALFVISYRLFQSVIDYRLSHRNGCKPPPTYPHKDWYLGLHHVFGLLKAKKENRLPTAFSELFDASGPDVHTLGHYVLGKKSYWTRDPENIKAVLSSKFNDWGLPSARKATFRTCLGGGIFGVDGKEWEHSRAMLKPSFTRTQIGDTATLSKHADNLIARIPEGETVDLAELFPLLTMDVGTEMLFGESVGSLDPAEIKQATRFTTSFDYIVQTMSKHMALPILTKLRDKTLQGCVEFVDDFAADVVNRTIANESKTEKPSSLGKYIFPTELAKMGLPEKQIRIEVINIMVAGRDT... | Function: Cytochrome P450 monooxygenase; part of the asc-2 gene cluster that mediates the biosynthesis of ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis . The first step in the pathway is performed by the non-reducing polyketid... |
Q03288 | MDVTRLLLATLVGFLCFFTVHSHLALEETLGDDRSLRSNSSMNSLDFSSVSIVALNKKSKKISRKEAEKRKRSSKKKASMKKVARPPPPSPCVATRDSCKPPAPACCDPCASCQCRFFGSACTCRVLNPNC | Function: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). Causes hair follicle mela... |
Q6ZYM3 | MDVTRLLLATLLVCLCFFTASSHLAPEEKSKDERSLRSNSSMNLLDFPSVSIVALNKKSKKISRKEAEKRSSKKKASMKKVAQPRPPRPAPCVANRDSCKPPALACCDPCAFCQCRFFRSACSCRVLNPTC | Function: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment) (By similarity).
Sequence ... |
Q99JA2 | MDVTRLLLATLVGFLCFLTVHSHLVFEETLGDDRSLKSNSSINSLDFSSVSIVALNKKSKKISRKEAEKRKRSSKKKASIKKVARPPPPSPCVATRDSCKPPAPACCNPCASCQCRFFGSACTCRVLNPNC | Function: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment).
Sequence Mass (Da): 14276... |
A7GNN8 | MYQSLMTVRETQIAIKEVKTFFEDQLAKRLGLFRVSAPLFVTKKSGLNDHLNGVERPIEFDMLHSGEELEIVHSLAKWKRFALHEYGYEAGEGLYTNMNAIRRDEELDATHSIYVDQWDWEKIVQKEWRTVEYLQETVRTIYGIFKDLEDHLFEKYPFLGKYLPEDIAFITSQELEDKYPELTPKEREHAIAKEYGAVFIIGIGDVLRSGEKHDGRAADYDDWKLNGDILFWHPVLQSSFELSSMGIRVDSQSLDEQLTKAGEDFKRDYDFHKGILEDVLPLTIGGGIGQSRMCMYFLRKAHIGEVQSSVWPDEMREACK... | Catalytic Activity: ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) + L-asparagine
Sequence Mass (Da): 38101
Sequence Length: 327
Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.1.1
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Q8A5V7 | MSYLIKPKNYKPLLDLKQTELGIKQIKEFFQLNLSSELRLRRVTAPLFVLKGMGINDDLNGIERPVSFPIKDLGDAQAEVVHSLAKWKRLTLADYNIEPGYGIYTDMNAIRSDEELGNLHSLYVDQWDWERVITNEDRNVEFLKEIVNRIYAAMIRTEYMVYEMYPQIKPCLPQKLHFIHSEELRQLYPNLEPKCREHAICQKYGAVFIIGIGCKLSDGKKHDGRAPDYDDYTSTGLNNLPGLNGDLLLWDDVLQRSIELSSMGVRVDREALQRQLKEENEEERLKLYFHKRLMDDTLPLSIGGGIGQSRLCMFYLRKAH... | Catalytic Activity: ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) + L-asparagine
Sequence Mass (Da): 40120
Sequence Length: 345
Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.1.1
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A8Q3T2 | MMENTLEPTLQNVINQTTLKWIFVGGKGGVGKTTCSCSLAIQLSQVRRSVLIISTDPAHNISDAFAQKFNKTPSAVNGFNNLYAMEIEANLGNDAQMVNPGVESSEGDIISLGRQVLQEMVGGLPGIDEAMSFSQMMKLIQSMDFDVVVFDTAPTGHTLRLLQFPTLIESSLGKLIGLQSSFAPLMTQMGGMLGLGEISADDTTNKLRETLDVVRRINSQFKDPDLTTFVCVCIAEFLSLYETERLIQELTKQNIDTHNIIVNQLLYPEEDENGCVKCKKCSARYGIQKKYLEQIADLYEDFNVTKLPLLESEVRGPGQL... | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored ... |
P30632 | MSDQLEASIKNILEQKTLKWIFVGGKGGVGKTTCSCSLAAQLSKVRERVLLISTDPAHNISDAFSQKFTKTPTLVEGFKNLFAMEIDSNPNGEGVEMGNIEEMLQNAAQNEGGSGGFSMGKDFLQSFAGGLPGIDEAMSFGEMIKLIDSLDFDVVVFDTAPTGHTLRLLQFPTLLEKVFTKILSLQGMFGPMMNQFGGMFGMGGGSMNEMIEKMTTTLESVKKMNAQFKDPNCTTFVCVCIAEFLSLYETERLIQELSKQGIDTHNIIVNQLLFPDTDANGTVSCRKCASRQAIQSKYLTDIDELYEDFHVVKLPLLEAE... | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored ... |
Q8I1T8 | MSEDESNSVSCSLSLESDGYSDEEYDTNLNKLIENESLNWIFVGGKGGVGKTTTSCSIAVQLSKRRESVLLLSTDPAHNTSDAFNQKFTNQPTLINSFDNLYCMEIDTNYSENTAFKLNKKEMFDNILPELLHSFPGIDEALCFAELMQSIKNMKYSVIVFDTAPTGHTLRLLAFPDLLKKALGYLINIREKLKGTLNVLKNFTNNEMEFDSLYEKINHLNAMSSSIQANFQNPMKTTFVCVCIPEFLSVYETERLIQELTKKNISCYNIVVNQVVFPLDSPNVNLENCKNLLSQIKNEQIQSYFNDLISKTEELEDVYI... | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored ... |
Q8MYN5 | MHLIFLLFLAPFCSAAVFQLPTKSTGSLRAKLIRAGKYQEFLITQHAARLNTISQPISDYSDEVYLGNFTVGTPPQPVSLVLDTGSANMWVIDASCDNMFCNGWIGSNYTRQKFDTSKSSSFSRENRKFSIQYGKGLCSGYLGTDTVGLGGGLTIRKQELGIANKLDVDFAVQPMDGIFGLAWPALAVDQITPPMQNLISQLDVPVFSVWLDRKIQASHGGSAGMITYGGIDTKNCDAGVTYVPLTAKTYWQFKMDGFAVGTYSQYGYNQVISDTGSSWISAPYAMINDIATQTHATWDEMNEIYTVKCSTMKTQPDLVF... | Function: Aspartic proteinase.
Sequence Mass (Da): 42754
Sequence Length: 391
Subcellular Location: Secreted
EC: 3.4.23.-
|
G5EEI4 | MQTFVLLALVAACSAAVIQVPTHKTESLRAKLIKEGKYTAFLASQHAARAQQLNTGFQPFVDYFDDFYLGNITLGTPPQPATVVLDTGSSNLWVIDAACKTQACNGYPDSGYTKQKFDTTKSTTFVKETRKFSIQYGSGSCNGYLGKDVLNFGGLTVQSQEFGVSTHLADVFGYQPVDGILGLGWPALAVDQVVPPMQNLIAQKQLDAPLFTVWLDRNLQIAQGTPGGLITYGAIDTVNCAKQVTYVPLSAKTYWQFPLDAFAVGTYSETKKDQVISDTGTSWLGAPNTIVSAIVKQTKAVFDWSTELYTVDCSTMKTQP... | Function: Aspartic protease, which is part of the necrosis cell death pathway . Promotes B.thuringiensis Cry6Aa stability by preventing its proteolysis by host gut proteases. Required for Cry6Aa-induced necrotic death of intestinal cells . Cry6Aa uptake into the host intestinal cells triggers an increase in intracellul... |
Q6PTV2 | MSPSSRFRNLVSVDSSSQDFGKRSSLYASLLDSASVSSLPGICSTAEDRDVEDESWKDPSSSSHCAKTEGGACAFPRLNQVLSSLRDPMGVFSRAKRRRSLGKAVGLSTSVICVVALFGIVCLCLYGLVNFSFTSVETSPLDDPRNSPVMGELGNPQASTPSSARADTPARHDRQNQMFSPWSVQNEQFLGEDSDALPHAGPLFRSGVMVMPLRKMKSLRRIGWDKNTITVPDLQAHLVAALRMQEGLSKKDDGNLSGLSDGDDISIHDYMNSQYYTEIYVGSPGQKVRVVVDTGSSDLWVCSASCGILLNILHKTYNHG... | Function: Aspartyl protease which is dispensable for protein degradation in the vacuolar compartment (VAC) or for tachyzoite and bradyzoite viability.
PTM: Proteolytically cleaved into the soluble active mature form by, at least, cysteine protease CPL . Undergoes at least four processing steps; the first cleavage remov... |
P0CZ17 | MRSLNTLLLSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTDPSEIPEVIILYSYQGLNPELIVKAVKDLGAKGIVLAGSGAGSWTATGSIVNEQLYEEYGIPIVHSRRTADGTVPPDDA... | Catalytic Activity: H2O + L-asparagine = L-aspartate + NH4(+)
Sequence Mass (Da): 38687
Sequence Length: 362
Subcellular Location: Secreted
EC: 3.5.1.1
|
Q0W7E0 | MFRIGIVGAGAIGKEIARAIDNGTVPAKLEAIYDRDTAEATSFAASLKSKPRVLPLEELVEASNFVVEAAAQSAVREVAIAALSRSRSVMIMSVGALADKELLETIRTMAKEHCCSIYLPSGAIGGLDAVKAASICKIDSVTITTRKPRDGLRGAPFIVRNNIDVDSMDEPTEIFSGPAAVAIKEFPANVNVAASLSLVGIGFERTLVRVVVDPTIKRNIHEISVRGEFGELHTVVENVPARSNPKTSFLAALSAIATLRQVCEPLKIGT | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 28621
Sequence Length: 270
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
Q2FSK9 | MVRIGLLGCGNVGRIIATHQDGFTVEALFDRLPDHAEELARMCGAPAYADFQEFISQDFDICVEAASVLAVREYAPKILENGKHVLILSVGALSDTNFRKILLDVARSQGKKIHIPSGAIMGLDNLKVGGISRIDSVLLRTTKSPASLGMQVSHRTLAFRGKANECIKQFPKNINVSVALALAVHHDVDVELWADPEVDRNIHDIFVSGEFGEASIRVVNHPSPDNPATSYLAALSVLSLLKNLDSPLVIGS | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 27227
Sequence Length: 252
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
Q58325 | MLKIGIVGCGAIGNFITKKVLDGTIKNAKISAVYDRNFDKAKTLSERTGAKICSSIDDLVKEDLDLVVEAASIKAVEEIAEKSLINNKDVLIMSVGALADKKLFLKLRDLAKTVGRKIYLPSGAIGGLDAIKALRLGEIEEVVLKTTKPVAALEDALKNLGYKPEDIKNPVIVFEGDVFKAIKEFPANINVSVTLSIAAEFPAKVVIVADPNAKLNKHELFVKSSIGTLRVCIENVPFEENPRTSALAAYSAVRLIRDLAEPVKVGT | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 28755
Sequence Length: 267
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
Q8TZ45 | MKKLSLALVGAGGIGTTVLREIREGRLEGKVEPVLVCDRHPEKLKRIERWFPDCDTSTDLDDAMSAEADVLLEAASVEAAASLLPDALKRFDVIVMSVGALVLEEGLLSRCREVAEVTGHRLHVPSGAVGGLDVLRALRGRVREVTLTTIKPPKALNKDVSERTVLYEGSVRDAVRKFPKNINVAAAVSLAVGDPSLVTVRIVCDPEVSVNTHVIEVESSAGTYRFELRNEALPDNPKTSAVAAYSAVALIERMTEGIRVGT | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 28185
Sequence Length: 262
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
Q8PV99 | MLKIGIIGCGFIGGQICRAIDSGEIDAELYALCDSSESKAFGLAKSLNTCKPAYMKIEELISSVDLVVESASQNAVRFIVPQALKAGCSVMVLSVGALADKELRETLFGLAKKHNCKLYFPSGAVVGIDGINSAHAAGISSVTLTTRKPPSGLMGAPYVVEHGIELEKLEKETILFEGTASEAVKAFPANVNVAATISLAGIGFERTMVRVIADPSLSRNIHEINVEGEFGKFCTKVENLPSPENPKTSYLAALSAISTLKKILNPVQIGT | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 28615
Sequence Length: 271
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
O27054 | MILMMVGIVGCGAIANLITGFVRDGRVPVKLGFFYDRDLERAENLASMVDGRAVLDVADMLPEVDLVVEAASPEAVRDLVPEILEAGKDVVVMSVGALMDPELREMLVELASLNDATIHVPSGAIVGLDGLKAASMGNIESVKLITRKPPRSLGISMDEKKVLYRGRASEAVKKFPLNINVAAALSLACDRDVDVEIIADPAVDRNVHEVTVRGDFGEFKTITENVRCSVNPKTSVMAAYSAIKLLKSLSENIHIGT | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 27569
Sequence Length: 257
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
A9A1F7 | MKRIALLGCGSMGTQIALAIDSENFPATLTHVYDESKDASFSLTQKLKNKPEIVENSHLLSSQPIDIVVEAASQNAVKDVALSVIQNKKDLMIMSVGALLDESIYDILSDACNDFKKTIYLPSGAIAGLDGLKSVKDELESISITTTKHPRSLKGAKFFETSDINLDEITSSTVVYKGTAKEAVTLFPANINVAALLSLTGIGSEKTSVTIVADPNTDKNTHHIEASGKFGTMTFTIENVPDSNNPKTSRLAILSAIETLKKYCSDDIQIGT | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 29185
Sequence Length: 272
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
Q126F5 | MLKIAMIGCGAIGASVLELLHGDSDVVVDRVITVPEARDRTEIAVARWAPRARVLEVLAADDAPDLVVECAGHGAIAAHVVPALERGIPCVVTSVGALSAPGMAQLLEQAARRGKTQVQLLSGAIGGIDALAAARVGGLDSVVYTGRKPPMAWKGTPAEAVCDLDSLTVAHCIFDGSAEQAAQLYPKNANVAATLSLAGLGLKRTQVQLFADPGVSENVHHVAAHGAFGSFELTMRGRPLAANPKTSALTVYSVVRALLNRGRALVI | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 27568
Sequence Length: 267
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
Q9HYA4 | MLNIVMIGCGAIGAGVLELLENDPQLRVDAVIVPRDSETQVRHRLASLRRPPRVLSALPAGERPDLLVECAGHRAIEQHVLPALAQGIPCLVVSVGALSEPGLVERLEAAAQAGGSRIELLPGAIGAIDALSAARVGGLESVRYTGRKPASAWLGTPGETVCDLQRLEKARVIFDGSAREAARLYPKNANVAATLSLAGLGLDRTQVRLIADPESCENVHQVEASGAFGGFELTLRGKPLAANPKTSALTVYSVVRALGNHAHAISI | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 27920
Sequence Length: 267
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
Q5LPG8 | MWKLWGSWPEGDRVRIALIGHGPIAAHVAAHLPVGVQLTGALCRPGRDDAARAALGVSVAQALEGLPQRPDLLVDCAGHSGLRAHGLTALGAGVEVLTVSVGALADAVFCAELEDAARAGGTRLCLASGAIGALDALAAAAMGTGLQVTYTGRKPPQGWRGSRAEKVLDLKALTGPVTHFTGTARAAAQAYPKNANVAAAVALAGAGLDATRAELIADPGAAANIHEIAAEGAFGRFRFQIEGLPLPGNPRSSALTALSLLAALRQRGAAIRPSF | Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate
Sequence Mass (Da): 27808
Sequence Length: 275
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-as... |
A4WA61 | MKKVLALVVAAAMGLSSAAFAAETTTSSAAPATATATTTKAAPAKTVHHKKHKKAVEQKAQAAKKHHKKAVKKQEAAPATTTAPVEQKAQAAKKHHKAAAKPAVAQKAQAAKKHHKKAVKHEAAKPAAQPAA | Function: Required for growth and/or survival at acidic conditions.
PTM: Proteolytic processing gives rise to the active protein.
Sequence Mass (Da): 13517
Sequence Length: 132
Subcellular Location: Periplasm
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Q93MH5 | MKKVLALVVAAAMGLSSAAFAADAVSTTQAPAATHSTAAKTTHHKKHHKAAAKPAAEQKAQAAKKHKKAEAKPAAAQKAQAAKKHKKVAAKPAAPQKAQAAKKHHKAAAKPAAQKAQAAKKHHKTTKHQAAKPTAQPAA | Function: Required for growth and/or survival at acidic conditions.
PTM: Proteolytic processing gives rise to the active protein.
Sequence Mass (Da): 14183
Sequence Length: 139
Subcellular Location: Periplasm
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Q83RD2 | MKKVLALVVAAAMGLSSAAFAAETATTPAPTATTTKAAPAKTTHHKKQHKAAPAQKAQAAKKHHKNTKAEQKAPEQKAQAAKKHAGKHGHQQPAKPAAQPAA | Function: Required for growth and/or survival at acidic conditions.
PTM: Proteolytic processing gives rise to the active protein.
Sequence Mass (Da): 10460
Sequence Length: 102
Subcellular Location: Periplasm
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A1JKC3 | MKKVLALIVAATMGLSSVAFAAETTAAATAAPAATSTTAAPAVEKAAPAKATHHKKHKATKQTTEQKAQAAKKAVKKAPAQKAQAAKKAVKKAPVQKAQAAKKHVKKAPAQKAQAAKKHHKTAKKSATAPAA | Function: Required for growth and/or survival at acidic conditions.
PTM: Proteolytic processing gives rise to the active protein.
Sequence Mass (Da): 13352
Sequence Length: 132
Subcellular Location: Periplasm
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Q8TPT3 | MSMKIKICIPTERIQNPIISETIVETGILLNIMVANIDSTYGELIADVKDSRFARIKKALESRGAIVAILDRPIHRDEEECVECGACISVCPMNVYSFDETWSLCVDEKKCIQCGMCIKMCPHGALKLGE | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis . Together with MA_1821, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine. May be involved in the reduction of the disulfide formed in ... |
P61523 | MAKAHKDVKKIVLAYSGGLDTSIILKWLKNEYGCEVIAFSADLGQGDELAPIRDKAIATGADKVYIDDLKEEFVKDFVFPMFRANAIYEGHYLLGTSIARPLIAKRQMEIAKIEGADAVSHGATGKGNDQVRFELAYYHFDPAITVVAPWREWKLNSRQALVNYARKNGIPIPVTKKRPWSSDRNLLHISFEGGILEDTWAEPPENMYVLTKAPEKAPNKPQFVEIEFKNGNAVAVDGEKMSPAQLLAHLNYIGGEHGIGRVDLLENRSVGMKSRGVYETPGGTILREAHSAVEQITMDREVMRIRDSLIPEYARQVYAG... | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 45657
Sequence Length: 406
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: ... |
P85910 | WFDPLRITETTTGSVTLK | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 2065
Sequence Length: 18
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Plastid
EC: 6.3.... |
P09034 | MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDVLEIEFKKGVPVKVTNVKDGTTHSTSLDLFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAEL... | Function: One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals (Probable). Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for t... |
A4W9J6 | MMVIRPVERGDLAGLMQLAGKTGGGLTSLPADEKTLSSRIDRALQTWQGTLPKSEQGYVFVLEESDTGTVVGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDRFNEKVVAEMRGVIDETGYSPFWESLGERFFSMEFSRADYLCGTGQKAFIAELMPKHPIYTDFLSPQAQAVIGQVHPQTAPARAVLEKEGFRYHNYVDIFDGGPTLECDVDRVRAIRKSRLVTVAEGQPAPGEWPACLVANEQYDQFRAMLIHTNPTCERLVLTAAQ... | Function: Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine.
Catalytic Activity: L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine
Sequence Mass (Da): 38302
Sequence Length: 344
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and suc... |
P80357 | MLVMRPAQAADLPQVQRLAADSPVGVTSLPDDAERLRDKILASEASFAAEVSYNGEESYFFVLEDSASGELVGCSAIVASAGFSEPFYSFRNETFVHASRSLSIHNKIHVLSLCHDLTGNSLLTSFYVQRDLVQSVYAELNSRGRLLFMASHPERFADAVVVEIVGYSDEQGESPFWNAVGRNFFDLNYIEAEKLSGLKSRTFLAELMPHYPIYVPLLPDAAQESMGQVHPRAQITFDILMREGFETDNYIDIFDGGPTLHARTSGIRSIAQSRVVPVKIGEAPKSGRPYLVTNGQLQDFRAVVLDLDWAPGKPVALSVE... | Function: Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. Also acts on L-ornithine.
Catalytic Activity: L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine
Sequence Mass (Da): 36931
Sequence Length: 338
Pathway: Amino-acid degradation; L-arginine degradation via AST pa... |
Q8X598 | MSQPITRENFDEWMIPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPELREALNEQASKFWHTGNGYTNESVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPPDIRHAAYNDINSASALIDDSTCAVIVEPIQGEGGVVPASNAFLQGLRELCDRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLTTAKALGGGFPVGALLATEECASVMTVGTHGTTYGGNPLASAVAGKVLELINTPEMLNGVKQRHDWFVERLN... | Function: Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.
Catalytic Activity: 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde
Seque... |
Q7N2H1 | MDLLTLLLEKKLADHLTFPETINAHWLAEGVLQLIPHEEGNRSLVISAGIHGNETAPIEILIQLLAQLAEGTLALKNNVLIIFGNLPAMRTNRRYLHDDLNRMFGGRYLNFPLGNERSRAAELENVVNRFFAEPSVSSTNIRWHIDLHTAIRASHHEQFALLPAQNRPFSAEFMQWLHDSDIDALVYHREKAGTFSHFLSEKFGADSCTMEMGKAMPFGENDLTRFQKITDALYGLISLSQITARIKFELKHYQVINSIIKSHDSFQLHIPADTLNFTELPEGFEIASQHDHHWKIKFPAKFILFPNAEVANGLRAGLLL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
Catalytic Activity: H2O + N-succinyl-L-glutamate = L-glutamate + succinate
Sequence Mass (Da): 36889
Sequence Length: 325
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate... |
Q15TS5 | MQTVNTHKLISHLQQQGQFLTLSRCSGELVQNPISFTLYEHTQVSIISPGIISFSPKIKSDKAIVLSSGIHGNETAPIEICDQYVIDILTGKIRVAHRILFIFGNLPAMDRATRFVDENLNRLFSHAHASESVDQNSYECARAKEIEEAVAEFYGSGHGEESRYHYDLHTAIRPSKNEKFAVYPFLHGEKHDKEQISFLLACGIDTFLLSGSPTTTFSYYSSRQFGAHAFTVELGKVQAFGQNDMSRFTQVNDTLKRFISGQPLNLKSFNDQDVLIYQVNQVINKHAEDFELDFSDDLPNFSDFPKGTLLAHETGNEYRA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
Catalytic Activity: H2O + N-succinyl-L-glutamate = L-glutamate + succinate
Sequence Mass (Da): 39246
Sequence Length: 350
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate... |
Q88EI7 | MLALGKLLELTLTDHEPAEKTQVTPKGARLRWLGEGALEVRPAESDDCGLDLLLSAGIHGNETAPIELLERLLHGVANGKIRPRARVLFLFGNPAAIRKGERFIEQDINRLFNGRHELSSGFEALRAAELEQFARVFFSKPGRNRLHYDLHTAIRGSKIEQFALYPYKEGRKHSRRELARLAAAGMEAVLLQSKSSITFSAFTYEQLEAEAFTLELGKARPFGQNEQVNLDKLEERLIRIIEATEPEDESSLDGLQLFSVSREIIKHSDSFHLHLPADIENFSELSKGYLLAEDLAEMRWVVEEEGARIIFPNPKVKNGL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
Catalytic Activity: H2O + N-succinyl-L-glutamate = L-glutamate + succinate
Sequence Mass (Da): 37581
Sequence Length: 335
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate... |
Q3IGV3 | MSATTPDYIEELKQTGDFLTLSRNNEWHLAAGEFTLNNGTVVTIHDTGVIEFQPATVSSKDVVYSSAVHGNETAPIEICDELIKQIIAGELLLKQRALFIFGNPQSINIGLRFVEENLNRLFNGHHSVDGVPMNNERTRAAKLEQYVSDFFSRGEQGSSRCHYDLHTAIRGSKNEKFAVYPYLHGKPWKKSQLQFLLSCGVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFAKTKQTLTALISQDKVEYPEFNADEFELFTVHRTINRTQNEFSFPFSDQAENFTGFAKGELLATDGDTPYYADVQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
Catalytic Activity: H2O + N-succinyl-L-glutamate = L-glutamate + succinate
Sequence Mass (Da): 39230
Sequence Length: 351
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate... |
Q9YH26 | MGLGKGKDEYKLAATSEDGGKKDKKAKAKKDMDDLKKEVDLDDHKLTLDELHRKYGTDLTRGLSSSRAKEILARDGPNALTPPPTTPEWVKFCKQLFGGFSMLLWIGAILCFLAYGIQAASEDEPANDNLYLGIVLSAVVIITGCFSYYQEAKSSKIMESFKNLVPRQALGIRDGEKKNINAEEVVLGDLVEVKGGDRIPADLRIISAHGCKVDNSSLTGESEPQTRSPDFSNENPLETRNISFFSTNCIEGTARGIVINTEDRTVMGRIATLASSLEGGKTPIAIEIEHFIHIITGVAVFLGVSFFILSLILGYNWLEA... | Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... |
P06685 | MGKGVGRDKYEPAAVSEHGDKKSKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSATEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEA... | Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... |
P30714 | MGYGAGRDKYEPAATSEHGGKKGKGKGKDRDMEELKKEVTMEDHKMTLEELHRKYGTDLTRGLTTARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRKASDLEPDNDNLYLGVVLSAVVIITGCFSYYQEAKSSRIMESFKNMVPQQALVIRNGEKLSINAENVVQGDLVEVKGGDRIPADLRIISAHGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVINTGDRTVMGRIATLASGLEGGQTPIAVEIGHFIHIITGVAVFLGVSFFILSLILHYTWLEA... | Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... |
P50993 | MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVI... | Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrient... |
Q0CS68 | MPTTAAFLRALYILTTLRGIGTSHEVRNIKHGSESSASRARFLLHTLVIIAAKYLVLDMMTFQPPSPEDTDRMFGEGKEYLLFRPDGLPPPKMQDILTNLGVTLLGWGPIGSWFIEVHYRILSVASVGLGISQPHQWPPLFGSITEAHTLRRFWANFWHQLFRWPMQGLSSFLCRDVLRLPRPSLAERYLKITLVFAISSCLHLAIDGRAGIMLPRSGALRCFLLQPVGIILEDGAQALYRRLRGDAPLSKWTRAVGYIWTWAFLSLVAPMYNFPLFRYQDPARNGVPVPVLRPAMEYFRVKG | Function: Acetyltransferase; part of the gene cluster that mediates the biosynthesis of acetylaranotin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide-bridged cyclic dipeptide . The first step of acetylaranotin biosynthesis is performed by the NRPS ataP which produces dike... |
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