ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q84FH6 | MVRGIRGAITVEEDTPEAIHQATRELLLKMLEANGIQSYEELAAVIFTVTEDLTSAFPAEAARQIGMHRVPLLSAREVPVPGSLPRVIRVLALWNTDTPQDRVRHVYLREAVRLRPDLESAQ | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 13650
Sequence Length: 122
Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorisma... |
Q8G5X4 | MTARPRAVIIGMMGAGKTRVGKEVAHMLRLPFADADVEIEREVGMKIPSYFEEYGEPAFREVEADLIADMLEDFDGIFSLGGGAPMTPSTQHALASYIDHGGRVVYLDADPAEAMERANRGGGRPMLNGNANSRWKKLFKQRDPVFREVANVHVHTRGLTPQGAAKKVIDMVSERAVHVTGAAIEPYDVVIGEGAMNHLVDVLGPKPAKIALIHTQPVQRHSDRARALLRQGGYEVSDIVIPDAEPGKTITVANGIWERLGNEGFTRSDAVVGLGGGAATDLAGFVAATWMRGVRYVNCPTSLLAMVDASTGGKTGINTP... | Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 58712
Sequence Length: 540
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytopl... |
P0A4Z3 | MAPKAVLVGLPGSGKSTIGRRLAKALGVGLLDTDVAIEQRTGRSIADIFATDGEQEFRRIEEDVVRAALADHDGVLSLGGGAVTSPGVRAALAGHTVVYLEISAAEGVRRTGGNTVRPLLAGPDRAEKYRALMAKRAPLYRRVATMRVDTNRRNPGAVVRHILSRLQVPSPSEAAT | 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): 18583
Sequence Length: 176
Pathway: Metabolic intermediate biosynthesi... |
Q9CCS5 | MAPKAVLVGLPGAGKSTIGRRLSKALGVSLLDTDAAIEKQTGRSIADIFAIDGEEEFRRIEEGVVRAALVEHDGVVSLGGGAVTSPGVCAALAGHIVIYLEINAEEAMRRACGSTVRPLLAGPDRAEKFQDLMARRVPLYRRVATIRVDTNCHNLGAVVRYIMARLQAQLATPVSGGDRKSSEAERSGAPLRKSSEVVK | 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): 21084
Sequence Length: 199
Pathway: Metabolic intermediate biosynthesi... |
B2HNC7 | MAPKAVLVGLPGSGKSTIGRRLAKALGVGLLDTDAAIEQQAGRSIAEIFATDGEEEFRRIEEEVVRAALADHDGVLSLGGGAVTSPGVRSALDGHTVVYLEISAAEGVRRTGGSNVRPLLAGPDRAEKFRALMSQRIPLYRRVSTIRVDTNRRNPGAVVRYIMSRLDDPTPNTSPSSTASGAAT | 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): 19347
Sequence Length: 184
Pathway: Metabolic intermediate biosynthesi... |
Q5FAD3 | MKNFNGKLILIGLMGAGKTTLGRQMAQRLDYRFYDSDHEIAAAAGVPIPTIFEMEGEQGFRSRETAILKKLIVLPHIVLSTGGGAVLKEENRALIRKSGTVVYLHAPPETLLERTRCDNSRPLLQVADPLAKLRELYAARDPVYRQTADFTVESANCRETVQTLLKRLSR | 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): 18980
Sequence Length: 170
Pathway: Metabolic intermediate biosynthesi... |
Q82TC0 | MHFRYNYRMQRSKTPNTKNSDTGSIPGNIILIGMMGSGKTTVGKLLANLVGKTFIDIDHEIQRRTGVGIPVIFEIEGEAGFRKRESEVLRDIVRQQNIVLATGGGAILHPDNRALLRQHGTVVYLCAPVTELRRRTYLDKNRPLLQTGNVHAKLIELFTQRDPLYRETAHIIMDSGRQSARAFVQKLIQKLRQSNQEFTAAGSPPCVKPSE | 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): 23703
Sequence Length: 211
Pathway: Metabolic intermediate biosynthesi... |
Q2YBB2 | MISTDAVAPAVDVKGEAGDRAATGNIFLVGMMGAGKTTVGRLLSHFLEKTFYDSDREIQKRTGVSIPTIFEIEGEEGFRRRETEILSELMNARNIILATGGGAVLSGVNRAMLKHGGTVIYLRASIDDLWRRTRHDKNRPLLQTSDPRARLAELFVQRDPLYRETAHIVVESGKRSPRHLAQSLAQQLTISSRTG | 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): 21542
Sequence Length: 195
Pathway: Metabolic intermediate biosynthesi... |
B2IX35 | MSSLLQGVNLYLIGMMGVGKTTVGPLLAKHLGYGFLDLDGVIAKATDKSINQLFAEEGEAGFRQIESDVLSQVCAFTKLTIATGGGIVLRRENWGYLHHGLIVWLDVPVELIYRRLAEDTTRPLLQDADLKGKLRSLLEQRTPLYSQADLHITVQEGETPEDIANRIIEVIPNVLKPQASH | 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): 19959
Sequence Length: 181
Pathway: Metabolic intermediate biosynthesi... |
A4W763 | MTQPIFLVGPRGCGKTTVGLELARACQSQFVDTDHWLQTKAGRTIAEIVEKEGWETFRALETETLKAVSAPSTVIATGGGIILAEHNRGFMREHGIVIYLCAPVATLVERLEAFPEEGQRPTLTGKPISDEVSEVLAERDALYREAAHHVVDASQTPEQVVSHIVTALRLACAS | 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): 18890
Sequence Length: 174
Domain: The LID domain closes over the acti... |
B7LMJ7 | MIQPLFLVGPRGCGKTTVGKALADALERRFVDTDQWLQANVQMTVADIVEREGWAGFRAREAAALEAVTAPATVVATGGGIILAEQNRHFMRNNGIVIYLSAPVDVLVNRLEAEPEVGLRPTLTGKSLSEEVAEVLEQRDILYRETANIIVDATYEPGQVISEIRALLDQMALRNLGGAYT | 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): 19690
Sequence Length: 181
Domain: The LID domain closes over the acti... |
Q741J6 | MIVQVINGPNLGRLGRREPDVYGDTTHDQLAALIEAEAAALGLKAIVRQSDSEAELLDWIHGAADANQPVILNAGGLTHTSVALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPVATGAIVGLGVQGYLLALRYLAGRPA | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 15192
Sequence Length: 143
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step... |
Q1QLB8 | MARTIYVLNGPNLNMLGTREPETYGRATLADVEKLCADTAGDFGLAADCRQSNREGELIDFIHDAHAKKAAGIVINAGGYSHTSVALHDALVAVNIPTVEVHISNIHAREDFRHHSFTARAAFASLCGFGIDGYRLAINGLAAKIGAVKSGAKVKS | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16530
Sequence Length: 156
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step... |
A6Q235 | MKVMVIQGPNLNMLGIREQHIYGPMKLEDIHKQMKNFADANGLDIEFFQSNLEGEIVDKIQESLGDADGIIINAGAYTHTSIAIRDAIAAVQLPTIEVHLSNVYRREEFRQKSMIAPVCAGVITGFGPFSYHLAMVAMHQIFQEIEALKAQQPQQA | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 17380
Sequence Length: 156
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step... |
Q8N5I2 | MGRVQLFEISLSHGRVVYSPGEPLAGTVRVRLGAPLPFRAIRVTCIGSCGVSNKANDTAWVVEEGYFNSSLSLADKGSLPAGEHSFPFQFLLPATAPTSFEGPFGKIVHQVRAAIHTPRFSKDHKCSLVFYILSPLNLNSIPDIEQPNVASATKKFSYKLVKTGSVVLTASTDLRGYVVGQALQLHADVENQSGKDTSPVVASLLQKVSYKAKRWIHDVRTIAEVEGAGVKAWRRAQWHEQILVPALPQSALPGCSLIHIDYYLQVSLKAPEATVTLPVFIGNIAVNHAPVSPRPGLGLPPGAPPLVVPSAPPQEEAEAE... | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates . Through an ubiquitination-dependent mechanism plays for instance a role in the incorporation of SLC11A2 into extracellular vesicles . More generally, plays a role in the extracellular transport of proteins between cell... |
Q99KN1 | MGRVQLFEIRLSQGRVVYGPGEPLAGTVHLRLGAPLPFRAIRVTCMGSCGVSTKANDGAWVVEESYFNSSLSLADKGSLPAGEHNFPFQFLLPATAPTSFEGPFGKIVHQVRASIDTPRFSKDHKCSLVFYILSPLNLNSIPDIEQPNVASTTKKFSYKLVKTGNVVLTASTDLRGYVVGQVLRLQADIENQSGKDTSPVVASLLQKVSYKAKRWIYDVRTIAEVEGTGVKAWRRAQWQEQILVPALPQSALPGCSLIHIDYYLQVSMKAPEATVTLPLFVGNIAVNQTPLSPCPGRESSPGTLSLVVPSAPPQEEAEAV... | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates . Through an ubiquitination-dependent mechanism plays for instance a role in the incorporation of SLC11A2 into extracellular vesicles . More generally, plays a role in the extracellular transport of proteins between cell... |
Q96B67 | MVLGKVKSLTISFDCLNDSNVPVYSSGDTVSGRVNLEVTGEIRVKSLKIHARGHAKVRWTESRNAGSNTAYTQNYTEEVEYFNHKDILIGHERDDDNSEEGFHTIHSGRHEYAFSFELPQTPLATSFEGRHGSVRYWVKAELHRPWLLPVKLKKEFTVFEHIDINTPSLLSPQAGTKEKTLCCWFCTSGPISLSAKIERKGYTPGESIQIFAEIENCSSRMVVPKAAIYQTQAFYAKGKMKEVKQLVANLRGESLSSGKTETWNGKLLKIPPVSPSILDCSIIRVEYSLMVYVDIPGAMDLFLNLPLVIGTIPLHPFGSR... | Function: Adapter protein that plays a role in regulating cell-surface expression of adrenergic receptors and probably also other G protein-coupled receptors . Plays a role in NEDD4-mediated ubiquitination and endocytosis af activated ADRB2 and subsequent ADRB2 degradation . May recruit NEDD4 to ADRB2 . Alternatively, ... |
Q8NCT1 | MGGEAGCAAAVGAEGRVKSLGLVFEDERKGCYSSGETVAGHVLLEASEPVALRALRLEAQGRATAAWGPSTCPRASASTAALAVFSEVEYLNVRLSLREPPAGEGIILLQPGKHEFPFRFQLPSEPLVTSFTGKYGSIQYCVRAVLERPKVPDQSVKRELQVVSHVDVNTPALLTPVLKTQEKMVGCWFFTSGPVSLSAKIERKGYCNGEAIPIYAEIENCSSRLIVPKAAIFQTQTYLASGKTKTIRHMVANVRGNHIASGSTDTWNGKTLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKKLMLELPLVIGTIPYNG... | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates (By similarity). Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (Probable). Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular... |
A0A0B4J1F4 | MGGEAGADGPRGRVKSLGLVFEDESKGCYSSGETVAGHVLLEAAEPVALRGLRLEAQGRATSAWGPSAGARVCIGGGSPAASSEVEYLNLRLSLLEAPAGEGVTLLQPGKHEFPFRFQLPSEPLATSFTGKYGSIQYCVRAVLERPQVPDQSVRRELQVVSHVDVNTPPLLTPMLKTQEKMVGCWLFTSGPVSLSVKIERKGYCNGEAIPIYAEIENCSSRLVVPKAAIFQTQTYLASGKTKTVRHMVANVRGNHIGSGSTDTWNGKMLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKRLMLELPLVIGTIPYSGFGR... | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates . Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (By similarity). Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular vesicles ... |
Q7TP90 | MSSQSSILVDFRPLATSFTGKYGSIQYCVRAVLERPQVPDQSVRRELQVVSHVDVNTPPLLTPMLKTQEKMVGCWLFTSGPVSLSVKIERKGYCNGEAIPIYAEIENCSSRLVVPKAAIFQTQTYLASGKTKTVRHMVANVRGNHIGSGSTDTWNGKMLKIPPVTPSILDCCIIRVYIHIPGAKKLMLELPLVIGTIPYSGFGRRNSSMASQFSMDMCWLALALPEQPEAPPNYADVVSEEEFSRHIPPYPQPSACDGEACYSMFACIQEFRFQPPPLYSESHAQLFCLQPVGPTNRAHF | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates. Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular vesicles. May play a role i... |
O24972 | MRFSIFFKVVALFMITLFSFGAFAYYFVSSQISHENYQNEMRHYQFVTTINEILNNYSDYRAIEDYLYKIGFRETTIENLEKVLAKRRHQLHHRNIGYAEVFKFSDMVFILLKKDEHFVLYKDLHSVSYRNYFLAITVGLLLILFLFLFVLQSLLPLRELRSQVKPFAQGDKSVSCKSKQKDEIGDLANEFDNCILKINAMNESRVLFLRSIMHELRTPITKGKILSSMLKEELSCKRFSSIFDHLNMLIEQFARIEQLASKNYGSNKEKFLMSDLIDKIEKMLLIDEDKESPIHVSSSNYIIEADFELFSIALKNMVDN... | Function: Member of the two-component regulatory system ArsS/ArsR that regulates genes involved in biofilm formation and acid adaptation by acting on major ammonia-producing pathways . Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conser... |
O27106 | MMNDKKITSFIALPDLLSMLNASSGYLSILLSIDGSLNAACILMLLAVLFDSLDGWVARKTGRIDIHGFGKNMDSLSDVISFGVAPAILIYSAAVDFRYINILVGPLIVLCGILRLSRFNVLTGGGKNFTGLPIPVAAVTISSFYLTGFYSELSAAFIMIAVSVLMISSIEYPRVDGMGASTALILIIATIISVAAVEILQAASVVAGPVAIILFIATLTYIAVPILPKRDVI | Function: Involved in the lipid biosynthesis. Catalyzes the formation of unsaturated archaetidylserine from CDP-unsaturated archaeol and L-serine. Activity with ester-linked substrate analogs containing straight aliphatic chains (typical bacterial substrates) is two to three times higher than that with the correspondin... |
P14000 | MKSAPFLFLLGLLGLVTAQTQDPALLDLLRENPDLLSLLLQSNEHRAPLVKPNVVLLVADHMGSGDLTSYGHPTQEAGFIDKMAAEGLRFTNGYVGDAVCTPSRSAIMTGRLPVRIGTFGETRVFLPWTKTGLPKSELTIAEAMKEAGYATGMVGKWHLGINENSSTDGAHLPFNHGFDFVGHNLPFTNSWSCDDTGLHKDFPDSQRCYLYVNATLVSQPYQHKGLTQLFTDDALGFIEDNHADPFFLYVAFAHMHTSLFSSDDFSCTSRRGRYGDNLLEMHDAVQKIVDKLEENNISENTIIFFISDHGPHREYCEEGG... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May be a structural component of the extracellular matrices involved in cell movement during morphogenesis.
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 eukaryote... |
P51691 | MSKRPNFLVIVADDLGFSDIGAFGGEIATPNLDALAIAGLRLTDFHTASTCSPTRSMLLTGTDHHIAGIGTMAEALTPELEGKPGYEGHLNERVVALPELLREAGYQTLMAGKWHLGLKPEQTPHARGFERSFSLLPGAANHYGFEPPYDESTPRILKGTPALYVEDERYLDTLPEGFYSSDAFGDKLLQYLKERDQSRPFFAYLPFSAPHWPLQAPREIVEKYRGRYDAGPEALRQERLARLKELGLVEADVEAHPVLALTREWEALEDEERAKSARAMEVYAAMVERMDWNIGRVVDYLRRQGELDNTFVLFMSDNGA... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Hydrolyzes the bond between sulfate and the aromatic ring in a compound such as 4-nitrocatechol 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, ... |
P28607 | MQKISIIFNLFLSLGCLAFTFNGSASETKNEWITLGTMAGPIPNAKHSQPANAMLVNGNTYVVDAGDGTAGQLAKVGLDIKNVDAVFLSHLHFDHTGGLPAILSLRWQTSARNELVVYGPPGTQQTVDGIFEYMTYGTLGHYGVPGQVPAPANTNIKVVEVEDGTQLKLPDFTVDVIRNSHYSWPKGSEEWKKFQALSFKFSLQDYTVVYTGDTGPSSAVEKLSSGVDLLVSEMMDIDHTVNMIKETNPQMPKGKFIGIHKHLSKHHLSPKQVGELAKAANVGSLVITHMAPGLDTQAEIDFYTKQVASEYKGPISVAQD... | Function: May function as a glycosulphohydrolase involved with desulfation of sulfated polysaccharides.
Catalytic Activity: an aryl sulfate + H2O = a phenol + H(+) + sulfate
Sequence Mass (Da): 35793
Sequence Length: 328
Subcellular Location: Periplasm
EC: 3.1.6.1
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Q10723 | MLQRLVVALCLLGFAALTAAAAHQRPNFVVIFTDDQDGIQNSTHPRYQPKLHEHIRYPGIELKNYFVTTPVCCPSRTNLWRGQFSHNTNFTDVLGPHGGYAKWKSLGIDKSYLPVWLQNLGYNTYYVGKFLVDYSVSNYQNVPAGWTDIDALVTPYTFDYNNPGFSRNGATPNIYPGFYSTDVIADKAVAQIKTAVAAGKPFYAQISPIAPHTSTQIYFDPVANATKTFFYPPIPAPRHWELFSDATLPEGTSHKNLYEADVSDKPAWIRALPLAQQNNRTYLEEVYRLRLRSLASVDELIDRVVATLQEAGVLDNTYLI... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Is commonly produced by soil microorganisms and plays an important role in the mineralization of sulfates.
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... |
P18634 | MAPKISISLNPPYNGEFYSSNDQMSGIVSLQLTKALSIRKISVILKGFSETLTKIDQEYMFQQNGMMMPGQDNKSFHTLMKFEQRVFPPDNVWNALDGSSKPFKVKPGSYNYSFQFDKFPRKPECLKNHTAKTVAFVTRSNARLPPTFNSHWQEFNKIDNLDLYFYSFGKVIYMVQVQLELGKSSSWFKPFHKLIREIETFEFIPEPKDLIIEPDEDDNEELNAFSNNSRGNSMVTNNEFFNSSNLKVPSKDVKVVNGVGYIKSDRNFSQANSILIENGDIRSRPVSSVTSTRQSTRLVNGMKVFPSTYKMGLPDGESNM... | Function: May regulate endocytosis by recruiting RSP5 ubiquitin ligase activity to specific plasma membrane proteins in response to extracellular stimuli.
PTM: Ubiquitinated by RSP5.
Sequence Mass (Da): 59758
Sequence Length: 518
Subcellular Location: Cytoplasm
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Q9UT55 | MKFLNPPFPYSMTSDPESFGHECFTRRWGIILTGIEKDVSERLSKLASTSKDSEVVAQGKPLLNDLEAFKSDIKNDRPLVPLEGEGQDIVEYNEELKQLDNASWGNAPWLYSECYYYRRISLIFARYSEWKAYDPFFQQKDSTLKSSRAAVEELAGRYCLLEEELNSIAKKGDSHIAYMVFVEMAQISLWGNATDLSLLTNLSYEELQNLQGQKVVEESQKNILVNDFPTVWSKLKDVHNGRIDFVLDNAGFELYVDLIFAAYLLKAGIAKEIVLHPKDFPWFVSDVLPYDIEYLLTNLDTIFPTESVTKFATDLRSFSA... | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-... |
Q94GF1 | MASLVLSLRIAPSTPPLGLGGGRFRGRRGAVACRAATFQQLDAVAVREEESKFKAGAAEGCNILPLKRCIFSDHLTPVLAYRCLVREDDREAPSFLFESVEQGSEGTNVGRYSVVGAQPAMEIVAKANHVTVMDHKMKSRREQFAPDPMKIPRSIMEQWNPQIVEGLPDAFCGGWVGFFSYDTVRYVETKKLPFSNAPEDDRNLPDIHLGLYNDIVVFDHVEKKTHVIHWVRVDCHESVDEAYEDGKNQLEALLSRLHSVNVPTLTAGSVKLNVGQFGSALQKSSMSREDYKKAVVQAKEHILAGDIFQVVLSQRFERRT... | 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... |
Q9H765 | MSSSMWYIMQSIQSKYSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEKDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLIGQTPISRLVALLVRGLGTEKEDSCFELLHRAVGHFELRKNGTMPREVARDPQLCEKLTVLCSAPGTLKTLARYAVRRSLGLQYLPDAVKGLPLPASLKEYLLLLE | Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 31642
Sequence Length: 288
Domain: The SOCS box domain mediates the ... |
Q91ZT9 | MSSSMWYIMQSIQSKYSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAERDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLKGQTPISRLVALLVRGLGTEKEDSCFELLHRAVGQFELRKNGIMPREVTKDQQLCEKLTVLCSAPGTLKTLARYAVRRSLGLQYLPDAVKGLPLPVSLKDYLLLLE | Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 31735
Sequence Length: 288
Domain: The SOCS box domain mediates the ... |
Q96DX5 | MDGKQGGMDGSKPAGPRDFPGIRLLSNPLMGDAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVNQGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL | Function: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes at least two forms of creatine kinase, CKB and CKMT1A.
Sequence Mass (Da): 31858
Seque... |
Q91ZT8 | MDGEQRGRSDRPGGSPHLPFLSNPLMGDVVSDWSPLHDAAIHGCLLTLRNLISQGWPVNIITADHVSPLHEACLRGHLSCASVLLSHGAQVNGMTIDWRTPLFNACVSGSQDCVNLLLQHGATPHPETELASPIHEAAKRGYVKCIESLAAHGANIDYNISHLGTPLYVACKNQQVACAKKLLESGVSVNQGKGLDSPLHVVARMSSVELVHLLMDFGANAQAKNADGKRPVDLVPLESPLIQIFLQNEGPQSLRQLCRLRIRKCFGIRQHHKISELLLPEDLKRFLLHL | Function: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes at least two forms of creatine kinase, CKB and CKMT1A (By similarity).
Sequence Mass (... |
A0A0F7RJ52 | MKHAKQIAEHATIQSFLNCYLRETGSGEWITEDKRIEDIFYHLFQRDTCSTYLCCRLSAQNITLYGEVIYKSPTDRHLFGEQFYYQMGDSNSVMKADYVTVITFLIKEMSINYGEGTNPAELMLRVIRSCQNIEEFTKERKEDTSALYGFHTSFIEAEQSLLFGHLTHPTPKSRQGILEWKSAMYSPELKGECQLHYFRAHKSIVNEKSLLLDSTTVILKEELRNDEMVSKEFISKYCNEDEYSLLPIHPLQAEWLLHQPYVQDWIEQGVLEYIGPTGKCYMATSSLRTLYHPDAKYMLKFSFPVKVTNSMRINKLKELE... | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Catalyzes the ATP-dependent condensation of citric acid and spermidine to form N(8)-citryl-spermidine . It can also catalyze the condensation of several di- and triamine analogs of sp... |
Q81RQ8 | MRMDMYHTKILKAIESEDYISVRRRVLRQLVESLIYEGIITPARIEKEEQILFLIQGLDEDNKSVTYECYGRERITFGRISIDSLIVRVQDGKQEIQSVAQFLEEVFRVVNVEQTKLDSFIHELEQTIFKDTIAQYERCNKLKYTQKSYDELENHLIDGHPYHPSYKARIGFQYRDNFRYGYEFMRPIKLIWIAAHKKNATVGYENEVIYDKILKSEVGERKLEAYKERIHSMGCDPKQYLFIPVHPWQWENFIISNYAEDIQDKGIIYLGESADDYCAQQSMRTLRNVTNPKRPYVKVSLNILNTSTLRTLKPYSVASA... | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Catalyzes the ATP-dependent condensation of spermidine with N(8)-citryl-spermidine or N(1)-(3,4-dihydroxbenzoyl)-N(8)-citryl-spermidine, two intermediates in petrobactin biosynthesis ... |
Q81RQ7 | MLIVNREEYSKSDFDLRLQAYEEMEQFQEAAGNRFALCLKDPFDIITLVFFLKEKKSSVLLIHEDTPKETAIEMAKRANCIGILYGENSDFTKLEAVNYLAEEPSLLQYSSGTTGEPKLIRRAWTEVDTEIKVYNEALNCDIDEVPIVMAPVSHSYGLICGTLSAITRGSKPIIITNKNPKFALNIVRNTEKHIVYAVPLMLHIMGSFPQGTFQFHKIMTSGAPLPEALFYKLKETTTYMMQQYGCSEAGCISICHDMKSHLDLGNPLPHASISIGSDENAPEEIIVKMNDKEIFTKDLGYKSERGLHFMGRMDDVINVS... | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Catalyzes the adenylation of 3,4-dihydroxybenzoate (3,4-DHBA) to the corresponding AMP ester, followed by the transfer of the activated unit to the phosphopantetheine thiol of the ary... |
A0A0J1I1I3 | MRREALKNAVLKIMTEKMELKNVTHLEETMRLNQDLYIDSVMMLQLIVYIEMDVKLCVPEDEVDPKAFLTVGSLLDFMEELQPLQDVNVNN | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Aryl-carrier protein that activates 3,4-dihydroxybenzoate (3,4-DHBA) prior to its incorporation into petrobactin .
PTM: Activated by the transfer of a 4'-phosphopantetheine group from... |
Q81RQ5 | MTSIKVHCLVSCFCEIIKRRSDIDFRPFYFGLWDGDFDITEGGIISYHSENINHDHYLLWYEKLYGMKVNEWYDHAKDKDSNVETFLQLVENKPENRYVIVMVDMSLLPERENKFHQKPFPHYLMISETEKEEEWFMLDPDFRWEGNMEREKVLYSVQDNPFGGGYFIDVEEIQEPTAEMVASYFIETFKRNDNELTMELKNLIIKMANEEEGYLLSGLVAAVKQIPVLAIRKYSYEHAFAYFRETLQYSEQEFDYWCDRVEDIVQGFTNVQYRAIKMAMTNNKGMLLSIVEKLDEMNAIELQIKTELERQFLSWKEMKS... | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Transfers the activated 3,4-dihydroxybenzoate (3,4-DHBA) moiety from 3,4-DHBA-loaded AsbD to different receipient molecules, including N-citryl-spermidine, N8,N'8-citryl-bis(spermidin... |
Q81RQ4 | MKYSLCTISFRHQLISFTDIVQFAYENGFEGIELWGTHAQNLYMQEYETTERELNCLKDKTLEITMISDYLDISLSADFEKTIEKCEQLAILANWFKTNKIRTFAGQKGSADFSQQERQEYVNRIRMICELFAQHNMYVLLETHPNTLTDTLPSTLELLGEVDHPNLKINLDFLHIWESGADPVDSFQQLRPWIQHYHFKNISSADYLHVFEPNNVYAAAGNRTGMVPLFEGIVNYDEIIQEVRDTDHFASLEWFGHNAKDILKAEMKVLTNRNLEVVTS | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Catalyzes the conversion of 3-dehydroshikimate to 3,4-dihydroxybenzoate (3,4-DHBA) .
Catalytic Activity: 3-dehydroshikimate = 3,4-dihydroxybe... |
Q9M6A3 | MKNLDHIAASVDWEKESLPEYQDLIFLLFFALFFPVLRFILDRFVFEALAKRMIFGKKTVVNINGREERKKINKFKESAWKFVYFLSTELLALSVTCNEPWFTDSRYFWAGPGDVVWPNLKMKLKLKLLYMYAGGFYFYSIFATLYWETRRYDFAAQIIHHVTTVSLIVLSYVYGFARIGSVVLALHDGSDVFMEIAKMSKYSGFDLIADIFFSLFALVFTSLRIICYPFWIIRSTCYELLYVLDIQKERTTGIILYFVFNALLICLLVLHLFWFKIILRMVKNQILSRGHITDDVREDSESDDDHKD | Function: Mediates resistance to sphinganine-analog mycotoxins (SAMs) by restoring the sphingolipid biosynthesis. Could salvage the transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted cells after SAM exposure.
Location Topology: Multi-pass membrane protein
Sequ... |
A0A3G5BIB1 | MRFLNIFLFFAVMIAFVSASPVLEEEEIDIEPRITCDLIGNERLCVVHCLAKGFRGGWCDSRKVCNCRR | Function: The recombinant peptide moderately increases Kv11.1/KCNH2/ERG1 currents and shifts the voltage-dependence of the channel activation to hyperpolarised potentials . In vivo, induces neurotoxic effects when injected into insects (tested on L.cuprina and A.domesticus) .
Sequence Mass (Da): 7939
Sequence Length: 6... |
Q94BQ3 | MDNLSFHDGNIFNLLHTRSQDPSHEVDQRMQFHSSLVRRLSQEQELEGHQGCVNALAWNSNGSLLISGSDDLRINIWNYSSRKLLHSIDTGHTANIFCTKFVPETSDELVVSGAGDAEVRLFNTSRLSGRAEDDNAIIPSALYQCHTRRVKKLAVEPGNPNVVWSASEDGTLRQHDFRESTSCPPAGTAHQECRSVLLDLRSGAKRALADPPKQTLSLKSCDISATRPHLLLVGGSDAFARLYDRRMLPPLASSRKRMPPPPCVNYFCPMHLSERGRTNLHLTHVTFSPNGEEVLLSYSGEHVYLMNVNNGICSTGIMQY... | Function: May function as a substrate adapter for CUL4-DDB1 E3 ubiquitin-protein ligase complex (Probable). Negative regulator of fatty acid biosynthetic process and accumulation . Acts as an abscisic acid (ABA) negative regulator . Involved in responses to salt (NaCl) and osmotic (e.g. in response to mannitol and PEG)... |
P46993 | MTTLASSIEHKTKHLAAPFENDENPWMKKYCCQCKSCKMSVPVQPWLPRFFVFGILCPVFWLVNLLAWWFLQYWQPHELEFHDLQEDEYPGFYEYEAITKRTVIPIKEEVLQEIRVMQNFSDSNSEEYYESKDGMPSSFLNVNTEQVEDENDTLKKYRYAFLKKVAHDVLESHDLLRKTFRDWNLRSLLGLLIDSILIIFVVLLCKKSR | Function: Required for receptor inhibition of inappropriately expressed a-factor receptor (STE3) in MAT a cells. Inhibits signaling by relocalizing the G protein beta-gamma (STE4-STE18) subunit to intracellular membranes. May also be a mechanism for the down-regulation of the mating pheromone response after the zygotic... |
Q5BKW9 | MLPVVVVHGGAGHIPKERTEESTIGVKEAARTGYAILQRGGSAVDAVVEAVALMETNPRFNAGRGSVLNIKGEVEMDALVMDGRTLDSGAVSAVRRIANPVQLARLVMEKTKHLCLTAEGASKFARSMGVPEVPEESLITDYAKMRWKKNLEPDANPVECQMGKMGTVGAVAVDMDGNIACATSTGGMINKMEGRVGDTPCVGCGGYADNKIGAVSPTGHGEAIMKVTLSRLVLFHMEQGKTPEEASDLALAYMKERVDGLGGVVVVDHNGTWAARFSSLQMSWAAAQQGKLHFGLFHGDHFTEPVEEHT | Function: Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the bet... |
Q9VXT7 | MPRPVLLIHGGAGDISDSRIAGKFAGIKQALRSAWGLLSPDNGSGGGSALDAVEAAVRSMELDENFNAGYGSCLNTSGQVELEASLMEGRDLRAGCITLLRDVMHPITVARRLMEKQRHTFLGGAAAQELALATGSERLQPGALVTEGARLTLKEFEDQVAQGKDPFFARTELTDDKPVPKTDPSGETVGAVAMDASGQIVVGTSTGGITGKWPGRIGDTPILGSGTYADNCRGGVSTTGHGETLMRYNLAQRILSAMEYQGLSAQAAADKECREMTKRLGGTGGAIVVGHSGDLGISFTSRRMAWGYVQDGTIFYGIEG... | Function: Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the bet... |
Q7L266 | MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP | Function: Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl... |
P08243 | MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPFLPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEG... | Catalytic Activity: ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate
Sequence Mass (Da): 64370
Sequence Length: 561
Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.
EC: 6.3.5.4
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Q5UQE1 | MCGIICFIQYGGQKIDLVSCLNCLDKLNNRGPDAQSYQVIELGDITIFLGFTRLAIMDTSEAGLQPFKDNNSNYSICNGEIYNYKNLAEKFNIEMQSQCDCEILLPLFNLRGFEGLLSDLDAEFATVIVDKYNSKLYAARDKYGVRPLYYGYNCEKGLIGFASELKALHSVMEYVEQVKPNQYVTIDLSFRPSIPFDLQNFVKLFQFTNYHEYYQSHKSLIDYHEPNIEQLQTSINHLLTEAVRKRLYADRQIGFLLSGGLDSSLIVAIATRLLGPTNIVCFSVGFEGSPDVAAAREVVKFLGIKNHHIVPFSVDIGLNA... | Catalytic Activity: ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate
Sequence Mass (Da): 63335
Sequence Length: 550
Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.
EC: 6.3.5.4
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P78753 | MCGILAVHHVAEDIEAFKPKALHLSKQLRHRGPDWSGKAIRNQTILCHERLAIVGVESGAQPLVSDDGKLVLTVNGEIYNHLKLRENLKGNYKFKTYSDCEVILYLYREHGPACANMLDGMFSWVLYDQDKDKVVAARDPIGITTLYQGFSSDSPDTAYFASELKALHPVCDKIIAFPPGHYYDSETKQTVRYFKPSWWDENKIPSNPVDYKLLRETLEASVRKRLMAEVPYGVLLSGGLDSSLIASIAARETEKLANSTSQSEEARTITAWPKLHSFAIGLPGSPDLLAARKVADFLHTFHHEHTFTIDEGLDALRDVI... | Catalytic Activity: ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate
Sequence Mass (Da): 63241
Sequence Length: 557
Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.5.4... |
Q00624 | MRGVKLLAACLYLAAAATVVVHAEDPYFHHVWNVTYGTASPLGVPQQVILINGQFPGPNINSTSNNNVIINVFNNLDEPFLLTWNGIQHRKNCWQDGTPGTMCPIMPGTNYTYHFQPKDQIGSYFYYPTTGMHRAAGGYGGLRVNSRLLIPVPYADPEDDYTVLIGDWYTKSHTQLKKFLDGGRTIGRPDGIVINGKSGKGDGSDAPLFTLKPGKTYRVRICNVGVKTSINFRIQNHKMKLVEMEGSHVLQNDYDSLDVHVGQCFGTIVTANQEPKDYYMVASSRFLKTVITTTGLLRYEGGKGPASSQLPAGPVGWAWS... | Function: Probable oxidase that may be involved in pollen tube growth.
Sequence Mass (Da): 62131
Sequence Length: 555
Subcellular Location: Secreted
EC: 1.10.3.-
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P29162 | MGSGKVTFVALLLCLSVGVIAEDPYLYFNWNVTYGTIAPLGVPQQGILINGQFPGPRINCTSNNNIVVNVFNNLDEPFLFTWNGVQHRKNSWQDGTPGTMCPIMPGQNFTYRFQVKDQIGSYSYFPTTALHRAAGGYGALNVHSRALIPVPFDNPADEYNVFVGDWYNKGHKTLKKILDGGRTIGRPDGIIINGKSAKVGEAKEPLFTMEAGKTYRYRFCNLGMRSSVNIRFQGHPMKLVELEGSHTVQNIYDSLDLHVGQCLSVLVTADQEPKDYYLVVSSRFLKQALSSVAIIRYANGKGPASPELPTPPPENTEGIA... | Function: Probable oxidoreductase that may be involved in pollen tube growth.
Sequence Mass (Da): 62034
Sequence Length: 554
Subcellular Location: Secreted
EC: 1.10.3.-
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Q8LPL3 | MAVIVWWLLTVVVVAFHSASAAVVESTWEVEYKYWWPDCKEGIVMAINGQFPGPTIDAVAGDTVIIHVVNKLSTEGVVIHWHGIRQKGTPWADGAAGVTQCPINPGETFTYKFIVDKAGTHFYHGHYGMQRSSGLYGMLIVRSPKERLIYDGEFNLLLSDWWHQSIHAQELALSSRPMRWIGEPQSLLINGRGQFNCSQAAYFNKGGEKDVCTFKENDQCAPQTLRVEPNRVYRLRIASTTALASLNLAVQGHQLVVVEADGNYVAPFTVNDIDVYSGETYSVLLKTNALPSKKYWISVGVRGREPKTPQALTVINYVDA... | Cofactor: Binds 4 Cu cations per monomer.
Function: Ascorbate oxidase involved in a redox system involving ascorbic acid (AsA) . The oxidation of AsA represses responses to high salinity and oxidative stress conditions such as vegetative growth and seed production reductions . Negative regulator of defense responses to... |
M4DUF2 | MGMWWIVAVAILAHTASAAVREYAWEVEYKFGWPDCKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAP... | Cofactor: Binds 4 Cu cations per monomer.
Function: Ascorbate oxidase involved in a redox system involving ascorbic acid (AsA) . The oxidation of AsA represses responses to high salinity and oxidative stress conditions such as vegetative growth and seed production reductions (By similarity). Negative regulator of defen... |
A0A2S1XB67 | MIKKVPIVLSIFCFLLLLSSSHGSIPEAFLNCISNKFSLDVSILNILHVPSNSSYDSVLKSTIQNPRFLKSPKPLAIITPVLHSHVQSAVICTKQAGLQIRIRSGGADYEGLSYRSEVPFILLDLQNLRSISVDIEDNSAWVESGATIGEFYHEIAQNSPVHAFPAGVSSSVGIGGHLSSGGFGTLLRKYGLAADNIIDAKIVDARGRILDRESMGEDLFWAIRGGGGASFGVIVSWKVKLVKVPPMVTVFILSKTYEEGGLDLLHKWQYIEHKLPEDLFLAVSIMDDSSSGNKTLMAGFMSLFLGKTEDLLKVMAENFP... | Function: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts O-acetylstemmadenine (OAS) to reactive acetylated intermediates, likely dihydropreco... |
P37064 | SQIRHYKWEVEYMFWAPNCNENIVMGINGQFPGPTIRANAGDSVVVELTNKLHTEGVVIHWHGILQRGTPWADGTASISQCAINPGETFFYNFTVDNPGTFFYHGHLGMQRSAGLYGSLIVDPPQGKKEPFHYDGEINLLLSDWWHQSIHKQEVGLSSKPIRWIGEPQTILLNGRGQFDCSIAAKYDSNLEPCKLKGSESCAPYIFHVSPKKTYRIRIASTTALAALNFAIGNHQLLVVEADGNYVQPFYTSDIDIYSGESYSVLITTDQNPSENYWVSVGTRARHPNTPPGLTLLNYLPNSVSKLPTSPPPQTPAWDDF... | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: May be involved in a redox system involving ascorbic acid.
Catalytic Activity: 4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical
... |
Q40588 | MASLGFLFFFLLPLILLELSSSRSVMAAKTRHFKWDVEYIHWSPDGEESVVMGINGQFPGPTIRAKAGDTVAVHLTNKLHTEGVVIHWHGIRQIGTPWADGTAAISQCAINPGETFLYRFKVDKAGTYFYHGHYGMQRSAGLYGSLIVEVGEGEKEPFHYDGEFNLLLSDWWHKGSHEQEVDLSSNPLRWIGEPQTLLLNGRGQYNCSLAARFSKPPLPQCKLRGGEQYAPQILRVRPNKIYRLRVASTTALGSLSLAIGGHKMVVVEADGNYVQPFSVQDMDIYSGESYSVLFKTDQDPTKNYWISINVRGREPKTPQG... | Cofactor: Binds 4 Cu cations per monomer.
Function: May be involved in a redox system involving ascorbic acid.
Catalytic Activity: 4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical
Sequence Mass (Da): 64865
Sequence Length: 578
Subcellular Location: Secreted
EC: 1.10.3.3
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Q03168 | MLIKSIIALVCLAVLAQADFVRVQLHKTESARQHFRNVDTEIKQLRLKYNAVSGPVPEPLSNYLDAQYYGAITIGTPPQSFKVVFDTGSSNLWVPSKECSFTNIACLMHNKYNAKKSSTFEKNGTAFHIQYGSGSLSGYLSTDTVGLGGVSVTKQTFAEAINEPGLVFVAAKFDGILGLGYSSISVDGVVPVFYNMFNQGLIDAPVFSFYLNRDPSAAEGGEIIFGGSDSNKYTGDFTYLSVDRKAYWQFKMDSVKVGDTEFCNNGCEAIADTGTSLIAGPVSEVTAINKAIGGTPIMNGEYMVDCSLIPKLPKISFVLG... | Function: May degrade organelles involved in the biosynthesis and secretion of vitellogenin.
Sequence Mass (Da): 41790
Sequence Length: 387
Subcellular Location: Lysosome
EC: 3.4.23.-
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O07002 | MSKQGNFQKSMSLFDLILIGMGAIFGSAWLFAVSNVASKAGPSGAFSWILGGAIILLIGLVYAELGAALPRTGGIIRYPVYSHGHLVGYLISFVTIVAYTSLISIEVTAVRQYVAYWFPGLTIKGSDSPTISGWILQFALLCLFFLLNYWSVKTFAKANFIISIFKYIVPITIIIVLIFHFQPENLSVQGFAPFGFTGIQAAISTGGVMFAYLGLHPIVSVAGEVQNPKRNIPIALIICIIVSTIIYTVLQVTFIGAIPTETLKHGWPAIGREFSLPFKDIAVMLGLGWLATLVILDAILSPGGNGNIFMNTTSRLVYAW... | Function: Uptake of L-aspartate with the concomitant import of a proton. Can also transport aspartate hydroxamate and L-glutamate with lower affinity and efficiency.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56989
Sequence Length: 520
Subcellular Location: Cell membrane
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P83712 | NVVVLATGGTIAGAGTNAFASQXGPLGMVVEGK | Catalytic Activity: H2O + L-glutamine = L-glutamate + NH4(+)
Sequence Mass (Da): 3099
Sequence Length: 33
Subcellular Location: Periplasm
EC: 3.5.1.38
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P10182 | KEVENQQKLANVVILATGGTIAGAGASAANSATYQAAKVGVDKLIAGVPELADLANVRGEQVMQIASESITNDDLLKLGKRVAELADSNDVDGIVITHGTDTLEETAYFLDLTLNTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASNKDSRGKGVLVTMNDEIQSGRDVSKSINIKTEAFKSAWGPLGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYSYGNVTDTAYKALAQNGAKALIHAGTGNGSVSSRLTPALQTLRKTGTQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPEKARILVELA... | Catalytic Activity: H2O + L-glutamine = L-glutamate + NH4(+)
Sequence Mass (Da): 36200
Sequence Length: 337
Subcellular Location: Periplasm
EC: 3.5.1.38
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O60020 | MISDTVIAILAVALVGSTVQAAPVDATATSTSGIIAVPISKSAAQLAREADPVVSLDWLKKTKAQAQYKHKQANARLHSKRATGASVLTDQGSESLWTGPITIGGQSFTVDWDTGSSDLWVPSSACSSAACNAHHKYTLTSTGKKQSGTFSISYGDGSSASGPVYKDNVVASGLQATSQVFGAVTSESSSFSSDPSDGISGLGWPALAQLSGTSYFWSLINQGTVTSPVFSFRLATTNSELYLGGINSAHYTGAITYTPVTQKAYWTIALGGVSVNGAAINPSVSSAIIDTGTTLVYGPTAGVAALYAKIPGSASMADTY... | Function: Possesses acidic protease activity. Hydrolyzes casein and azoalbumin in vitro.
Sequence Mass (Da): 41370
Sequence Length: 405
Subcellular Location: Secreted
EC: 3.4.23.-
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O04057 | MASYHSKAAFLCLFLLVSFNIVSSASNDGLLRVGLKKIKLDPENRLAARVESKDAEILKAAFRKYNPKGNLGESSDTDIVALKNYLDAQYYGEIAIGTPPQKFTVIFDTGSSNLWVLCECLFSVACHFHARYKSSRSSSYKKNGTSASIRYGTGAVSGFFSYDNVKVGDLVVKEQVFIEATREPSLTFLVAKFDGLLGLGFQEIAVGNAVPVWYNMVEQGLVKEPVFSFWLNRNVEEEEGGEIVFGGVDPKHYRGKHTYVPVTQKGYWQFDMGDVLIDGEPTGFCDGGCSAIADSGTSLLAGPTPVITMINHAIGAKGVV... | Function: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles.
Sequence Mass (Da): 55856
Sequence Length: 513
Subcellular Location: Vacuole
EC: 3.4.23.-
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P42210 | MGTRGLALALLAAVLLLQTVLPAASEAEGLVRIALKKRPIDRNSRVATGLSGGEEQPLLSGANPLRSEEEGDIVALKNYMNAQYFGEIGVGTPPQKFTVIFDTGSSNLWVPSAKCYFSIACYLHSRYKAGASSTYKKNGKPAAIQYGTGSIAGYFSEDSVTVGDLVVKDQEFIEATKEPGITFLVAKFDGILGLGFKEISVGKAVPVWYKMIEQGLVSDPVFSFWLNRHVDEGEGGEIIFGGMDPKHYVGEHTYVPVTQKGYWQFDMGDVLVGGKSTGFCAGGCAAIADSGTSLLAGPTAIITEINEKIGAAGVVSQECK... | Function: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles.
Catalytic Activity: Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.
Sequence Mass (Da): 54226
Sequence Length: 50... |
C0HJJ8 | GTQTNAPWGLARLIS | Function: Protease capable of hydrolyzing gelatin and cell surface heparan sulfate proteoglycans (HSPGs) in vitro.
Sequence Mass (Da): 1585
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.21.-
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E3PJ88 | MSIKQMPGRVLISLLLSVTGLLSGCASHNENASLLAKKQAQNISQNLPIKSAGYTLVLAQSSGTTVKMTIISEAGTQTTQTPDAFLTSYQRQMCADPTVKLMLTEGINYSITINDTRTGNQYQRKLDRTTCGIVKA | Function: Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). Required for correct assembly of the type II secretion system-beta (T2SS-beta), for localization of GspD-beta to the cell outer membrane and for export of ... |
Q8L3K8 | MNAIGNFLVGTPVFTIFICLALGYLLGKLKIGSFTLGATVGVLIVALLIGQLGVFPRDTLLGDIFFDFFMFAIGYRVGPSFISSMKKFGAKIVYATLIFLVSAFIVAYACFKMFHIGPGIAAGIIAGGLTQSAVIGSSLETISKLPISDHLKTLYSNQIPIVYTLTYVFGTIGVLIFLRDIMPKLMHIDLKKQAVKTAKELDMIPVPVIVASTHFYTINDGSSLIGQTLGTVNTKFAKGLVAAGLNDSADMASVINAGDVLAISGGIDEIGRAVQEFNLLEVTGKTKAYVSKQVVLKKNFSADVLKNAQDKGVLVATLAG... | Function: Catalyzes the electrogenic exchange of aspartate with alanine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57213
Sequence Length: 543
Subcellular Location: Cell membrane
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Q1QVN0 | MSDVKKVVLAYSGGLDTSVIVKWLQETYDCEVVTFTADIGQGEEVEPARAKAQALGVKEIYIEDLREEFVRDYVYPMFRANTIYEGEYLLGTSIARPLIAKRLVEIANETGADAISHGATGKGNDQVRFELGAYALKPGVKVIAPWREWDLNSREKLMNYCEEHDIPVDFSTSKKKSPYSMDANLLHISYEGGILEDPWAEAEEDMWRWSVSPEAAPEQPTYVELTFDKGDIVAIDGEPLKPHEVLSRLNRMGGDNGIGRLDIVENRYVGMKSRGCYETPGGTIMLRAHRAIESLTLDREAAHLKDELMPKYAEVIYNGY... | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 45409
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: ... |
C1FU68 | MKEKVVLAYSGGLDTSIIIPWLKENYDLDVIAVCVNVGQGDDMDYVKTKAIKSGASKIYVEDVKEEFVVDYLYKAIKSEALYEQDYMLGTSFARPLMAKKLVEIAHKEQAKYICHGCTGKGNDQVRFEVGVKAQDPIIKIIAPWRIWDIKSREDAIDYAKKVGVEVPVTKKKIYSVDKNLWHVSHEGGDLEDLKNEHKEDMYFMVTPPEKAKNEPTYLEIYFEKGAPVKINGEVLNPVDIIDKLNTIGGENGIGIADIIENRLVGMKSRGIYETPAGTLLYAAHKKLESVTLDKYTYQYKKIVSAQYGELVYNGLWFTSL... | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 44742
Sequence Length: 397
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: ... |
Q186Z6 | MKEKVVLAYSGGLDTSIIIPWLKENYEDIDVIAVCGNVGQEDKMEDVYEKALQSGASKAYVDDISEEFVTETIFKAVKAEAKYEGKYLLGTSLARPIIAKKLVEVAHKEGAKYICHGCTGKGNDQVRFEATIAALDPTIKVIAPWRIWDIKSREDAIDYAEKHNIKVTATKAKIYSVDANLWHVSTEGGDIEHLENEHKKDVYKQCVDPEDACDVAEYVEVYFEKGVPKKVNGEELSPVALIHKLNELGCKHGIGVIDIVENRLVGMKSRGIYETPGGTILYEAHNILESATLDKDTLHFKQMVSYKYGELIYNGLWYCK... | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 44624
Sequence Length: 399
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: ... |
Q827Z1 | MQCEEKPVTERVVLAYSGGLDTSVAIGWIAEETGAEVIAVAVDVGQGGEDLDVIRKRALACGAVEAEVADAKDEFADEYCLPAVKANALYMDRYPLVSALSRPTIVKHLVAAAQKHGATTVAHGCTGKGNDQVRFEAGIVALAPGLKCIAPVRDYAMTRDKAIAFCEEKRLPIATTKKSPYSIDQNVFGRAVETGFLEDIWNAPIEDIYEYTSNPAEPREADEVVISFKEGVPVAIDGRPVTVLQAIQQLNERAGAQGVGRIDMVEDRLVGIKSREVYEAPGAIALITAHQELENVTVERELARYKRQVEQRWGELVYDG... | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 44066
Sequence Length: 404
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: ... |
Q06734 | MSKVLTSLPAGERVGIAFSGGLDTSVAVAWMRDKGAVPCTYTADIGQYDEPDIASVPSRASAYGAEITRLVDCRAALVEEGLAALACGAFHIRSGGRPYFNTTPLGRAVTGTLLVRAMLEDGVQIWGDGSTFKGNDIERFYRYGLLANPHLRIYKPWLDADFVTELGGRKEMSEWLLAHGLPYRDSTEKAYSTDANIWGATHEAKTLEHLDTGIETVDPIMGVRFWDPSVEIATEDVTVGFEQGRPVSINGKEFASAVDLVMEANAIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIVYERLVNAIHNEDTLAAY... | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 52383
Sequence Length: 482
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: ... |
Q04MW7 | MSKEKVILAYSGGLDTSVAITWLKKDYDVVAVCMDVGEGKDLDFIHDKALKVGAVESYVIDVKDEFATDYVLVAHQSHAYYEQKYPLVSALSRPLISKKLVEIAHQIGATTIAHGCTGKGNDQVRFEVSIAALDLNLKVIAPVREWKWSREEEIYYAKENGVPVPADLDNPYSVDQNLWGRANECGILENPWNQAPEEAFGITTSPEQAPDMPEYIEIEFSEGVPVSLNGEVLKLADLIQKLNEIAGKHGVGRIDHVENRLVGIKSREIYECPGAVTLLTAHKEIEDLTLVREVAHFKPIIENELSNLIYNALWFSSATQ... | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 44065
Sequence Length: 398
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: ... |
Q87Q40 | MTKSLFRQSFLTDTLDVHIDVAPAEQVLSNGVQLKLYQRGVLEVIPENPTQETKNIIISCGIHGDETAPMELVDSIIKDIESGFQKVDARCLFIIAHPESTLAHTRFLEENLNRLFDEKEHEPTKELAIADTLKLLVRDFYQDTEPKTRWHLDLHCAIRGSKHYTFAVSPKTRHPVRSKALVDFLDSAHIEAVLLSNSPSSTFSWYSAENYSAQALTMELGRVARIGENALDRLTAFDLALRNLIAEAQPEHLSKPCIKYRVSRTIVRLHDDFDFMFDDNVENFTSFVHGEVFGHDGDKPLMAKNDNEAIVFPNRHVAIG... | 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): 38837
Sequence Length: 342
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate... |
Q2UEK7 | MLPTLPNIAGRINTMATFLLPVAIGTIILLFLYGKYVTSTLIPGPPTLPLIGNLHQLPSDDRRHVLAQWHKKHGPIISLKFGWSSVVILGNIAVTKELFGKRSLKYGSRPRMVMARDCMTKQMQTSTLPWGEKWKIHNRIQLSLVGGPKIRSYQSLLDIESCKVLYQLLSTESLVTCFNRFKFNIIYTLAYGKDPDQNESDFHEILELADHFTQTLTNATWVVDLFPILNCLPRRLAPWKAVGDDFHRRAMGWFRRNSEAAVKSNSWNWTKHVQFNEDTGNLSVSEMQYLIGVLFEAGVDSTATVLHFFVLACTLYPDAV... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catal... |
Q2UEK8 | MGEQTEFEPIQLSPLDQAIPPVYIRILLCFSVVNVDRAISQLQTGVSSLLSALPFLSGDVVRYTAPGKTKWLYQLCPPTHQVQATGVLVVKHHQMRCMVDEKRFAPSSTSHIPLSPFAEPARPAPIFRVQANAYIDGITLGFAFHHIAVDATGMGVIISELARHCRSSPPPSLLCPDYERATRQLISNSRATECSGLDHSGDYISCQALSPPAEGSEDASPSIEISTETRTFVFPAARLESLKNACIEMLPTLDQQQRQQNPCLDEPARTKVPWLSTNDVFVALLWVCLTRCRYQEDQNSGLPSDEHTRICMGVNMRSRI... | Function: O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the f... |
P80358 | MIVRPVTSADLPALIELARSTGTGLTTLPANEQRLQHRVSWAEKAFRGEAERGDADYLFVLEDDAGKVVGISAIAGAVGLREPWYNYRVGLTVSASQELNIHREIPTLFLANDLTGNSELCSLFLHADHRSGLNGKLLSRARFLFIAEFRHLFGDKLIAEMRGMSDEEGRSPFWESLGRHFFKMEFSQADYLTGVGNKAFIAELMPKFPLYTCFLSEEARGVIGRVHPNTEPALAMLKAEGFSYQGYVDIFDAGPAIEAETDKIRAIAESQNLVLAVGTPGDDAEPYLIHNRKREDCRITAAPARAAAGTLVVDPLTAKR... | Catalytic Activity: L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine
Sequence Mass (Da): 37245
Sequence Length: 340
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5.
EC: 2.3.1.109
|
Q2UEK9 | MTDISTGVQLKPGIGDGTVYNGNMSKDTLVNCSPDPENPEKGQASSPRTQISVDDNEESTTEYPSSWKLAMIMISLCLAVFCLALDTTIMATAIPKIADQFNSLNDVGWYGSAYLLTTSALTLSFGKLYSFYSIKWVYLQALGMFEIGSLICGATPNSLGLIIGRAIAGSGSAGIYSGSMLIVARSAPLERRPLLTGILGGLFGVASVVGPLIGGAFTDNLSWRWCFYINLPLGAVTGLFLILFFDGAKATTQRATIRDQLSQLDLLGSLCFLPAIICVLLALQWGGTTYPWHDGRIIALFTVFGVLLLAFAGVQWWRQE... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . Seems not to be involved in astellolides translocation .
Location Topology: Multi-pass membrane protein
Seque... |
Q2UEL0 | MTRQSHYQAIILDLGNVVFEWDTSQNPPTAAPNQISLLRTSMKSPVYHSYERGQLSTEECHRLLGESLHVDPGQIKEAFDLARQSLRSNPALLDFIRQLKQTRGVAVYAMSNIPQAEIEYLKESRAGDMEVFDEVFASGYVGSRKPETEFYRRVMGEIGLKAERVVFVDDKEENVDVARGLGLYGVCFGGVEELRGHLLGI | Function: Sesquiterpene phosphatase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes... |
Q2UEL1 | MSRRFPIQVAQSEIPPIAWGLWRMVYRLWLHPLSGYPGPRLAAVSNLPYFAWTCTGNLHLRLQELHKVYGDVIRIRPNALTYRTPEAWTDIYGHRKPGTLPFSKDPEFFMPAQAGSSHMINANEKDHTRQKRLLNHAFSERSLRQQEHLIMGYIDLFIQRLRGQARMGAETVNMEEWLNFLTFDIIGDLAFGEPFGCLQNSEYHPWVATIFKSIKTGAILRALNIYPILLGFIRRFLPKSLVQKRIAHYQMSKDRVTRRLQTETSRPDFISYILKYNDDRGMSTPEIEMNAALLIQAGSETTATVLAACLYFLQKNAACH... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catal... |
P42662 | MDLKMLLIFTAFLLPAVLGFPIQDNYENSTATSESTQVTTEESIYDSPSPTETDSEDDVIFNRILEVNKDSSRYLQEGDIVPRRSRSAFNCRNCYWPQSMDGIVRIPYVLDPTYEENHVRGILEAMAEFETLTCINFVKRKTERDYLIIRSADGCWSNYGKVGGGQTVSVMKGGCMWKGIIQHELDHALGFLHEHSRSDRDKYVKIMWEYISPACRPDFRKFENSNNLGLPYDYSSVMHYGPHTFTNTTGKATIVPVPDGSVHIGQRLGLSNLDVAKINKLYNCSRCSTIIDAAFGSLKSANYPRNYSDNTNCVWLIRTR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization (By similarity). Protease which may play a role in the breaking down of the vitelline membrane (days 0-5) and possibly, in the digestion of the egg white (days 9-12) .
Sequen... |
P33879 | MSKETKKPFRQSVAEWRQFVYNPNSGEFLGRTAKSWGLILLFYLVFYGFLAALFTFTMWVMLQTLSNDIPKYRDRISSPGLMISPKPDTALEFYFNKSDAQSYAEYVSTLRKFLETYDDSKQSQNINCTPGKVFDQNDVAVKKACRFNLSELGQCSGKEDKTFGYSKGTPCVLVKMNRIIGLKPEGEPYIQCTSKEPGAVEINYFPSGGLIDLMYFPYYGKTLHAHYLQPLVAVQLAINSNSTNEEIAIECKILGSPNLKNEDDRDKFLGRIAFKVEMTE | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31859
... |
P54709 | MTKNEKKSLNQSLAEWKLFIYNPTTGEFLGRTAKSWGLILLFYLVFYGFLAALFSFTMWVMLQTLNDEVPKYRDQIPSPGLMVFPKPVTALEYTFSRSDPTSYAGYIEDLKKFLKPYTLEEQKNLTVCPDGALFEQKGPVYVACQFPISLLQACSGMNDPDFGYSQGNPCILVKMNRIIGLKPEGVPRIDCVSKNEDIPNVAVYPHNGMIDLKYFPYYGKKLHVGYLQPLVAVQVSFAPNNTGKEVTVECKIDGSANLKSQDDRDKFLGRVMFKITARA | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31513
... |
Q63377 | MTKTEKKSFHQSLAEWKLFIYNPTSGEFLGRTSKSWGLILLFYLVFYGFLAALFTFTMWVMLQTLNDEVPKYRDQIPSPGLMVFPKPPTALDYTYSMSDPHTYKKFVEDLKNFLKPYSVEEQKNLTDCPGGALFHQEGPDYSACQFPVSLLQECSGVNDSNFGYSKGQPCVLVKMNRIIELVPDGAPYITCITKEENIANIVTYPDDGLIDLKYFPYYGKKRHVGYRQPLVAVQVIFGADATKKEVTIECQIDGTRNLKNKNERDKFLGRVSFKVIAHA | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31830
... |
P30716 | MAKEENKSGEQSSSEWKQFIYNPSSGEILGRTASSWALILLFYLVFYGFLAGLFTLTMWVMLQTLDDSVPKYRDRVSFPGLMISPKSAGLEISFSKSDKSHMKSILKFFTHFYHHTMTPYKLQMCSARKAITTEQEGVEEKKSCQFNRSSLGPCAGLEGNEYFGYNDGSPCVLVKMNRIIGLKPDGNPHINCTSKAENISLQYYPEYGKIDLMYYPYYGKKTHVNYVQPLVAVKITPSNSTGTSEIVLECKLYGSPNLKNNDDRDKFLGRVNFKLEIKD | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of this glycoprotein is not known. Some specific sequence of the beta subunit can modulate the activation of the Na,K-... |
P21188 | MAKEENKGSEQSGSDWKQFIYNPQKGEFMGRTASSWALILLFYLVFYGFLAGLFTLTMWVMLQTLDDSVPKYRDRVSSPGLMISPKSAGLEIKFSRSKTQSYMEYVQTLNTFLAPYNDSIQAKNEFCPPGLYFDQDEEVEKKTCQFNRTSLGICSGIEDPMFGYGEGKPCVIVKINRIIGLKPEGNPKINCTSKTEDVNLQYFPDNGKIDLMYFPYYGKKTHVNYVQPVVAVKISPSNFTSEEIAVECKIHGSRNLKNEDERDKFLGRVTFKVKITE | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31570
... |
Q2HZ96 | MEPGMEMNTASEGGTRRGPENKHEEKVQDPNRGEAETKAEMGNKTWADLAGEMKTFLWNPEERTCMGRTAKSWGLILLFYFIFYTCLAGMFAFCMYVMLLTLSPYTPTYRDRVSPPGVMIRPYLNGFTIAFNVSKPSTWQPYVDSMHQFLAAYDDKVQEEKNIECISGQYFIQGGNDSEEKKACQFKRSLLQNCSGIEDPTFGFSKGQPCILLKMNRIIGYRPGAGVPVNVDCKVQKGNESDLRSVDFYPGNGTFDLMYYPYYGKLTHVNYTSPLVAMHFTDVKRNSLVHIQCKLNGKGIINDVNSDRFLGRIIFTLSIG... | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane.
PTM: Glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36363
Sequence Length: 321
Subcellular Loc... |
Q9UN42 | MRRQLRSRRAPSFPYSYRYRLDDPDEANQNYLADEEEEAEEEARVTVVPKSEEEEEEEEKEEEEEEEKEEEEGQGQPTGNAWWQKLQIMSEYLWDPERRMFLARTGQSWSLILLIYFFFYASLAAVITLCMYTLFLTISPYIPTFTERVKPPGVMIRPFAHSLNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGNEDEDKKACQFKRSFLKNCSGLEDPTFGYSTGQPCILLKMNRIVGFRPELGDPVKVSCKVQRGDENDIRSISYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVV... | Function: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 41598
Sequence Length: 357
Subcellular Location: Nucleus inner membra... |
Q202B1 | MATTAGEQANYLQSADSMSDGRQHHPEEAGEKKQEEQKKSWGEWLQDLKIFIWNPEKKEVLGRDKKSWALILLFYFILYCFLAGLFALCIYGLLATISPYVPTYRDRVFPPGLTIRPQFNALYFSFNPSDRSTWSSHAESLNTFLEDYNDEIQQEKNLECTPGKYFFQPGEDHEERKACQFRRSLLKNCSGIEDPTFGFAQGKPCILLKMNRIVGYQAGSGIPIYVTCEILKADASYLGPVNFYPSDKFDLMYYPYYGKLTHVNYTSPLIAMQFTEVKNNQDINIQCKINGKDIISDHDKDRFLGRVAFTLHIG | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane.
PTM: Glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36129
Sequence Length: 314
Subcellular Loc... |
P28774 | MAKGKQKKGKDLNELKKELDIDFHKIPIEECYQRLGSNPETGLTNAQARSNIERDGPNCLTPPKTTPEWIKFCKNLFGGFALLLWTGAILCFLAYGIEASSGNEDMLKDNLYLGIVLATVVIVTGIFSYYQENKSSRIMDSFKNLVPQYALALREGQRVTLKAEELTMGDIVEVKFGDRVPADLRVLEARSFKVDNSSLTGESEPQARSPEFTNDNPLETKNLAFFSTNAVEGTMRGIVIGIGDNTVMGRIAGLASGLDTGETPIAKEIAHFIHIITGVAVFLGVTFFIIAFVLGYHWLDAVVFLIGIIVANVPEGLLAT... | 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... |
A0A068BGA5 | MASFPPSLVFTVRRKEPILVLPSKPTPRELKQLSDIDDQEGLRFQVPVIMFYKRKLSTEGEDPVKVIREALAEALAFYYPFAGRLIEGPNRKLMVDCTSEGVLFIEADADIELNQLIGDTIDPGTYLDELLHDVPGSEGILGCPLLLIQVTRFRCGGWAFAIRLNHTMSDTLGLVQFLTTIAEFTRGAEGAPSVPPVWQREFLAARQPPFIPFQHHEYEQVIDTTPDDNKKSMTHKSFFFGPKEIRAIRSHLPLHHRSTSSTFDVLTACLWRCRTCALVLDPKKTVRISCAASGRGKHDLHVPRGYYGNVSAFPATVLRA... | Function: Involved in the biosynthesis of volatile esters which confer kiwifruit flavor . Alcohol acyl transferase that can use a wide range of alcohols as substrate to produce esters . Exhibits benzoyl-CoA:alcohol O-acyltransferase activity .
Catalytic Activity: 3-(methylsulfanyl)propanoyl-CoA + butan-1-ol = butyl 3-(... |
A1L209 | MKMEDMSLSGLDNTKLEALAHDVYSDLVEDACLGLCFEVHRAVKQGYFFLDETDQESMKDFEIVDQPGVDIFGQVYNQWKNKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIASSNNTSKSESDQEDNDDINDNDWSYGSEKKAKKRKSEKNPNSPRRSKSLKHKNGELSGSVNPDMYKYNYSSGISYETLGPEELRSILTTQCGVVSEHTKKMCTRSQRCPQHTDEQRRAVRVFLLGPSASTLPDADTMLENEAYEPPDGQLIMSRLHWDASSDISPSDSASSKASTNNSESKRPKKKKPSTLSLTPAGER... | Function: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone ... |
Q14CW9 | MKMEEMSLSGLDNSKLEAIAQEIYADLVEDSCLGFCFEVHRAVKCGYFFLDDTDPDSMKDFEIVDQPGLDIFGQVFNQWKSKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIANSNNMNKSESDQEDNDDINDNDWSYGSEKKAKKRKSDKNPNSPRRSKSLKHKNGELSNSDPFKYNNSTGISYETLGPEELRSLLTTQCGVISEHTKKMCTRSLRCPQHTDEQRRTVRIYFLGPSAVLPEVESSLDNDSFDMTDSQALISRLQWDGSSDLSPSDSGSSKTSENQGWGLGTNSSESRKTKKKKSHLSLVGT... | Function: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both his... |
O14261 | MRFRLNDSFSGKSWTIDNVQWTPQNLVAWIMELNIGLSDEAKLLLPNGMSLNETVLNSESDVVIYVLDQNLLTFTYDGDKIPSIPSLKGQPISNVLTGIIADSSSDQWKDKISKCLSLLSDILESSSKIHNQLSVCHDEYSTSIVSPEVAMNYLQRRQSGMKDLLFVFYERLDRVSVSDLLHDFLALPTGSLPITPLKILSTNWTKLDSWLNSISARYAEAQKRVQQCIGAANSIIVSPFKEVPSIKEGDDAYYHLRSVAQDAANILQEILKIESTSTTSQIKPKCNYETEITDCMEKLQSNLSELKSSRKSSLISLKSF... | Function: Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the preautophagosome (PAS), the site of vesicle/autophagosome forma... |
Q6CFR0 | MSEIRVSCASSGVSVSAARDQFSSLPHLKAWIELEFSVSVSEQLLLTVAAEQVKMAHLGTQNELFVFDRSVVGGTVSNEHKYSAPKLKTLTPGTDPSQWALTVLTHCSRLVEETKRVTAEIATIKRATNVAITQMKQHSQNLDKNLLNVKEYSKELNQGITPLLSVDLAQLRDNTRAVKLVAPAVFGKKQFLNDWLDLQQLQSIVVEFKADFPSCMDKLQTLEQDLAQLSKDTQTLVNSTDVWIGGTNSDVLCNEAVGILRKLSELTSGDHVTNEAVKSVQNCQSQILDLHKALSKAKFQTVQHSQKVLQSISQLQSRST... | Function: Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome form... |
Q6BH63 | MSDDTEWSEDILNRLNVRDQYEKKDSRYFKAFSQLSQEARTNDQASNNDKSIEYNKLLKENNQLKKDNEILTTSLNQTTISLEKSDLKINQLLKSQDQLERHNTSLNNKIKHLNLEIIEKNKSVEILNDELLLNEIQTNVLNDKITRLSDENKKLVERWIEKAKSDAEKLNDANEFLESVNRK | Function: Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticul... |
Q5BH90 | MAHWREEYAAALAARDRREKANVAIYNAYSQLADRTASSMIAVSDLQSDAQRSALSTPVADPRQQQPSPASGPSPQDIILAIRADLAEAQRSRSELEEQLARVTTELEKLRRRNIQNGKRISSMESEITHLQLRLKDRDEELREKAKLLEGFQDEIATFELQLNMAEERSNRLQKENQELIDRWMARMGKEADAMNDAYQFS | Function: Stabilizes the atg5-atg12 conjugate which is necessary for autophagy. The atg5-atg12/atg16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticul... |
I1RFS8 | MPNWRDQYLSGIKDAELNNPVNMELVQTCSQMADRISALEAEKNGLETLVTTNGKTTARPTEPSTNDPAVAQLKQDLAEALRSKGVAEKRLRSSEEELLQLRSKHKTNTRSIRDLTADKNSLTTRLKDREYELREKRKFIEQVQDEMIALNLQMSMAEKERDKVKKENKELVDRWMKRMAQEAEAMNLANEPIFKKGR | Function: Stabilizes the ATG5-ATG12 conjugate (By similarity). The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS) (By similarity). Recruits also ATG3 to the PAS (By similarity). Involved in endo... |
W0T661 | MEYELLESIRARDLVDKRFSQLFEEVPLVPKLEKAGEGDTNVKESSIKNLKDYLKLRDEEVYKLKDILKLKNRDTERLNDELLSANIESNLLQERLEKLQQEYDRLIERWLLKAQKEADTMNSHFK | Function: Stabilizes the ATG5-ATG12 conjugate (By similarity). The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS) . Recruits also ATG3 to the PAS (By similarity). Involved in endoplasmic reticul... |
Q520U5 | MSSLPDWRDEYLASIKEAEKNSPVNRDLVEACSQLQDRVAALEAERDALKASGASAGQSASDPASQSGDAAQSAVVARLRLDLAEALGTQERLQSRLGLAESELERLRAKTAEDAKTIRTLNTQCVSLSTKVKDRNEELQGKSKLVENVQDELIALTLQLNVMEQQKAKIQAENDQLVERWMKRMGQEAEAMNLANEPKFAKRG | Function: Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticul... |
A7KAK0 | MSWKNDLLAKLAQRDKSMETQKDVFLSFQFLSTRIASLERQLDTVQRDDSKKTVLDLLGEIDQLKQKLDLAEDSLKHETAKNKELVKELSTVKNNLNILTDGYKKLQERHLRLQEESKIKFQNLESLNDDILSLNIENNLLNDRMAKLKQENESLIERWMKRVKQEAEVLNDANEALSRSEKSLKPEG | Function: Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticul... |
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