ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P46960 | MAVLLRDKHISYLHDIGNRTDELDFWLKEHLHVSAIYWSCMSFWLLKKKDQIDKERIVSFLLSCLTESGGFACYPGHDDHITNTVYAVQVLAMLDSLHVVDKDKVASYIIGLQNEDGSMKGDRWGEIDARFLYSGINCLAILGKLDYLNKNTAVDWLMKCYNFDGGFGLCPGAESHGAMVFTCVAALKILNKLDLIDEELLGWWISERQVKGGGLNGRPEKLPDSCYGWWDLSPLAIIGKLDWIDRNQLIDFLLGTQDADSGGFADRKEDATDVYHTCFSLAGLSLLQFPNIEPVDPRFCLPLEVTQKMKL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-gera... |
P20133 | MSGSLTLLKEKHIRYIESLDTKKHNFEYWLTEHLRLNGIYWGLTALCVLDSPETFVKEEVISFVLSCWDDKYGAFAPFPRHDAHLLTTLSAVQILATYDALDVLGKDRKVRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVVDPAVDFVLKCYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLEEIGWWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSLAIIGRLDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLSLMGYDNLVPIDPIYCMPKSVTSKFK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein]... |
P85868 | MKTPITEAIASADTQGRFLSNTELQAVDGRRAAASMEAARAQKLIDGATSAVYSKFPYTTSTPGNQYASDARGKRDVGHYLRKANHGLSGQAANEANTYIDYAINALS | Function: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.
PTM: Two isomers exist.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 11500
Sequence Length: 108
Subcellular Location: Cellular thylakoid membrane
|
P84340 | MKTPLTEAVSIADSQGRFLSSTQIQVLFGRFRQAKAGLXAAKAL | Function: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.
PTM: Contains one covalently linked bilin chromophore.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 4720
Sequence Length:... |
P31020 | MTTQRNDNLEQPGRSVIFDDGLSATDTPNETNVVETEVLIVGSGPAGSSAAMFLSTQGISNIMITKYRWTANTPRAHITNQRTMEILRDAGIEDQVLAEAVPHELMGDTVYCESMAGEEIGRRPTWGTRPDRRADYELASPAMPCDIPQTLLEPIMLKNATMRGTQTQFSTEYLSHTQDDKGVSVQVLNRLTGQEYTIRAKYLIGADGARSKVAADIGGSMNITFKADLSHWRPSALDPVLGLPPRIEYRWPRRWFDRMVRPWNEWLVVWGFDINQEPPKLNDDEAIQIVRNLVGIEDLDVEILGYSLWGNNDQYATHLQ... | Catalytic Activity: H(+) + NADPH + O2 + phenol = catechol + H2O + NADP(+)
Sequence Mass (Da): 67419
Sequence Length: 607
Pathway: Aromatic compound metabolism; phenol degradation.
EC: 1.14.13.7
|
Q7SIF9 | MLDAFSRVISNADAKAAYVGGSDLQALRTFISDGNKRLDAVNYIVSNSSCIVSDAISGMICENPGLITPGGNCYTNRRMAACLRDGEIILRYISYALLAGDSSVLEDRCLNGLKETYIALGVPTNSTVRAVSIMKAAVGAFISNTASQRKGEVIEGDCSALAAEIASYCDRISAAVS | Function: Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.
PTM: Contains two covalently linked phycoerythrobilin chromophores and one covalently linked phycourobilin chromophore.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18604
Sequence Length: ... |
P00438 | MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphat... |
Q9M3B8 | MVLSNKKLKQRIRQDLAESLSVSVSETNPQSQSLKLLLDSSSHKPRLSKREKRRNCETFAREDDEIRENEVGNGGSSEKTDTKIKKKRKRDDAVEVDELEGDEGTKEEQKPQKKKNKKKKKKRKVNKTPKKAEEGNVEEKVKVEEIEVNTDNKEEDGVVPNKLYVGGIPYQSTEDEIRSYFRSCGVIIKVDCKMRPEDGAFSGIAFITFDTEDGAKRALAFDRAAMGDRYLTIQQYVKTTTPSIPRRKTSSGFAPEMVDGYNRVYIGNLAWDTTERDIRKLFSDCVINSVRLGKNKETGEFKGYAHVDFKDSVSVAIALK... | Function: RNA-binding protein which mediates polarized mRNA (e.g. Ran2 transcripts mRNA) transport from the nucleus to the vicinity of the cell plate during cytokinesis and phragmoplast formation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65997
Sequence Length: 597
Subcellular Location: Nucleus... |
Q4K423 | MEARNMTPFTYFSLPMQKLFLRNQAAVRNKPYAKYFRSEMRVPLSAVRKIQQGPMALEDTLTPSIEDINRLLEPDFVSEESGYALLPGPMAYVQSRKFFPGCTAQMFKWWFIWHPAESERYTLWFPYAHVSNPCVHHQRLRDESLSFEERLYGNTFCASEYVGDRLMHLHIDFQQPASLGLNTDLYREAKIDGSVSALMSLADHPEVPVSLMVHLFKEVPDGMYLTSRYWVGAHPSMARFPGAEKAASLLKENGFGEAELETLAYEFAVHDMCEFNHLASFLPDLYREFGTPAA | Function: Hydrolase that specifically degrades the potent antimicrobial compound 2,4-diacetylphloroglucinol (DAPG) to equimolar amounts of mildly toxic monoacetylphloroglucinol (MAPG) and acetate.
Catalytic Activity: 2,4-diacetylphloroglucinol + H2O = 2-acetylphloroglucinol + acetate
Sequence Mass (Da): 33773
Sequence ... |
Q9RGS8 | MTNQNRRDFLRLAAGTAGAAALQLFPPVIREALAIPANRRTGTIRDVEHIVILMQENRSFDHYFGKLRGVRGFGDPRPLALQNGKSVFHQPVLLGPAELLPFHPDASNLGMQFLQDLPHGWQDMHGAWNKGRYDRWIANKGTTTMAYLERDDIPFHYQLADAFTICDAYHCSIPSSTDPNRYYMWTGYVGNDGAGGGPVLGNEEAGYGWSTYPETLEQAGVSWKIYQDIGTGLDAAGSWGWTQNPYIGNYGDNSLLYFNQYRNAQPGSPLYDKARTGTNVSAGGTLFDVLQQDVKNGTLPQVSWICAPEAYSEHPNWPAN... | Function: Hydrolyzes phosphatidylserine as well as phosphatidylcholine.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine
S... |
P15713 | MISKSRRSFIRLAAGTVGATVATSMLPSSIQAALAIPAHRRHGNLKDVEHVVILMQENRSFDHYFGTLKGVRGFGDRMAIPLPDGQRVWHQKGSKGEILPYHFDTSTTSAQRVDGTPHTWPDAQQAWNEGRMDKWLPAKTERSLGYYKEQDIAFQFAMANAFTICDAYHCSFQGGTNPNRLFLWTGTNDPLGQHGGPVTTNDHDSNGPVEQGYTWTTYPERLQAAGITWRVYQDMADNFSDNPLIGFRQYRAAAPDSPLIVNGLSTWKLDALKRDVLANSLPQVSWIVAPAKYSEHPGPSSPIWGAEYTSWVLDALTANP... | Function: Hydrolyzes phosphatidylserine as well as phosphatidylcholine.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine
S... |
Q9VJ07 | MLKATRKQADPYKSKLKVSASHSGPHPLPVEVTAAEEEQAATFGQTSPQKLSLKGSQLGGSILIGNYNYLTQLEVCENEMEVLDLSSLAQLETLKCSRNKLMELIINGTNLQTLVADHNYLHNISTTNTHPVPLKLQRIDISHNNFSELPNWVGACASLTAINASHNRLNNVAVLLRNYRITELVSLDLAYNDLKQLDQFPEGFSSIRSLQLQSNELPSLPDNFFAVTHARLETLNVSCNKLSTLPRYEQNNHAALVNLSLAGNHLNDSIFEPLHNAAKLRVLHLAYNRIGVLPAACVRNWPELEILVLSGNMLQQLPEE... | Function: Protein phosphatase that specifically mediates dephosphorylation of 'Ser-586' of Akt1, a protein that regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-58... |
A0QQ68 | MTTEITRPPAPPSRPSESRKPSLPGLLHLVAIAAVLATIVSAWAIDFVPTALIDGSDNIVALLQRMIPPRLDDPARIGMLAVETLLMAVLGTTLAAIASVPLAFLAARNTTPHPAVQAVARAVITFCRAMPDLLFAVLFVRALGIGVLPGVLALALHSIGMLGKVFADAIEQTDAGPREAVRSTGVGYFRELLNAVVPQVVPSWIAMFVYRIDINLRMSVVLGFVGAGGIGFALQDALRGLIYPRALGIVCVILVIIAGMELLAIAIRRILLDPSRSNPLRDRIARFGLSGVLVGSCVAAFVLLKINPLALFTWVFPSVG... | Function: Part of the ABC transporter complex PhnCDE involved in phosphate import. Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55928
Sequence Length: 532
Subcellular Location: Cell membrane
|
A0A142C7A4 | MSAPTQTTPVFKALTEASFSDSSLSEEAKQNALYWWNTSANDLARMLHQADYSEEVQRGFLSYYRDNICPRLGGKPDKDSADSGVGWDGNPLEYSFELKGSTKKKSVRFVVDLTELRPADHSNPLSMKHTQEMVDLLAEKTPNFDDTWYKVLKNWFVYAHLTPEEQTALIAKAGQQTSVIIGFDIYPKLTSPDQLPVMGKVYFPPCYVASDKGISRWQAVRQGIQSLPGVESFPNILSSTEIINDYLSEKPDSWQMGTRYLATDLVSPNKARFKVYMRCFDTSFEGIWDYYTLGGRIPNLDEDREKFRQLMDLVSGTTYA... | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of phenalenones such as herqueinone, compounds that have been reported to treat tumors, bacterial infections and/or mycoses, and rheumatic diseases . The non-reducing polyketide synthase phnA synthesizes the heptaketide backbone and cy... |
P16685 | MHADTATRQHWMSVLAHSQPAELAARLNALNITADYEVIRAAETGLVQIQARMGGTGERFFAGDATLTRAAVRLTDGTLGYSWVQGRDKQHAERCALIDALMQQSRHFQNLSETLIAPLDADRMARIAARQAEVNASRVDFFTMVRGDNA | Function: Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Catalytic Activity: ATP + methylphosphonate = adenine + alpha-D-ribose 1-methylphosphonate 5-triphosphate
Sequence Mass (Da): 16540
Sequence Length: 150
EC: 2.7.8.37
|
A0A142C7A5 | MAAETATSKQNLVILGGSYAGLSTAHYLLRHVVPQLPGKESYQVILISASSEAMCRPACPRALISDDMFQQDKLFVSIPAQFEQYLKDTFKFIHGTVTSLDHQDRCVTVSVKDGDPEKIKCHAIVIATGASTASPLLGLNRDSETLRTNWNEFRAALPTAKHIVIAGGGPAGVETAGELGEYLNGRAGWFHSKLENPKVEITLVTADSKILPILRPALATKAEKLLNKVGVTVIKKSRVTNVTPPGAGAEDALTANATVTLEDGKELQADLYIPATGMTYNSSFVDASLLTDYGRVETDPGTLRVVNGGALLYAIGDVGS... | Cofactor: Binds 6-hydroxy-FAD non-covalently.
Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of phenalenones such as herqueinone, compounds that have been reported to treat tumors, bacterial infections and/or mycoses, and rheumatic diseases . The non-reducing polyketide synthase phnA ... |
Q52984 | MMDAAKTSDDAGVAQRREGMRLLARATLGELSLAWDAIDDKPEVAPVRGPETGLVMVRGKIGGGGDPFNLGEATVSRATVRLSTGEVGHGQLLGTDKARARLAAIFDALFQSAAHRASVEALHEQVAARLDAEDRRKAEETAATRVDFFTMVRGED | Function: Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Catalytic Activity: ATP + methylphosphonate = adenine + alpha-D-ribose 1-methylphosphonate 5-triphosphate
Sequence Mass (Da): 16616
Sequence Length: 156
EC: 2.7.8.37
|
P86807 | GSTLLEQMSLHGVRHAPGSLEANDFFLANDQRHGALGSFVRADEHDLSTLGDHPLRSHGGLSEQQLPLLLSR | Cofactor: Unlike bacterial phosphonoacetate hydrolase, does not require zinc as a cofactor.
Catalytic Activity: H2O + phosphonoacetate = acetate + H(+) + phosphate
Sequence Mass (Da): 7812
Sequence Length: 72
EC: 3.11.1.2
|
Q51782 | MTQLISVNSRSYRLSSAPTIVICVDGCEQEYINQAIQAGQAPFLAELTGFGTVLTGDCVVPSFTNPNNLSIVTGAPPSVHGICGNFFFDQETQEEVLMNDAKYLRAPTILAEMAKAGQLVAVVTAKDKLRNLLGHQLKGICFSAEKADQVNLEEHGVENILARVGMPVPSVYSADLSEFVFAAGLSLLTNERPDFMYLSTTDYVQHKHAPGTPEANAFYAMMDSYFKRYHEQGAIVAITADHGMNAKTDAIGRPNILFLQDLLDAQYGAQRTRVLLPITDPYVVHHGALGSYATVYLRDAVPQRDAIDFLAGIAGVEAVL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Specifically hydrolyzes phosphonoacetate. Does not have activity on other organophosphonates or acetates.
Catalytic Activity: H2O + phosphonoacetate = acetate + H(+) + phosphate
Sequence Mass (Da): 44239
Sequence Length: 407
EC: 3.11.1.2
|
P16686 | MTLETAFMLPVQDAQHSFRRLLKAMSEPGVIVALHQLKRGWQPLNIATTSVLLTLADNDTPVWLSTPLNNDIVNQSLRFHTNAPLVSQPEQATFAVTDEAISSEQLNALSTGTAVAPEAGATLILQVASLSGGRMLRLTGAGIAEERMIAPQLPECILHELTERPHPFPLGIDLILTCGERLLAIPRTTHVEVC | Function: Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Catalytic Activity: ATP + methylphosphonate = adenine + alpha-D-ribose 1-methylphosphonate 5-triphosphate
Sequence Mass (Da): 21027
Sequence Length: 194
EC: 2.7.8.37
|
A0A1S6PUA4 | MKFTYLVSLAAFAVTALGSRPTPPNLEFLFSANLTKGPAYIYDQSDAQIKALQTLTGGIIAGPNFDGTVIGGTALSTRGADGTIRADAHYLIQTSDGANILVTESAAIPYVAVLFDTSSEKYNWLNNVTAWGTPPNLNEINFLEYWQIE | Function: Hydroalkoxylation enzyme; part of the gene cluster that mediates the biosynthesis of phenalenones such as herqueinone, compounds that have been reported to treat tumors, bacterial infections and/or mycoses, and rheumatic diseases . The non-reducing polyketide synthase phnA synthesizes the heptaketide backbone... |
Q52985 | MTAQSQIYSGAFADPVFEAQSVFRSLMDCFARPGIIGRLSTAAAPPAPLGEASGAVALTLCDHDTPVWLSPALSKSSAPKWIAFHTGAGVTDTKDEPRFAFFEKGAAVPGFDQFALGTQEYPDRSTTLVVEVEALEGGQPLIGRGPGIKNGIVIAPKGLPDVFLDLWAANRAIFPRGIDLVLTAREAVLCLPRTTKLERE | Function: Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Catalytic Activity: ATP + methylphosphonate = adenine + alpha-D-ribose 1-methylphosphonate 5-triphosphate
Sequence Mass (Da): 21253
Sequence Length: 200
EC: 2.7.8.37
|
P16687 | MYVAVKGGEKAIDAAHALQESRRRGDTDLPELSVAQIEQQLNLAVDRVMTEGGIADRELAALALKQASGDNVEAIFLLRAYRTTLAKLAVSEPLDTTGMRLERRISAVYKDIPGGQLLGPTYDYTHRLLDFTLLANGEAPTLTTADSEQQPSPHVFSLLARQGLAKFEEDSGAQPDDITRTPPVYPCSRSSRLQQLMRGDEGYLLALAYSTQRGYGRNHPFAGEIRSGYIDVSIVPEELGFAVNVGELLMTECEMVNGFIDPPGEPPHFTRGYGLVFGMSERKAMAMALVDRALQAPEYGEHATGPAQDEEFVLAHADNV... | Function: Together with PhnG, PhnH and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. PhnI alone has nucleosidase activity, catalyzing the hydrolysis of ATP or GTP forming alpha-D-ribose 5-triphosphate and adenine or guanine, respectively.
Catalytic Activity: ATP + m... |
P16688 | MANLSGYNFAYLDEQTKRMIRRAILKAVAIPGYQVPFGGREMPMPYGWGTGGIQLTASVIGESDVLKVIDQGADDTTNAVSIRNFFKRVTGVNTTERTDDATVIQTRHRIPETPLTEDQIIIFQVPIPEPLRFIEPRETETRTMHALEEYGVMQVKLYEDIARFGHIATTYAYPVKVNGRYVMDPSPIPKFDNPKMDMMPALQLFGAGREKRIYAVPPFTRVESLDFDDHPFTVQQWDEPCAICGSTHSYLDEVVLDDAGNRMFVCSDTDYCRQQSEAKNQ | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the breakage of the C-P bond in alpha-D-ribose 1-methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose 1,2-cyclic phosphate 5-phosphate (PRcP).
Catalytic Activity: AH2 + alpha-D-ribose 1-methylphosphonate 5-phosphate + S-adenosyl-L-methionine = 5... |
Q52987 | MNDLATYNFAYLDEQTKRMIRRAILKAIAIPGYQVPFASREMPMPYGWGTGGVQVTASILGPDDVLKVIDQGADDTTNAVSIRAFFQKVADVAVTTRTTEATIIQTRHRIPEEQLREGQTLVYQVPIPEPLRFLEPRETETRKMHALEEYGLMHVKLYEDIARNGHIATTYAYPVKVEGRYVMDPSPTPKFDNPKMHMSEALQLFGAGREKRIYAVPPYTEVVSLDFEDHPFEVQKFDKPCALCGAENVYLDEVVLDDKGGRMFVCSDTDHCEDRRAHGHAGAMLAPAAKESQEAAE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the breakage of the C-P bond in alpha-D-ribose 1-methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose 1,2-cyclic phosphate 5-phosphate (PRcP).
Catalytic Activity: AH2 + alpha-D-ribose 1-methylphosphonate 5-phosphate + S-adenosyl-L-methionine = 5... |
O31156 | MKIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEEARKPMGLLKIDHVRALTEMPRIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASPINGVKEVIASLRERGIKIGSTTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGMWTVGVILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAHFTIETMQELESVMEHIEKQELIIS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 30060
Sequence Length: 264
EC: 3.11.1.1
|
Q5L9P9 | MKKIECIIMDWAGTAVDYGCFAPVAAFIKAFAGKGLTIDVEQTRKPMGLPKIQHIRELLTMPEVNEQFINRYRRAWTEEDVVELNHLFEKYLFASLKEYTDPIPGVIPTLEKLRAEGLKIGSTTGYTREMMDVVLPEAQAKGYRVDYCATPNLLPAGRPAPYMIFENLTKLAVPDPDTVVKVGDTIADIQEGVHAKVWSVGVVLGSNEMALTEEETHALPAAELENRIAEVKQRMLAAGASYVIRSIEELPALIQLINSKLNH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 29268
Sequence Length: 263
EC: 3.11.1.1
|
B8DKP2 | MKPFLRTRVYDGPVRAVVLDWAGTAVDHGCLGPAAVFVQAFALHGVEVAVSEAREPMGSEKREHVRRMLAMDSVAARWRAVHGHVPHEADVDAVYRDVEPLMLQTIAAHAVPVPGLAEFVDRVRGRGMGLGSCTGYTGPMMEVLVPEAARRGYSPDVVVHASEVPAGRPYPWMCYLNAMRLGVHPMESMVKIGDTVADMHEARNAGMWTVGVVRTGNDVGLSEVDAARMPPDQLAARMTVAAARLREAGAHYVVDSIADCFSVIKAIEARLARGDTPYPA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 30244
Sequence Length: 280
EC: 3.11.1.1
|
Q2SHM4 | MSYAYQRFYRGPIEAVIFDWAGTTYDFGSMAPIRAFQNLFAEQEIPITLAEAREPMGTEKREHITRILNMPRVREAWREKYGALASEADIERLYHAFVPMQIEAIRECARPVPGLMETVAWLERRNIKIGANTGYNRDMLDVLTDIAAAQGYRPASNVCATDVPKGRPYPHMSLKNALELGVGDVRACIKVDDTLPGIEEGLAAGMWTVGVTTSGNEVGLSQEDWTALDSASKTVLREQAQERFRRGGAHVIIGSVADLPAAVEYIERWLAQGHGPDTTGLAGVTLTAAGVSLR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 32353
Sequence Length: 294
EC: 3.11.1.1
|
Q88YN8 | MTIKAVIFDWAGTTIDYGSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAIQNDWQARFQVLPTEDDCNQIFSNFKAILLSSLTEFGQLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITSEQTGGVGRPAPAMLALAAEQLTVTDPTTVMKIGDSVNDILEGNNADAVSVGIIDGSNIMGLSELAFNALSPAEQAERRAHVTAAYQRAGADYILQSMAELPALLDQINQPVATDH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 28527
Sequence Length: 265
EC: 3.11.1.1
|
P23836 | MRVLVVEDNALLRHHLKVQIQDAGHQVDDAEDAKEADYYLNEHIPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNSGLASQVISLPPFQVDLSRRELSINDEVIKLTAFEYTIMETLIRNNGKVVSKDSLMLQLYPDAELRESHTIDVLMGRLRKKIQAQYPQEVITTVRGQGYLFELR | Function: Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ phosphorylates PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In hi... |
P23837 | MKKLLRLFFPLSLRVRFLLATAAVVLVLSLAYGMVALIGYSVSFDKTTFRLLRGESNLFYTLAKWENNKLHVELPENIDKQSPTMTLIYDENGQLLWAQRDVPWLMKMIQPDWLKSNGFHEIEADVNDTSLLLSGDHSIQQQLQEVREDDDDAEMTHSVAVNVYPATSRMPKLTIVVVDTIPVELKSSYMVWSWFIYVLSANLLLVIPLLWVAAWWSLRPIEALAKEVRELEEHNRELLNPATTRELTSLVRNLNRLLKSERERYDKYRTTLTDLTHSLKTPLAVLQSTLRSLRSEKMSVSDAEPVMLEQISRISQQIGY... | Function: Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to P... |
Q9I4F8 | MIRSLRIRLMLGAAALAVLFMLALLPALQRAFGIALENTIEQRLAADVATLVSAARVEKGRLVMPEHLPVEEFNLPEAKVLGYIYDQNGDLLWRSTSAADESINYTPRYDGRGNEFHTTRDAKGEEFFVFDVEIDLLRGKQAAYSIVTMQSVSEFESLLKGFREQLYLWLGGALLVLLGLLWLGLTWGFRAMRGLSSELDQIESGERESLSEEHPRELLRLTHSLNRLLRSEHKQRERYRHSLGDLAHSLKTPLAVLQGVGDQLAEEPGNREQVRVLQGQIERMSQQIGYQLQRASLRKSGLVRHREQLAPLVETLCDAL... | Function: Member of the two-component regulatory system PhoP/PhoQ that plays a role in the regulation of resistance towards polymyxin B and cationic antimicrobial peptides in response to limiting concentrations of Mg(2+) . May function as a membrane-associated protein kinase that phosphorylates PhoP in response to envi... |
L0E2Z4 | MTPAPTPRTDQLHGSRVLVIGGTSGIGFAVCAAALGHGAIVTIVGSNAQKLKDSVARLKSSFPSTDPDDIVAVRCDLSNSDTVEQDIEKALQLAAGNSKINHIVITAADMTAPPPLEDLTVDSVQRPGIIRLVAPLMVAKHLPKYMNKCPQSSLTLTSGAHCLRPDPGWTVISGYCGAVEAMSRGLAIDLKPLRVNVVAPGAVLTEAVKDILGDAYDAAVEMAEAKSTVGQTGSPESVAQAYIYLMKDHYASGSVVSTNGGMLLV | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide is the produc... |
L0E4G6 | MHNTQSDTKCENASDTPESPTGEEESVGLARWKLGLLMFGNTLAVFCVALDNTIMSNAIPRVTQTFDSLEDIGWGSPARRHFDRQRERTTSPKTAVYGCFGGIGGAFAENSTWRWCFYINLPLGAVTTVLILCFFFDSRTGTSDVSMSSWNRFRGLDIPGLLLFLPTVFCLLLALQWGGAKYPWNNVRVIVLFVIFILAGGCWIFIQHSMKDQASVPPRLIRNRNVWSSAVYMGCIVGSFIIILYYFPIWFQAVKGGSPIQSGTMILPIIIGLIVWLGFGFQLPFIAVQTALPRSDIPVATAIVTFAQNLSEAVLVALAQ... | Function: Efflux pump; part of the gene cluster that mediates the biosynthesis of paraherquamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45211
Seque... |
L0E2U6 | MTIQVKRVVTVFGGTGNQGSSVARSLLAHKAKIFHVRVITRDPQSDKAKAIASLGAELVQADGFNLGEMTNAFAGSWGVFINTNSDDEALKSLDGPSDYDLGVSVIDSAKKAGVQHVVYSSGPSITNATKGRMHLEGFETKYHVEQYGRRKGFTSFTPILCASFMECFFYDPFVDAFGGFPWIPEPETGEVVFRTPDYGGKGDMPWVSCEEDLGDIVHGIFLNPCKYDQVLVQATSQQITMFDVAASYTQATGIPARYEELPSWSSIKLNGTRCRAETRQMFWYMKHCGGRWFAEHESDMSTAVALKESAMLSQDRVGGL... | Function: NmrA-like family domain-containing oxidoreductase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide... |
L0E2Q5 | MAFQLAGFFLILALGLGHYFSNDQESRCRQLELYATKSIIPTTPAMSSFNTIATPHGALTIPVNWLYPEVPKVTSAHTNCLFIAAALQVDTWEHSRPLKQSCHAQDLPEHGQCHQGRVAHYSAYVNSVSAVQQVIQFAASHRLRLAIRNTGHDLAGRSSAPNSLQLHTAGLKGIDYVESFTPQAPAGQSVPSDGPAVTVGAGVLTGELYSAAAEAGYTVVGGSCSTVGIAGGWMQGGGYGILTPSRGLGVDNVLEIGVVTAQGVYVTANQYQNQDLFWAIRGGGGGTFGAVVHVTFRTYPDSPATVSKLNVVSPHGLNSA... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide is the production of th... |
L0E168 | MTIEATEGHVSKGMLAKGDSTSPIPTIFDVLSRDHVFVDSHQKVWWERTGQLLDKILASAGYNPARRLEALTFYIQVLIPFLGPHPHQFRSAITRSGLPLEFSVNYQQRGDIDPVVRIGFEPVAAASGTEIDPYNQIPVVDLLNQLEVLNIPAFDPSLFRYFLDAHTVNGHEKGLLKEKKIEGSELTSQSAFGFDLKEKAISVKGYTFPAIKCTLNEKGFGNFISESIQPLAAQMGPIPSFDMVHSYLEGTNGYSQFAFWSFDCVDPAQSRLKLYSSHNSVVWSKVEEIWTLGGRAKSPVVQEGLVYLKELWELTKLSEG... | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide is the production of the beta-m... |
L0E301 | MTVSTESNFPHGASTQKPQSAEPEIYSSLTKSLDFSNDAEEKWWTRTAPLLSRILDSAGYTLPQQCQFLTLFNTLMIPNFGPHPHIWHSSITHSGLPVEFSVNYQPGKQPTVRIGFEPASSISGTARDPYNMVTVLNVLNKMSRLNFKGFDPSLFHTLISSLALSKNESDLLQGAKLEGSKFKTQAAFGLDLKGDAVTVKTYLYPALKCKVSGLAFSELLEAALAKHQNAHDFSRVLPLVQSYMEEGQCYNQYSFVGFDCVDSSKSRLKIYGALLDISWKKVEEVWTLGARLVNSETNKEGLRYMRALWEYLTPGKERRP... | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide is the production of the beta-m... |
L0E4H0 | MGSLGEEVQVIIVGLGIVGLAAAIECREKGHSVHAFEKSNILKSIGDCIGLQSNATRIIKRWGDGAVHEALRPWIVSSKEIRIHNSSGRLIIRQDLSEVCEQPNYLLPRSELIRVMYEHALKIGVEISLGVEVCEPSEDEEGASVVALTRDGERQIVRGDFIICSDGVHSKMRKAIMPQPVEPRPSGYAAFRALVDTETLKGDPEASWVFEGVEENDRFDVFFLSGAQIALQSCNKGKVFSWFCIHQDTRNLLDVWTSPADPNEMLDLIKVWPIGQRLWSVIRHTQPQKFINYPLLNHKPLDHWVSSHGRLILIGDAAHP... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . Within the pathway, phqK catalyzes spirocycle formation through two paralle... |
L0E2V1 | MEPHHDGHILKVLPMLASNENFSRLTTAFVAGIAAHIIIFRRGEWDIAAARIPVGLFILQSCLFSYYLFVPGPPTSIYTALWLVGQITLGFIAGTTVSILSYRAFFHRLNSFPGPFPARLSMWYVTSLYAQNPDAFNTVRGLHQQYGDFVRTGPTELSVNHPDALQAVHSGRSECTKGPWYSMLHPFISLFAIRDKAEHSRRRKPWELAFRPNAVLEYLPALEKGTNELLEQVERRKGKSMDMTYWINLFTFDLTGRVAFSQEYECVKHNKRHPIMEINDSSNLVTGVVSHVVWLISFIKATPGLNANMKALIGFSEEQV... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide is the production o... |
L0E2R0 | MKQGTTGMYCEVGPCTNAKDAHSPCLRPPGYAKPPTVRVCRTRGHNLPLSKVPGPKLAALTKWYGFYHNVIRDGQYSLSFSSLHKKYDSPVIRIGPNAVHVDDPSFYQEMFSMTTKYYKEPEFYKALGAEGAMASILDPKHHRMYRNHLRPLFASRAVDGVVPRLKLELEKATRIFDMHRKDYHPLNIQALYRSFTSDMVCELLFGESPDFIGDGNGYHPFVAALDRFTAFSWLVVYFPWVKSIQFHLPFGLGDKLAPEFNDFKRQCETWEAKAQLKRESGVQVGQKNLFDYYAELGAGPETAVSGVAQPVEDAFNFLTA... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide is the production o... |
L0E172 | MTMSQMNQDAEGYFRVWKPEEASPGHQESPEELDSGRMCGHLCRLSPNEPMAQSLVRHEHYLAHRVNIQEGQRIIDLGCGIGNPARSIARFTGANITGLNINAQQLRQARQLTQEAGLSYQVNFVEQNFLKIEFADDTFDGAYAIESTCYAPDLVEVYSEIFRVLKPGARFGVYEAVLTDKYDDNNPMHREVKTNIERGGGLARIHTSAEAIAAMKAVGFEVLAIDDLGARPDQIPWETQLSDPFLEKQGLLSFALLSVFFAARAMPLINRGLQAVVGKLEQMTVFPAGSQKVVDLVVTILDGMYRGGELGIFSPMFLIV... | Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide is the production of the beta-m... |
L0E307 | MSKYLLMSFTEGSMSTWHYLAMLTTIWLVYQYLKPVPIVPGLPVINRAERWDFFSIKMKRRFLNNAAALMKEGFEQPKLVLSPDYADELKNDARFSLEDAGLRRHYRMKPASLFKIIGQTTPISGRAFLGPEVCGDIRWIEATMGYLEMGVRTAFLLQVFPRFLFPLQRWFPLCRKVRKHIDMAGTILRPVIDSRRADGRPAQDAISWFDEAAAGETYNPVYSQLSLSFASTHTTADTMTKVIIHLAENPAVVTDLRKEVVEAIAKHGELTKTALSQMNLLDSTLKESQRLEPLASATMNRVTREEVTLSNGLWIPRNMY... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide is the production o... |
Q94CL7 | MEARPVHRSGSRDLTRTSSIPSTQKPSPVEDSFMRSDNNSQLMSRPLGQTYHLLSSSNGGAVGHICSSSSSGFATNLHYSTMVSHEKQQHYTGSSSNNAVQTPSNNDSAWCHDSLPGGFLDFHETNPAIQNNCQIEDGGIAAAFDDIQKRSDWHEWADHLITDDDPLMSTNWNDLLLETNSNSDSKDQKTLQIPQPQIVQQQPSPSVELRPVSTTSSNSNNGTGKARMRWTPELHEAFVEAVNSLGGSERATPKGVLKIMKVEGLTIYHVKSHLQKYRTARYRPEPSETGSPERKLTPLEHITSLDLKGGIGITEALRLQ... | Function: Transcription factor involved in phosphate starvation signaling . Binds as a dimer to P1BS, an imperfect palindromic sequence 5'-GNATATNC-3', to promote the expression of inorganic phosphate (Pi) starvation-responsive genes . SPX1 is a competitive inhibitor of this DNA-binding . PHR1 binding to its targets is... |
P43076 | MYSLIKSLATFATLFSLTLAKFESSTPPVEVVGNKFYFSNNGSQFLIRGIAYQQDAAGSVSSGYDADPNRKYNDPLADADACKRDVKYFKESNTNTLRVYAIDPDKDHEECMKIFSDAGIYIVADLSEPTVSINRNNPEWNLDLYKRYTKVIDKMQEYSNVLGFFAGNEVTNNRSNTDASAFVKAAIRDMKKYIKESDYRQIPVGYSSNDDEEIRVAIADYFSCGSLDDRADFFGINMYEWCGKSTFETSGYKDRTEEIKNLTIPAFFSEYGCNANRPRLFQEIGTLYSDKMTDVWSGGIVYMYFEEANKYGLVSVDGNS... | Function: Required for apical cell growth and plays an essential role in morphogenesis. May be integral to the pathogenic ability of the organism.
Location Topology: Lipid-anchor
Sequence Mass (Da): 59457
Sequence Length: 548
Subcellular Location: Cell membrane
|
Q3ZBD3 | MAGKAHRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDVNLASFIEQVAVSMT | Function: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity (By similarity). Also a... |
Q9LZ76 | MAATLPLSPINHQLCRFGNNSLTTHRFCSPGFLISSPCFIGLTGMGSATQLRARRSLISSAVATNSLLHDVGATVAVLGGAYALVLSFESLTKRNVIQQSLSRKLVHILSGLLFVLAWPIFSGSTEARYFAAFVPLVNGLRLVINGLSISPNSMLIKSVTREGRAEELLKGPLFYVLALLFSAVFFWRESPIGMISLAMMCGGDGIADIMGRKFGSTKIPYNPRKSWAGSISMFIFGFFISIALLYYYSSLGYLHMNWETTLQRVAMVSMVATVVESLPITDQLDDNISVPLATILAAYLSFGY | Function: Kinase involved in the activation and reutilization of phytol from chlorophyll degradation in plant metabolism, including tocopherol biosynthesis. Catalyzes the conversion of phytol to phytol monophosphate (PMP) in the presence of CTP or UTP. No activity with ATP or GTP as phosphoryl donor.
Catalytic Activity... |
Q7XR51 | MAAAARPVDVVRHFPCSSSVAASSSLLLSRSKSRLASPAAAAASSMRRRLVLGVGAAAAPAVAALAASATPAALRDCAATLLITAGAYSLVRAFDGLTARRLIEQNLSRKIVHVLSGVLFMSSWPLFSNSTEARFFAAIVPLLNCIRLLTYGLRLSTDEALVKSVTREGKPEELLRGPLYYVIVLLVSVLVFWRQSPIGIVSLSMMSGGDGFADIVGRRYGSAKLPFNENKSWIGSISMFISGFLLSALMLFYFSCLGYFTVCWDLALGKLALVALAATVVECIPVNDVVDDNISVPLATMLAAYLLFGYSSCC | Function: Involved in the activation and reutilization of phytol from chlorophyll degradation in plant metabolism, including tocopherol biosynthesis. Catalyzes the conversion of phytol to phytol monophosphate (PMP) (By similarity).
Catalytic Activity: CTP + phytol = CDP + H(+) + phytyl phosphate
Location Topology: Mult... |
Q2N2K1 | MTLLSSHLLVFSAVHHRAPPTTTTRNSPTTNHTVRFLCSPGVPPAVRLDQRLPRFVVPGAGAEDLLYNAGATVGVLGGGYALVRAFDELTRRNILQQGLSRKLVHILSGLLFLVSWPIFSNSPKARYFAAFVPLVNCLRLLVNGLSLASDEGLIKSVTREGDPLELLRGPLYYVLILILSALVFWRESPIGVISLAMMCAGDGIADIIGRRYGSMKIPYNEHKSLAGSMSMLVFGFLVSIGMLYYYSVLGHVQLDWASTLPRVAFISFVATLVESLPITKVVDDNISVPLATMAVAFFTFHH | Function: Involved in the activation and reutilization of phytol from chlorophyll degradation in plant metabolism, including tocopherol biosynthesis. Catalyzes the conversion of phytol to phytol monophosphate (PMP) (By similarity).
Catalytic Activity: CTP + phytol = CDP + H(+) + phytyl phosphate
Location Topology: Mult... |
Q5N9J9 | MVSLISAHLLSLPSSAPRSRPQSRPPLSPPAAAAAASCSFDLPRPRRLVADGSRRKGTMAAAIPPEASGLAHDLGSAAVTAGVALALLRFFEELAKRGVFEQKLNRKLVHITIGMVFLLFWPLFSSGSYAPFLAAVAPGINIIRMLLLGLGVMKNEAMVKSMSRSGDPRELLKGPLYYATTITFATSIFWRTSPIAIALICNLCAGDGIADIVGRRLGQEKLPYNPNKSYAGSIAMALAGFMASIGYMHYFQSFGFIEESWSLAFGFLVVSVTAALVESHPISTHLDDNLTVPLTSFLVGSLVF | Function: Involved in the activation and reutilization of phytol from chlorophyll degradation in plant metabolism, including tocopherol biosynthesis. Catalyzes the conversion of phytol to phytol monophosphate (PMP) (By similarity).
Catalytic Activity: CTP + phytol = CDP + H(+) + phytyl phosphate
Location Topology: Mult... |
Q2N2K0 | MMFLSFNMISGGNTLQRFDPVACVSSVPLLLAPTTRPTFHFPSPFLSKPKPTYLFTSFSSSSSSSSSFFSSTTPPRSTMLHHDPLVSDVYATAISGVVALSFLRLFQETAKRDLFDQKLNRKLVHISIGLIFMLCXPLFSTETWASFFAALIPGINIFRMLVIGLGILKDEATVKSMSRFGDYRELLKGPLYYAATITLAAIIYWRTSPISIAAICNLCAGDGMADIVGRRLGGEKIPYNKNKSFAGSIAMATAGFLTSIGYMWYFSSFGFIEGSWKLVLGFLLVSIVTAFVESLPISTELDDNLTVPLTSILVGSIIL | Function: Involved in the activation and reutilization of phytol from chlorophyll degradation in plant metabolism, including tocopherol biosynthesis. Catalyzes the conversion of phytol to phytol monophosphate (PMP) (By similarity).
Catalytic Activity: CTP + phytol = CDP + H(+) + phytyl phosphate
Location Topology: Mult... |
Q2N2K4 | MAAAAAWTGAASPNSLLLSRSPPHAAALAPSPGSSMRRRLLLGVGTPAVAALAAAAPPAVLQDGAVTVLITAGAYSLVRVFDELTERRLIEKSLSRKVVHVLSGVLFMSSWPLFSNSTEARYFAAVVPFLNSMRLLIYGLRLYTDEALVKSVTREGKPEELLRGPLYYVLVLLFSVLVFWRESPIGIVSLSMMSGGDGFADIVGRRYGSAKLPFNRKKSWAGSISMFISGFLLSAMMMLYFSSLGYIDVIWEEALGKLALVALAATVVECVPVTEVVDDNISVPLATMLVAFLLFSSNRTIVN | Function: Involved in the activation and reutilization of phytol from chlorophyll degradation in plant metabolism, including tocopherol biosynthesis. Catalyzes the conversion of phytol to phytol monophosphate (PMP) (By similarity).
Catalytic Activity: CTP + phytol = CDP + H(+) + phytyl phosphate
Location Topology: Mult... |
P74653 | MGIEQNNPMALPLWIAVGLAATYLGAVVLTAELLNRLSLSPAEVTRKIVHIGAGQVVLIAWWLSIPGWVGAIAGVFAAGIAVLSYRLPILPSLESVGRHSYGTLFYALSIGLLVGGFFSLGLPIFAAIGILVMAWGDGLAALVGQRWGRHRYQVFGFRKSWEGTLTMVLASFLVTVVFLSYTFGFTVIVLVVAGTVAIASAGLESFSRWGIDNLTVPLGSALIAWAGSYLWLG | Function: Catalyzes the CTP-dependent phosphorylation of phytol to phytylmonophosphate (PMP). Can also use UTP as an alternative phosphate donor, but not ATP or GTP. Is involved in tocopherol biosynthesis, via the utilization of phytol generated by chlorophyll degradation . Also plays a significant but not critical rol... |
Q56S59 | MASAKIFLIFLLAALIATPAAFAILVPTLVSTHISGLVFCSVNGNLDVINGLSPQVFPNASVQLRCGATNVISSTITNGSGAFSLAVNTFPLLNCNLVVATPLSTCNATLQSVGRLASSLRLVNITLGSGTGLIRVGLAPTGFILNLNIN | Function: Inhibits spore germination and leaf infection by fungal pathogens.
PTM: Probably covalently linked to cuticular lipids and/or trichome exudate diterpens or sugar esters in order to increase the solubility in exudate and the dispersion on the leaf surface.
Sequence Mass (Da): 15310
Sequence Length: 150
Subcell... |
O60331 | MELEVPDEAESAEAGAVPSEAAWAAESGAAAGLAQKKAAPTEVLSMTAQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGHLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEKEKSFPTYKDLDFMQDMPEGLLLDADTFSALVKTLQRDCLVLESFKIMDYSLL... | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesio... |
O70161 | MELEVPDEAESAEAGAVTAEAAWSAESGAAAGMTQKKAGLAEAPLVTGQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLL... | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesio... |
Q56YP2 | MSDSEEDEEEEEASEVILSSVVQKKKKKNLRFGEEVERRDGLVLLAQSTPMVRSRSQGTTRRVTPTPLVDVEKPLPNGDLYIGSFSGGFPHGSGKYLWKDGCMYEGDWKRGKASGKGKFSWPSGATYEGEFKSGRMEGFGTFTGADGDTYRGTWVADRKHGHGQKRYANGDFYEGTWRRNLQDGRGRYVWRNGNQYTGEWRSGVISGKGLLVWPNGNRYEGLWENGIPKGNGVFTWSDGSSCVGAWNESNIMRSFFNGVEKNDLIVGNRKRSSVDSGAGSLGGEKVFPRICIWESDGEAGDITCDIIDNVEASMIYRDRI... | Function: Catalyzes the synthesis of phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4-bisphosphate.
PTM: Phosphorylation inactivates the enzyme.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphospha... |
Q6EX42 | MPGLHVVSFLVVLLLQLRSSGMHLVASELFWGNTLPNGDIYVGSFDGLVPHGPGKYMWTDGALYDGEWDKSKMTGRGLIQWPSGASYEGDFRGGFIDGAGTFKGVDGSVYKGSWRMNKKHGMGTMVYSNSDTYEGFWNEGLPDEFGKYTWADGNVYIGRWKSGKMNGSGVMQWINGDTLDCNWLNGLAHGKGYCKYASGACYIGTWDRGLKDGHGTFYQPGSKIPCNLEVSDCLTSHDGTSASSSSNEKITIGLLFLLQKLCKNWRLRRFLHRPRRISNGTTPVFDDNSGSHLCQDVSSKSFSADDQCLQDSEVDKDSVY... | Function: Involved in flowering. May suppress floral initiation by modifying the expression of genes related to floral induction.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+)
Sequence Mass (D... |
Q8L796 | MMREPLVSEEEEEEATEVLLVEKTKLCKRRGDEEKTEERRDDLLLLALTPMVRSKSQGTTRRVTPTPPPVDVEKPLPNGDLYMGTFSGGFPNGSGKYLWKDGCMYEGEWKRGKASGKGKFSWPSGATYEGEFKSGRMEGSGTFVGVDGDTYRGSWVADRKQGHGQKRYANGDYYEGTWRRNLQDGRGRYVWMNGNQYTGEWRNGVICGKGVLAWPNGNRYEGQWENGVPKGSGVFTWADGSSWIGSWNESSNLMRNFFDGIEKNELIVATRKRSSVDSGAGSLTGEKIFPRICIWESDGEAGDITCDIVDNVEASVIYRD... | Function: Possesses phosphatidylinositol (PtdIns) phosphate kinase activity (Probable). Phosphorylates PtdIns(4)P and PtdIns(3)P in vitro . Doesn't phosphorylate PtdIns(5)P nor PtdIns(3,4)P2 in vitro . Does not exhibit phosphatidylinositol kinase activity in vitro .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho... |
O48709 | MQETVFLFTEENLNKEQSLGVKYKQSSRRVVPMTSCEVSDTAAEIRIVEKVLKNGDLYNGGLSAGVPHGTGKYLWSDGCMYEGEWTRGKASGKGRFSWPSGATYEGQFKDGRMDGEGTFIGIDGDTYRGHWLWGRKHGYGEKRYANGDGYQGNWKANLQDGNGRYVWSDGNEYVGEWKNGVISGKGKMTWANGNRYDGLWENGAPVGKGVLSWGEEKTSYNGWGRKSKKKDEEIVQNHKLSSVETLSANTNFPRICISELEDTGVCDHVEASPYTSESDTSGCGEQEWARSPLLLESGGAMSVQQSPRWLDEGDVKKPGH... | Function: With DRP1A and DRP2B, required for the precise coordination of polar ARAC3/ROP6 and ARAC4/ROP2 placement and subsequent root hair positioning during planar polarity formation in root hair-forming cells, probably by mediating the correct basal-to-planar polarity switching of D6PK into the polar, lipid-enriched... |
Q8L850 | MSGLDVRGAVSFAERTKSVDALTKKEILSALNSGEVSETSEDARFRVRELVLPDGESYSGSLLGNVPEGPGKYIWSDGCVYDGEWRRGMRHGIGNMRWASGASYDGEFSGGYMHGSGTYVDANKLTYKGRWRLNLKHGLGYQVYPNGDVFEGSWIQGLGEGPGKYTWANKNVYLGDMKGGKMSGKGTLTWVTGDSYEGSWLNGMMHGVGVYTWSDGGCYVGTWTRGLKDGKGSFYSAGTRVPVVQEFYLNALRKRGVLPDMRRQNQVASSVNMENLRVGVNRNKLSKGSLINLEQSRNGRVSLERRWSLEVSIEKVIGHG... | Function: Plays a role in sugar-mediated root development. Interaction with CINV1 induces repression of CINV1 activity and negative regulation of sugar-mediated root cell elongation.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-ino... |
Q5T9C9 | MAAPSPGPREVLAPSPEAGCRAVTSSRRGLLWRLRDKQSRLGLFEISPGHELHGMTCMMQAGLWAATQVSMDHPPTGPPSRDDFSEVLTQVHEGFELGTLAGPAFAWLRRSLGLAEEDYQAALGPGGPYLQFLSTSKSKASFFLSHDQRFFLKTQGRREVQALLAHLPRYVQHLQRHPHSLLARLLGVHSLRVDRGKKTYFIVMQSVFYPAGRISERYDIKGCEVSRWVDPAPEGSPLVLVLKDLNFQGKTINLGPQRSWFLRQMELDTTFLRELNVLDYSLLIAFQRLHEDERGPGSSLIFRTARSVQGAQSPEESRAQ... | Function: May act as a scaffold to localize and regulate type I PI(4)P 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment and conversion to PI(3,4,5)P3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol ... |
Q15735 | MEGQSSRGSRRPGTRAGLGSLPMPQGVAQTGAPSKVDSSFQLPAKKNAALGPSEPRLALAPVGPRAAMSASSEGPRLALASPRPILAPLCTPEGQKTATAHRSSSLAPTSVGQLVMSASAGPKPPPATTGSVLAPTSLGLVMPASAGPRSPPVTLGPNLAPTSRDQKQEPPASVGPKPTLAASGLSLALASEEQPPELPSTPSPVPSPVLSPTQEQALAPASTASGAASVGQTSARKRDAPAPRPLPASEGHLQPPAQTSGPTGSPPCIQTSPDPRLSPSFRARPEALHSSPEDPVLPRPPQTLPLDVGQGPSEPGTHSP... | Function: Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the functi... |
Q5W269 | MNQPLVVEISGDKALEHHHLGGKGYSLNNLIHAGLPVPSAFCVTAQAYQQFIEEVVPGAELTDGDLIAVRDAILHADIPDSLKQAIGDAYQHLGHDTTIAVRSSALDEDGQRQSFAGQYETYLHVKGSEAVLHKVQACWASLWAERAAQYRHESASHSAIAVILQVMVDADAAGVMFTQDPLSGSTDKVVIDSCWGLGEGVVSGQVTTDSFTLDKATGELCDQQIRHKPNYCQRDEHGLVTLLQTPEAKRDLPSLTPAQLQQLVTLARQAQLIYSTELDIEWAVKDDKVWLLQARPVTTSAKTANVIYANPWESDPAAKE... | Function: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transfer of 2-methyl-3-n-amyl-pyrrole (MAP) to 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) to yield prodigiosin.
Sequence Mass (Da... |
Q5W268 | MTTMIGQTRQAGSSSYEQAWQAEQAPCPGMEPDTLTVGVVVVTRNPTFFQTGLSVLNDIRDYVFNRVHIQSELPLKLSELASDPLYSEAREKAIHFLKNQSKALNIQVIQCASLAEATGKIIYTHALEQQPEFQMGMLFYDQTSLGNVDDSIEKIDRDLDAFYSAMQRGGIPAFYTTFSTVTFIRDVRSSFRYLPQQYREIVRSEDPAIFQTELLCLWMDFFEMNYTNRRVKPIGALALHNTLAEQLIQFFERTAASRWLVSYYTGSIISNLIGYLDRHAEAHGALVLRGPNEHAIACGAMANWQLYRMPFLGVVTSGMM... | Function: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the decarboxylation of pyruvate, followed by the modification of the resulting two-carbon fragment acetaldehyde at the C3 position of th... |
A0A0J9X1Q5 | MKFGFIAHPTSLGLKRYVKMLDLLQRNSTEQHSGYTRELWERQNLVPFMNFARITSATGATCEGVIKYMPLVADEMLADARGIAARVVQGIEELAGDGAELVGLGGFTSIVGRRGEATAEKSPVPVTSGNSLTTYAGYKALMQIQSWLEIRPEEEPVAIVGYPGSICLALSRLLLAHGFSLHLLHRAGNHDRSELLSHLPEEYHSRVTLTSDPEDLYPRCKLFAAATSAGGVIDPARLQPGSIFIDVALPRDIASETRPARDDILIIDGGCVTATDAVKLGGESLNVTIKQQLNGCMAETIVLALENRRENFSLGRYLAP... | Function: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transamination to the aldehyde group of 3-acetyloctanal, resulting in an aminoketone, which spontaneously cyclizes to yield the dihy... |
Q07326 | MKDNDIKRLLYTHLLCIFSIILSVFIPSLFLENFSILETHLTWLCICSGFVTAVNLVLYLVVKPNTSSKRSSLSHKVTGFLKCCIYFLMSCFSFHVIFVLYGAPLIELALETFLFAVILSTFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFVGAWLGALPIPLDWERPWQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN | Function: Involved in GPI-anchor biosynthesis . It acts through the transfer of ethanolamine phosphate to the third mannose of GPI.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24890
Sequence Length: 219
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellula... |
Q5W266 | MTLTKQDAVNQMMGFFQSKTLITALSLKLFDHLRDQDRNAKQMAALLNCPLRSSEQLLIALQAMGYLEKQDGLYHLPQEHRAFLVSDEPQWLGWLGRHIDTFLYPLWGELKAAVENDTHQRQTVFGDDRSWFDILYQNPDDVTDFQEFLGKFAAPFIDGFIQDYDFSQHQAFLDIGSGIGSLPIAVANAYSGVNLAICELPQTSTFLRDKLVQQGYGQRIQVLEGDVISGDLPIGDYDLIHLGWMLHDYAPETQLIILKNIYDAMPVGGRFIASETPLNADKSGPEFTALLSLNMLVSTDGGIESSPQEYLSRFHQAGFS... | Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to the hydroxyl group of 4-hydroxy-2,2'-bipyrrole-5-carb... |
Q5H8A4 | MRLGSGTFATCCVAIEVLGIAVFLRGFFPAPVRSSARAEHGAEPPAPEPSAGASSNWTTLPPPLFSKVVIVLIDALRDDFVFGSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKPGDIRHPKHVQQTDVAATLAI... | Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 108173
Sequence Length: 983
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinos... |
Q32L89 | MEDERSLSDICGGRLALHRRYYSPSCLEFCLSCPRISLRSITAVTCTVWLAAYGLFTLCENSMILSAAIFITLLGLLGYLHFVKIDHETLLIIDSLGIQMTSSYASGKESTTFIEMGKVKDVIINEAIYMQKVIYYLCILLKDPVEPHGISQVVPIFQSAKPRLDCLIEVYRSCQEILAHQKAASTSP | Function: Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Sequence Mass (Da): 21006
Sequence Length: 188
Pathway: Gly... |
Q14442 | MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCENSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVKDIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAHQKATSTSP | Function: Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Sequence Mass (Da): 21081
Sequence Length: 188
Pathway: Gly... |
Q5M9N4 | MEDEKSFSDICGGRLALRCRYYSPYCREFGLSSARLSLCSLTAVTCAVWLAAYGLFTLCENSMVLSATIFITILGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMDKVKDIIINEAIYMQKVIYYLCILLKEPGKPHEISRVVPVFQSAKPRLDCLIEVYRSCQEVLAHQKATATSL | Function: Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Sequence Mass (Da): 21078
Sequence Length: 188
Pathway: Gly... |
Q5W264 | MNDVTTETYETLKQSVLHTFAQLTGYNVSELSLTSHLENDLGVDSIALAEIAVSLSRQFQLNTPLLIQDINTIKDALDGILQREFQLSEKVEPAAIALSGDADLWLGNLVRQIFASHSGYDVNALALDAEIESDLGIDSVSVASAQGELFNTLQLNSETIIANCNTLSALKQCLAARLVQEKGQDWFEQRGRGQSDSAIDHDADTTAEVTPPTATPVAINAEIGDPRTMRDFVGIEHPDIFHKAREFHLFYQDKKKRQLYFYGMPLETPCKNRAVMFDEATGQHREFLMFGSNSYLGLSNHPEIIHAIQDAASLYGATNT... | Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Carrier of the L-malonyl group (malonyl-S-PigH), which is decarboxylated by PigJ to yield a C2 carbanion acetyl-S-PigH. Then the pyr... |
Q5W263 | MTISTPVIIDSLIRHAQRTPEQTALLCGDQHWNYRQLVTRAHVMASALRQAGLSGQAILLNLPKSLDAVAAIYATWLSGNHYIPIDYSQPSSRIERIIAAAAPALIIDTAWLATLDSQPSFDAEQPVGRMVYHNPIAAILYTSGSTGTPKGVQISHEMLGFFIQWAVRDTQLTARDVLSNHASFAFDLSTFDLFASAYVGAATWIIRESEQKDCAALAQGLQRHAVSVWYSVPSILAMLEKSTLLNPTLGQSLRQVIFAGEPYPVTALKRLLPCLPQPCRVSNWYGPTETNVCVAYAIDRARLAMLKQVPIGLPLEGLTA... | Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig) . Catalyzes the conversion of L-proline to L-prolyl-AMP and the transfer of the L-prolyl group to acyl carrier protein PigG .
Catalyt... |
Q5W262 | MSNDKHIAPLAVVSMGCVLPGVDHFRALDTIADWETVFQSASPLAWSETSRPIQGRQMDDSGFDFKKFSIPPLFRKAVSRETRLALRAAEDALAGLVLPESLRDCCDQFCAIHLGSDAAYRNATKVGALRALAEKLQAQGCPAAEVRRRLDDYKQPLAESLGCSSHDRVGEMASSIPARIAHFAHTRGKCQTLDGADKGGLRLLQLAQDCFRYHDSQMAVLTSVQCFHHRPQAYMLLEQGVSQDACWLEGAISLVVCPLAVAHEQGWPVLTQLGDIVTTHDGSPQPEADHPAALYFAGANQVFCQIVEMVLRQHQRCEGR... | Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the decarboxylation on the malonyl group attached to PigH to yield a C2 carbanion of acetyl-S-PigH. Then, the heterocyclic... |
Q54C64 | MKNHLNNNEDNSTLIKKKVLFVIAHPDDECMFFTPTIQHYNFIGSEIFVACLSNGNAVGLGKIREKELIDSCIDMGINQENVFFDQTNNFQDGMNIIWDTDLVEKTILSFIKQTSADIVISFDECGISSHPNHISISNGLKQLMKNKSSSTTTTSTTSSSSSSSSLSNRTTNNLNKEIKAYKLETVNIIRKYIGIADIPLTKLLSYDENSTQTFISTQLFPPSSYSPMTKHKSQFVWFRYLFVFLSRYSFINTLIEIK | Function: Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol (By similarity).
Catalytic Activity: a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol
Sequ... |
Q9UKJ1 | MGRPLLLPLLPLLLPPAFLQPSGSTGSGPSYLYGVTQPKHLSASMGGSVEIPFSFYYPWELATAPDVRISWRRGHFHRQSFYSTRPPSIHKDYVNRLFLNWTEGQKSGFLRISNLQKQDQSVYFCRVELDTRSSGRQQWQSIEGTKLSITQAVTTTTQRPSSMTTTWRLSSTTTTTGLRVTQGKRRSDSWHISLETAVGVAVAVTVLGIMILGLICLLRWRRRKGQQRTKATTPAREPFQNTEEPYENIRNEGQNTDPKLNPKDDGIVYASLALSSSTSPRAPPSHRPLKSPQNETLYSVLKA | Function: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that... |
Q2YFS3 | MALLISLPGGTPAMAQILLLLSSACLHAGNSERSNRKNGFGVNQPESCSGVQGGSIDIPFSFYFPWKLAKDPQMSIAWRWKDFHGEFIYNSSLPFIHEHFKGRLILNWTQGQTSGVLRILNLKESDQTRYFGRVFLQTTEGIQFWQSIPGTQLNVTNATCTPTTLPSTTAATSAHTQNDITEVKSANIGGLDLQTTVGLATAAAVFLVGVLGLIVFLWWKRRRQGQKTKAEIPAREPLETSEKHESVGHEGQCMDPKENPKDNNIVYASISLSSPTSPGTAPNLPVHGNPQEETVYSIVKAK | Function: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. Receptor for CD99 and PIANP.
PTM: Phosphorylated on tyrosine residues.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 33064
Sequence Length... |
Q9UKJ0 | MGRPLLLPLLLLLQPPAFLQPGGSTGSGPSYLYGVTQPKHLSASMGGSVEIPFSFYYPWELAIVPNVRISWRRGHFHGQSFYSTRPPSIHKDYVNRLFLNWTEGQESGFLRISNLRKEDQSVYFCRVELDTRRSGRQQLQSIKGTKLTITQAVTTTTTWRPSSTTTIAGLRVTESKGHSESWHLSLDTAIRVALAVAVLKTVILGLLCLLLLWWRRRKGSRAPSSDF | Function: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRB is thought to act as a cellular signaling activating receptor that associates with ITAM-bearing adapter molecules on the cell surface.
Location Topology: Single-... |
Q2YFS2 | MALLISLPGGTPAMAQVLLLLSSGCLHAGNSERYNRKNGFGVNQPERCSGVQGGSIDIPFSFYFPWKLAKDPQMSIAWKWKDFHGEVIYNSSLPFIHEHFKGRLILNWTQGQTSGVLRILNLKESDQAQYFSRVNLQSTEGMKLWQSIPGTQLNVTQALNTTMRSPFIVTSEFTTAGLEHTSDQRNPSLMNLGAMVTMLLAKVLVIVLVYGWMIFLRWKQRPAH | Function: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRB is thought to act as a cellular signaling activating receptor that associates with ITAM-bearing adapter molecules on the cell surface. Seems to associate with DA... |
Q00934 | MSRQKALIVDDEPDIRELLEITLGRMKLDTRSARNVKEARELLAREPFDLCLTDMRLPDGSGLDLVQYIQQRHPQTPVAMITAYGSLDTAIQALKAGAFDFLTKPVDLGRLRELVATALRLRNPEAEEAPVDNRLLGESPPMRALRNQIGKLARSQAPVYISGESGSGKELVARLIHEQGPRIERPFVPVNCGAIPSELMESEFFGHKKGSFTGAIEDKQGLFQAASGGTLFLDEVADLPMAMQVKLLRAIQEKAVRAVGGQQEVAVDVRILCATHKDLAAEVGAGRFRQDLYYRLNVIELRVPPLRERREDIPLLAERI... | Function: Member of the two-component regulatory system PilS/PilR that regulates the expression of multiple genes including the type IV pilus (T4P) major subunit PilA . Thereby, plays a major role in the regulation of multiple motility pathways . Upon appropriate environmental signals, the histidine kinase PilS transfe... |
Q39VS0 | MNFDIARKRMVETQIISRGVKDRRLIEAMLKVPRHVFVEEAMAAQAYSDTPLPIGEKQTISQPYMVALMTELLELSGREKVLEIGTGSGYQAAILATLADRVYTVERIRPLALKARRALDRLGLLNVNIKISDGTIGWEEEAPFDAIIVTAGAPDVPDKLAEQLAVGGRLVIPVGNQFDQVLVRITKQEDGSLIRENVTGCRFVKLVGKYGWGTEE | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
Q74CZ5 | MVESQIIARGVSDRRVIEAMLKVPRHVFVEEAMAAQAYSDTPLPIGEKQTISQPYMVALMTELLELKGKEKVLEIGTGSGYQAAILAVMADRVYTVERIRPLALRARKALDSLGLLNVNIKMSDGTVGWEDEAPFDAIIVTAGAPDIPQQYIDQLKPGGRLVIPVGTQFEQVLVRVVKQEDGSVERENITGCRFVKLVGKFGWSSDD | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
Q7NJY2 | MVDEQLRPRGVEAQAVLAAMAKVPRHRFVPPPYTRLAYEDRPLPIGHSQTISQPFIVAYMSEAARITPGAKVLEIGTGSGYQAAVLAEMGAEVYTVEIVPELAKRAERTLEELGYRSVRVRSGDGYQGWPQHAPFDAIVVTAAPERIPQPLIDQLAVNGRLIVPVGTQTEDQRMTVLTRTPGGIVEQKTFPVRFVPLTREKPQEH | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
A1WWY5 | MRERNAAGIGMTSQRTRDRLVDALAAQGIQDERVLSAMREVPRHLFVDEALESRAYENTPLPIGEGQTISQPWVVARMTELLLEPGVPERVLEVGTGSGYQAAVLARLVPRVYSIERIGSLLRRARERLQAVRLFNCQLRHGDGYEGWPEYAPYDGIIVTAAPDALPEALLEQLADGGRLVAPIGGAGYQELLVVDRRGDAYEQRRVAGVSFVPMLEGRV | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
P56133 | MNSIKNHLMCEEINKRFNLHPKVREAMESIEREVFVPAPFKHFAYTLNALSMQAQQYISSPLTVAKMTQYLEIDHVDSVLEIGCGSGYQAAVLSQIFRRVFSIERIESLYIEARLRLKTLGLDNVHVKFADGNKGWEQYAPYDRILFSACAKNIPQALIDQLEEGGILVAPIQENNEQVIKRFVKQNNALRVQKVLEKCLFVPVVDGVQ | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
Catalytic Activity: [protein]-L-isoaspartate ... |
A9AUP1 | MSDVWQQQRQRMVDEQLRPRGIHDQRILAAMANVPRHLFVPEALQAQAYSDQALPLTLGQTISQPYIVALMAQELLLNPHEQLLEIGAGSGYAAAVFAELVRKVVTIERHQALAQQTQVRLRNLGYVNIEVVWGDGSLGYPTAAPYHAISIPAATPQLAQTLLSQLHDGGRLVAPIGDAQDQQLIRLQRQGQNWQKTTISNVRFVPLIGAGGWEHAPETTAEGE | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
P22061 | MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATISAPHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK | Function: Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins . Acts on EIF4EBP2, microtubule-associated protein 2, calreticuli... |
Q6L5F6 | MISWHELYMVLSAVVPLYVAMMVAYGSVRWWGVLTPEQCSGINRFVAVIAVPLLSFHFISSSDPYAMNLRFVAADTLQKVLVLAALAAWSRFPARFVPPAWPPLDCSITLFSVSTLPNTLVMGIPLLVSMYGPYSGDLMVQIVVLQSIVWYTLLLFLFEFRAARVLIAAQFPDTAASIAAVHVDPDVVSLEGSQAEAHAEVAPDGRLRMVVCRSSVSRRSAAAAATPRASNLTGVEIYSISSSRNATPRGSTFTLADIPGHQPPNSALRASSFGAADLFSLHSSSRQHTPRPSSFDEHAAARARASATVAPTNDLKDTHM... | Function: May act as a component of the auxin efflux carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62931
Sequence Length: 591
Subcellular Location: Membrane
|
Q06449 | MSASLINRSLTNIRTELDFLKGSNVISNDVYDQINKSLPAKWDPANAPRNASPASLEYVEALYQFDPQQDGDLGLKPGDKVQLLEKLSPEWYKGSCNGRTGIFPANYVKPAFSGSNGPSNLPPPPQYKAQELQQIPTQNSAASSYQQQPFPPPSTNYYQQPQQQPQQAPPPQQQQQQQQHQSSHSHLKSFGSKLGNAAIFGAGASIGSDIVNNIF | Function: Overproduction promotes the de novo induction of the [PSI+] prion form of SUP35. The prion-inducing effect depends on the association with the actin cytoskeleton. Also implicated in prion maintenance during heat stress.
PTM: Ubiquitinated by RSP5. Ubiquitination reduces the protein abundance and its prion-ind... |
Q8RWZ6 | MITWHDLYTVLTAVVPLYVAMILAYGSVQWWKIFSPDQCSGINRFVAIFAVPLLSFHFISTNDPYAMNFRFVAADTLQKIIMLVLLALWANLTKNGSLEWMITIFSLSTLPNTLVMGIPLLIAMYGTYAGSLMVQVVVLQCIIWYTLLLFLFEYRGAKLLIMEQFPETGASIVSFKVESDVVSLDGHDFLETDAEIGNDGKLHVTVRKSNASRRSLMMTPRPSNLTGAEIYSLSSTPRGSNFNHSDFYSVMGFPGGRLSNFGPADLYSVQSSRGPTPRPSNFEENNAVKYGFYNNTNSSVPAAGSYPAPNPEFSTGTGVS... | Function: Acts as a component of the auxin efflux carrier. Plays a role in generating a sink for auxin into columella cells . Maintains the endogenous auxin gradient, which is essential for correct root patterning . Involved in EXO70A3-regulated gravitropic responses in columella cells and in root system architecture (... |
Q4WJM6 | MAPKNNAKGGDKKGKGKDASEGDKGKGGGKGLKPATSINVRHILCEKFSKKEEALEKLRNGAKFDDVAREYSEDKARQGGSLGWKVRGSLNADFEKAAYELEPSTTANPKYVEVKTGFGYHIIMVEGRK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 14004
Sequence Length: 129
EC: 5.2.1.8
|
A6QPY8 | MPPKGKSGSGKGGKGKAASGSESSEKKAQGPKGGGNAVKVRHILCEKHGKILEAMEKLKSGMKFNEVAAQYSEDKARQGGDLGWMTRGSMVGPFQEAAFALPISVLDKPVFTDPPVKTKFGYHIIMVEGRK | Function: Involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA (By similarity).
PTM: Phosphorylated. Phosphorylation occurs both in the nucleus and the cytoplasm. Phosphorylation at Ser-19 does not affect its PPIase activity but is required... |
Q503Y7 | MPPKGKGGKGAKGAAASGSGDSDKKEKAQKGGTAVKVRHILCEKHGKCMEAMEKIKSGMRFSEVAAQYSEDKARQGGDLGWMTRGSMVGPFQDAAFALPISTMDKPVYTDPPVKTKFGYHIIMVEGKK | Function: May be involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to DNA (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 13664
Sequence Length: 128
Subcellular Location: Nucleus
EC: 5.2.1.8
|
Q4I665 | MGKNDKKGADKGGKAKGGDKGKDAKDTKDSGSGGKAKGAQSINVRHILCEKHAKKEEALAKLNDGVKFDEVAREYSEDKARQGGSLGWKTKGSLDPKFEEVAFALETSTTNSPKFVEVKTGFGYHIIMVEGRK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 14288
Sequence Length: 133
EC: 5.2.1.8
|
Q9Y237 | MPPKGKSGSGKAGKGGAASGSDSADKKAQGPKGGGNAVKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKARQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPPVKTKFGYHIIMVEGRK | Function: Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.
PTM: Phosphorylated. Isoform 1 phosphorylation occurs both in the nucleus and the cytoplasm. Isoform 1 phosphorylation at Ser-19 does not affect its PPIase activit... |
Q7RYY4 | MGKDKKASGSGSGSKGGKDAGNKDAGKDAGKASKGAQSINVRHILCEKHGKKEEALAKIRDGADFGAVAREYSEDKARTGGSLGWKQKGTLDPEFEKVAFALETSSTSSPKIGEVKTQFGYHIIMVEGKK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 13658
Sequence Length: 130
EC: 5.2.1.8
|
P34217 | METSSFENAPPAAINDAQDNNINTETNDQETNQQSIETRDAIDKENGVQTETGENSAKNAEQNVSSTNLNNAPTNGALDDDVIPNAIVIKNIPFAIKKEQLLDIIEEMDLPLPYAFNYHFDNGIFRGLAFANFTTPEETTQVITSLNGKEISGRKLKVEYKKMLPQAERERIEREKREKRGQLEEQHRSSSNLSLDSLSKMSGSGNNNTSNNQLFSTLMNGINANSMMNSPMNNTINNNSSNNNNSGNIILNQPSLSAQHTSSSLYQTNVNNQAQMSTERFYAPLPSTSTLPLPPQQLDFNDPDTLEIYSQLLLFKDREK... | Function: Involved in normal G2/M phase transition of the mitotic cell cycle. In association with RAD53, also involved in checkpoint control in response to DNA damage.
PTM: Hyperphosphorylated in response to DNA damage by MEC1.
Sequence Mass (Da): 73776
Sequence Length: 668
Subcellular Location: Cytoplasm
|
Q5JLM1 | MIGWGDVYKVVAATVPLYFALFLGYGSVRWWRIFTREQCDAVNRLVAFFALPFFTFEFTLHTDPFQVNYRAVAADVISKAVIVAVIGAWARFMSKGGCAVSWSITSFSLSTLTNSLVVGVPMARAMYGEWAQQLVVQLSVFQAIVWLTLLLFVLEVRKAAIGMYVDGAEAAAAAGKDVEAAGAAAAAGTVVVAAAAGKPSLWALVKVVAHKLARNPNTYASFVGITWACLANRLHIALPSAFEGSVLIMSKSGTGMAMFSMGLFMAQQEKIIACGTSFAALGLVLKFALGPAAMAIGSIAVGLRGDVLRVAIIQAALPQS... | Function: May act as a component of the auxin efflux carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38625
Sequence Length: 363
Subcellular Location: Membrane
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.