ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P0A2X3 | MKLISWNIDSLNAALTSDSARAKLSQEVLQTLVAENADIIAIQETKLSAKGPTKKHVEILEELFPGYENTWRSSQEPARKGYAGTMFLYKKELTPTISFPEIGAPSTMDLEGRIITLEFDAFFVTQVYTPNAGDGLKRLEERQVWDAKYAEYLAELDKEKPVLATGDYNVAHNEIDLANPASNRRSPGFTDEERAGFTNLLATGFTDTFRHVHGDVPERYTWWAQRSKTSKINNTGWRIDYWLTSNRIADKVTKSDMIDSGARQDHTPIVLEIDL | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Function: In addition to 3'- to 5'-exonuclease and 3'-phosphatase activities, ExoA was shown to make single-strand breaks at apurinic sites in DNA.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphat... |
Q59083 | MTDQTAASPRVLVTGGAGYIGSHVLHALTDAGIPAVTIDDLSAGRREAIPAAVPLVEGDIGSAELLDRVMRDHRVDAVMHFAGSIVVPESVVKPLDYYRNNTANSLTLLGACLRAGIDKVVFSSTAAVYGAPESVPIREDAPTVPINPYGASKLMTEQMLRDAGAAHGLRSVILRYFNVAGADPAGRTGQATPVATHLIKVACQALLGRRPPLAIFGTDYDTPDGTCIRDYIHVSDLADAHVLALLHLRRGGGSLLMNCGYGRGASVREVVRTLEEVSGEQVPATFADRRPGDPPQLVAGADRIREQLGWVPKHDRLDGI... | Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 36701
Sequence Length: 348
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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Q59745 | MAGETVLVVGGAGYIGSHTCLDLANKGYRPVVFDNFSNGHREFVRWGPAEEGDIRDRARLDEVLAKHKPAAILHFAALIEVGESVKDPVSFYENNVIGTLTLLSAAQAAGINAFVFSSTCATYGLPQSVPLDETHRQVPINPYGRTKYIVEQALADYDQYGSLRSVVLRYFNAAGADFEGRIGEWHQPETHAIPLAIDAALGRRQGFKVFGSDYETRDGTCVRDYIHVLDLADAHVRAVEYLLKGGDSVALNLGTGTGTTVKELLGAIEEVSNRPFPVEYIGRREGDSHTLVANNDKARDVLGWVPQYDLSEIIRSAWDW... | Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 35927
Sequence Length: 327
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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P26503 | MQNNNILVVGGAGYIGSHTCLQLAAKGYQPVVYDNLSNGHEEFVKWGVLEKGDIRDRQRLDEVLARHKPRAILHFAAMIEVGESVKDPAAFYDNNVIGTLTLLSAALAAGIDAFVFSSTCATYGLPDSVPMDESHKQAPINPYGRTKWICEQALKDYGLYKGLRSVILRYFNAAGADFEGRIGEWHEPETHAIPLAIDAALGRREGFKVFGTDYDTRDGTCVRDYIHVLDLADAHVRAVDYLLEGGESVALNLGTGTGTTVKELLDAIEKVAKRPFNIGYAERREGDSTTLVANNDKARQVLGWEPQYDLAAITESAWNW... | Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 36113
Sequence Length: 328
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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Q96KP1 | MSRSRQPPLVTGISPNEGIPWTKVTIRGENLGTGPTDLIGLTICGHNCLLTAEWMSASKIVCRVGQAKNDKGDIIVTTKSGGRGTSTVSFKLLKPEKIGILDQSAVWVDEMNYYDMRTDRNKGIPPLSLRPANPLGIEIEKSKFSQKDLEMLFHGMSADFTSENFSAAWYLIENHSNTSFEQLKMAVTNLKRQANKKSEGSLAYVKGGLSTFFEAQDALSAIHQKLEADGTEKVEGSMTQKLENVLNRASNTADTLFQEVLGRKDKADSTRNALNVLQRFKFLFNLPLNIERNIQKGDYDVVINDYEKAKSLFGKTEVQV... | Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence Mass (Da): 104066
Sequence Length: 924
Domain: Interacts with RALA through the TIG domain.
Subcellular Location: Midbody
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Q9D4H1 | MSRSRQPPLVTGISPNEGIPWTKVTIRGENLGTGPTDLIGLTICGHNCLLTAEWMSASKIVCRVGQAKNDKGDIIVTTKSGGKGTSTVSFKLLKPEKIGILDQSAVWVDEMNYYDMRTDRNKGIPPLSLRPANPLGIEIEKCKLPQKNLEVLFHGMSADFTSENFSAAWYLIENHSTTSFEQLKMAVTNLKRQANKKSEGSLAYVKGGLSTFFEAQDALSAIHQKLEADGTEKVEGSMTQKLENVLNRASNTADTLFQEVLGRKDKADSTRNALNVLQRFKFLFNLPLNIKRNIQKGDYDVVINDYEKAKSLFGKTEVQV... | Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence Mass (Da): 103959
Sequence Length: 924
Domain: Interacts with RALA through the TIG domain.
Subcellular Location: Midbody
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Q9SKU2 | MQLFPVILPTLCVFLHLLISGSGSTPPLTHSNQQVAATRWLPATATWYGSAEGDGSSGGACGYGSLVDVKPFKARVGAVSPILFKGGEGCGACYKVRCLDKTICSKRAVTIIATDQSPSGPSAKAKHTHFDLSGAAFGHMAIPGHNGVIRNRGLLNILYRRTACKYRGKNIAFHVNAGSTDYWLSLLIEYEDGEGDIGSMHIRQAGSKEWISMKHIWGANWCIVEGPLKGPFSVKLTTLSNNKTLSATDVIPSNWVPKATYTSRLNFSPVL | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29108
Sequence Length: 271
Subcellular Location: ... |
P58738 | MGSLANNIMVVGAVLAALVAGGSCGPPKVPPGPNITTNYNGKWLTARATWYGQPNGAGAPDNGGACGIKNVNLPPYSGMTACGNVPIFKDGKGCGSCYEVRCKEKPECSGNPVTVYITDMNYEPIAPYHFDLSGKAFGSLAKPGLNDKIRHCGIMDVEFRRVRCKYPAGQKIVFHIEKGCNPNYLAVLVKYVADDGDIVLMEIQDKLSAEWKPMKLSWGAIWRMDTAKALKGPFSIRLTSESGKKVIAKDVIPANWRPDAVYTSNVQFY | Function: May aid fertilization by loosening the cell wall of the stigma and style, thereby facilitating penetration of the pollen tube. Acts selectively on grass cell walls, which are relatively poor in pectins and xyloglucans and rich in glucuronoarabinoxylans and (1-3),(1-4)-beta-D-glucans, when compared with cell w... |
B8PYF3 | MGSLAKIVAVAAVLAALVAGGSCGPPKVPPGPNITTNYNGKWLPAKATWYGQPNGAGPDDNGGACGIKNVNLPPYNGFTACGNPPIFKDGKGCGSCYEIRCNKPECSGQPVTVFITDMNYEPIAPYHFDLSGKAFGAMAKPGLNDKLRHYGIFDLEFRRVRCKYQGGQKIVFHVEKGSNPNYLAMLVKFVADDGDIVLMELKEKSSDWKPMKLSWGAIWRMDTPKALVPPFSIRLTSESGKKVIAQDVIPVNWKPDTVYNSNVQF | Function: May cause loosening of the cell walls.
PTM: Glycosylated.
Sequence Mass (Da): 28775
Sequence Length: 265
Subcellular Location: Secreted
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P85909 | MAGASAKVVAMLLSLQGPXSLRMVSESG | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 2803
Sequence Length: 28
Subcellular Location: Secreted
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Q9SHY6 | MTILVVDRYYMLMNLLFALTCLLLNLTHCFSPKKFNISAATTSDSDWSIAGSTWYGNPTGYGSDGGACGYGNAVAQPPFSKMVSAGGPSLFKSGKGCGACYQVKCTSKSACSKNPVTVVITDECPGCVKESVHFDLSGTAFGAMAISGQDSQLRNVGELQILYKKVECNYIGKTVTFQVDKGSNANSFAVLVAYVNGDGEIGRIELKQALDSDKWLSMSQSWGAVWKLDVSSPLRAPLSLRVTSLESGKTVVASNVIPANWQPGAIYKSNVNF | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29127
Sequence Length: 273
Subcellular Location: ... |
O24230 | MAGASAKVVAMLLSVLATYGFAAGVVYTNDWLPAKATWYGQPNGAGPDDNGGACGFKNTNQYPFMSMTSCGNEPLFQDGKGCGACYQIRCTNNPSCSGQPRTVIITDMNYYPVARYHFDLSGTAFGAMARPGLNDQLRHAGIIDIQFRRVPCYHRGLYVNFHVEAGSNPVYLAVLVEFANKDGTVVQLDVMESLPSGKPTRVWTPMRRSWGSIWRLDANHRLQGPFSLRMVSESGQTVIAHQVIPANWRANTNYGSKVQFR | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q9M0I2 | MQLFPVMLATLCIVLQLLIGSSALATTNRHVSNSHWLPAVATWYGSPNGDGSDGGACGYGTLVDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPGCSKTSTHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRRTACKYRGKNIAFHVNEGSTDFWLSLLVEFEDGEGDIGSMHIRQAGAREWLEMKHVWGANWCIIGGPLKGPFSIKLTTLSAGKTLSATDVVPRNWAPKATYSSRLNFSPVL | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28425
Sequence Length: 264
Subcellular Location: ... |
Q336T5 | MAFSISKKAAVAALFSFLVVTCVAGARPGNFSASDFTADPNWEVARATWYGAPTGAGPDDDGGACGFKNTNQYPFSSMTSCGNEPIFKDGKGCGSCYQIRCVNHPACSGNPETVIITDMNYYPVSKYHFDLSGTAFGAMAKPGQNDQLRHAGIIDIQFKRVPCNFPGLKVTFHVEEGSNPVYFAVLVEYEDGDGDVVQVDLMEANSQSWTPMRESWGSIWRLDSNHRLTAPFSLRITNESGKQLVASQVIPANWAPMAVYRSFVQYSS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q9SHD1 | MASSQRYFALLALFAVSLKFCYCQNETIDVAGSGTAGVTWYGEPFGAGSTGGACGYGSAVANPPLYAMVSAGGPSLFNNGKGCGTCYQVVCIGHPACSGSPITVTITDECPGGPCASEPVHIDLSGKAMGALAKPGQADQLRSAGVIRVNYKRAACLYRGTNIVFRMDAGANPYYISFVVEYENGDGDLSNVEIQPAGGSFISMQEMRSAVWKVNSGSALRGPFNIRLTSGESHKVIVAYNVIPANWKPDESYRSIVNF | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27204
Sequence Length: 259
Subcellular Location: ... |
Q94LR4 | MGSLSSLAAAAVFLSLLAVGHCAAADFNATDADADFAGNGVDFNSSDAAVYWGPWTKARATWYGQPNGAGPDDNGGACGFKHTNQYPFMSMTSCGNQPLFKDGKGCGSCYKIRCTKDQSCSGRSETVIITDMNYYPVAPFHFDLSGTAFGRLAKPGLNDKLRHSGIIDIEFTRVPCEFPGLKIGFHVEEYSNPVYFAVLVEYEDGDGDVVQVDLMESKTAHGPPTGRWTPMRESWGSIWRLDTNHRLQAPFSIRIRNESGKTLVANNVIPANWRPNTFYRSFVQYS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q9M203 | MASSSLKCFSFIVVLTTFFAISLKPCYCHNKTHWNTAGITWYGDREGPGTTGGACGYGDAVAKHPYRCMVSAGGPSLFKDGKGCGACYRLKCDHPLCTKKPIKVMISDECPGCTKESVHFDLSGKAFGALAKRGKGDQLRNLGELKVSYKRACCKHPKTMIAIHVDAGANPYYMSFAVKFANGDGNFACIEVQPAGGQYMKMEEMRSAVWRLSPGVPLKGPFNIRLTSAVSGKKIIAKGVIPEKWSPGAIYHSKVNFPVQRKQK | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28688
Sequence Length: 264
Subcellular Location: ... |
Q7XT39 | MVSRGTFVFAVLVALPILSLPVSGYEQNYTAGRRSTMSLGRGYGWSSGGATWYGGPQGDGSEGGACGYQSAVGQRPFSSMIAAGGPSLFKNGKGCGSCYQIKCTGNRACSGRPVTVVITDSCPGGVCLNEAAHFDMSGTAFGAMANRGMGDRLRSAGVLKIQYKRVPCRFAMNVAFKVDAGSNPYYLAILVQYANGDGDLAAVHIMEARGGGGWKAMQQSWGATWRLNSNTGKPLSPPFSIRLTSGSGKVLVANNVIPSGWQAGLTYRSTVNYAA | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q7XCA7 | MAARMGSKVAAILAILSVLVVHGSCKGHPVNYNVSDASAYGSGWLPARATWYGAPTGAGPDDNGGACGFKNVNQYPFSSMTSCGNEPIFKDGKGCGSCYQIRCNKDPSCSGNIETVIITDMNYYPVARYHFDLSGTAFGAMAKPGLNDKLRHSGIIDIQFRRVPCNYPGLKINFHVEEGSNPVYFAVLVEYEDLDGDVVQVDLMESKSAYGGATGVWTPMRESWGSIWRLDSNHRLQAPFSLRIRSDSGKTLVANNVIPANWSPNSNYRSIVQFS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q9LD07 | MAGRSRRRSFWSVGVAAALLCLLAAHGCSAKHHKPKPTPGGISGNASSSSSNSSTPSIPPPVAPTPTAPTPPIPSPGTGSSNGSSGGGGGGWLNARATWYGAPNGAGPDDNGGACGFKNVNLPPFSAMTSCGNEPLFKDGKGCGSCYQIRCVGHPACSGLPETVIITDMNYYPVSLYHFDLSGTAFGAMAKDNRNDELRHAGIIDIQFRRVPCQYPGLTVTFHVEQGSNPVYMAILVEYENGDGDVVQVDLMESRYSTGGVDGTPTGVWTPMRESWGSIWRLDTNHPLQGPFSLRITNESGKTLIADQVIPADWQPNTVY... | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q10T32 | MVSGDVGVVVYYLLLVLVVVQGCKGSSAVQGEGRWYNESEAIGGAAAWGNAKATWYGQPNGAGAADNGGACGFKKVNQYPFMGMTSCGNQPLYKGGKGCGSCYRVRCNRNPACSGNAQTVAITDMNYFPLSQYHFDLSGIAFGRLAKPGRADDLRRAGIIDVQFARVPCEFPGLKVGFHVEEGSSPVYLAVLVEYENGDGDVAQVDLKEAGAGGGRWTPMRESWGSVWRLDSNHRLRAPFSIRIRSDSGKTLVAPDVIPLNWTPNTFYRSFVQYSS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
P00488 | MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAG... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to ... |
P36316 | MGNIFKPIPKADYQIVETVPQSLTAINSTNLSTYECFKRLIDLAKKEIYIATFCCNLSTNPEGTDILNRLIDVSSKVSVYILVDESSPHKDYEKIKSSHISYIKVDIGVLNNESVGNLLGNFWVVDKLHFYIGSASLMGNALTTIKNMGIYSENNSLAMDLYFRSLDYKIISKKKCLFFTRMATKYHFFKNHNGIFFSDSPEHMVGRKRTFDLDCVIHYIDAAKSTIDLAIVSLLPTKRTKDSIVYWPIIKDALIRAVLERGVKLRVLLGFWKKTDVISKASIKSLNELGVDHIDISTKVFRFPVNSKVDDINNSKMMII... | Function: Envelope protein associated with the inner side of the enveloped virion (EV) membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 43022
Sequence Length: 377
Subcellular Location: Virion membrane
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P26579 | MGNLTSARPAGCKIVETLPATLPLALPTGSMLTYDCFDTLISQTQRELCIASYCCNLRSTPEGGHVLLRLLELARADVRVTIIVDEQSRDADATQLAGVPNLRYLKLDVGELPGGKPGSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLGVYSECEPLARDLRRRFRDYERLCARRCVRCLSLSTRFHLRRHCENAFFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMELLSLVPLVRDEDSVQYWPRMHDALVRAALERNVRVRLLVGLWHRSDVFSLAAVKGLHELGVGHADISVRVFAIPGAKGDAVNNTKLLV... | Function: Envelope protein associated with the inner side of the enveloped virion (EV) membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42808
Sequence Length: 388
Subcellular Location: Virion membrane
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Q0PA50 | MQEVISYIQKAVLEISNALKFPDTSYSQNQNFTGDTQLKFDVLSDEIITKTLSQCSSIKAIISEEKDEILTLNERANFIVAYDPLDGSSLMDVNFAIGSIFAIYEEKASAKNLRAALYSMYGARLELVICKDQPKLYRLNANNEFIFIKDLRMNEKGKINATGGTQKFWEEKHAKFIKSLFDEGYRLRYSGAMVSDINQILLKGGGIFSYPATQDAPNGKLRAFFEVFPLAFIIEKAGGKTTNGKNRSLLELEFDKIHATTPCFFGSEYEISKLLKAYNE | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 31586
Sequence Length: 280
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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Q9EXV4 | MSGATLEAYLASCTARGDDLSRDVAAVIQRLAKAALDIRKLVNQGALGTAFNGTHGGSNTDGDLQKDLDILCDDQFLTCLQGAPVACYASEELENPVLLDPSARLAVAIDPLDGSSNIDNNVSIGTIFSVLPAAKGPDVDPSQSFLQPGNRQLAAGFFIYGPQTALVLSLGKGTEIFIFSSRLGCFVEAYKSAIIPERAHEFAINMSNYRHWEEAIRLYVDDCLAGSEGPRERDFNMRWIASLVAETYRILIRGGIFLYPADGRKGYSQGRLRLVYEANPIAFIIENAGGAATTSIDRILDLVPENLHQRVPLVFGSRRE... | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 38025
Sequence Length: 349
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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O34011 | MAIELEGLGLSPELADVMTRLARVGADLARTIARNGVETDLAAGVGTNAGGDGQKALDVMADDAFREALTGTAVAYYASEEQDEVVTLGKGTLALAIDPLDGSSNIDVNVSIGTIFSIFPATDDPNTSFLRKGSEQIAGGYIIYGPQCALVCSFGRGVHHWVLDLDSRSFKRLPDIKALPQDTSEYAINASNYRHWPSPIRAFIDDLVAGAEGPRGRNFNMRWIASLVAETHRILMRGGVFLYPGDERKGYARGRLRHVYECAPIAFLITQVGGGATDGCEDILSALPDKLHARTPFVFGCAAKVARVTAYHDLPGEETS... | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 35566
Sequence Length: 331
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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Q2RRP2 | MLATDRTTLAQFLVEECRGRAGDDSELLGLLLDVAQACKTISKMTAMGSLAGVHGYNGDVNPQGENQARLDLMSNQAFVRATERTGHAAGLASEEMEEVLGFPESYARGTLLLVFDPLDGSSNIDINGTVGSIFSILPMPRPGEAPQTADFLQSGRQQVAAGYALYGPSTMFVLTIGSGVHGFTLDPLLGDFILTHPSMTVIPESGEFAINSSNSRFWEPPIRAYVDELLAGRSGPRSKDYNMRWIAALVADVHRILLRGGIYLYPRDTKTPDLAGRLRLLYEAAPVAFLMEQAGGRCTTGTRTMLDLVPGSLHERVPLI... | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 38757
Sequence Length: 355
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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M1KXD0 | MEFISFVYTLIAFSSLLYFYLIWSESAKPKTTTHKAPPEASGAWPVIGHLRIMSGHPSAGIPHVNLGMLADKHGPIFSIRLGVHRVVVVSSPEVIKELFTTNDVAVSSRPSVKAGKHLAYDNAMLGFASYGAYWRQLRKIVSLELLSNRRLELQSHVSMSETGQFVKELYKLWEKKKSDGSGTEVGEGVVVDMKRWLGELNMNVVMRMVAGKRFGSGDNAEETKRCRRVMGDFFYLAGFFVPADALPYLGWLDLGGHEKRMKKAAKELDEVVGEWLAEHREREFSGEGKAQDFMDVMISVVKGADLQCEFDVDTIIKATC... | Function: Hydroxylase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inf... |
A0A0B6CGH9 | MRITLQYIKLESKNTKERDMAESKAIGRSLEVPNVQELAKGKLASVPARYVRYSDRENTTLPPLTQIPVIDMQALLHPNSFEAELNSLHKACKQWGFFQLINHGVEAAVMEKMKLEMQEFFNLPLEEKQKFRQSADDMEGYGQSFVVSDEQKLDWADGFSVISLPTYLRKPHLIPKLPAPFRDAIDAYGAQLKELAIKILGFMAEALGMDPHEMTALFEEGIQALRMNYYPPCPQPEMVSGLCPHSDAGGLTILMQVNEVEGLQVRKDGGWVPVSPLPDAFIINLGDILEIVTNGEYFSVEHQATVNGDKERLSVAAFLN... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxoglutarate-dependent dioxygenase (2-ODD) acting as a flavonoid 7-O-demethylase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit ... |
A0A076FFM5 | MPFPMEVLQASSLSFPLLRRHSRNNLINKFRNPTLPRIDIPRQNIDLKTFAATTPTVACPPSDPEIIPEKKEDKFDWYENWYPVATVCDLDKRRPHGRKVIGIDVVVWWDRKENAWKVFDDTCPHRLAPLSEGRIDQWGRLQCVYHGWCFDGVGACKFIPQAPHDGPPVETSKKACVKGVYPSCVRNGIVWFWPNSDPKYKDIYLTNKPHYIPELDDPSFTCTTITREVPYGYEILAENLMDPSHVPYAHYGILELEKVKESSKRDREGGHEMEISVGTIDVNGFSAKHVSADYYFVPPYVYYGRITPNAATKTKDATLP... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Rieske-type, PAO-family oxygenase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-a... |
Q9UBU6 | MAEGPEEARGHPPGQDDGGGDHEPVPSLRGPPTTAVPCPRDDPQAEPQAPGRPTAPGLAAAAAADKLEPPRELRKRGEAASGSGAELQEQAGCEAPEAAAPRERPARLSAREYSRQVHEWLWQSYCGYLTWHSGLAAFPAYCSPQPSPQSFPSGGAAVPQAAAPPPPQLGYYNPFYFLSPGAAGPDPRTAAGISTPAPVAGLGPRAPHVQASVRATPVTRVGSAAPSRSPSETGRQAGREYVIPSLAHRFMAEMVDFFILFFIKATIVLSIMHLSGIKDISKFAMHYIIEEIDEDTSMEDLQKMMVVALIYRLLVCFYEI... | Function: Plays a role in the assembly of the HRD1 complex, a complex involved in the ubiquitin-proteasome-dependent process of ER-associated degradation (ERAD).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44123
Sequence Length: 413
Subcellular Location: Membrane
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A4XJW0 | MAQNVKILSTGRYVPDRVLTNYDLEKMVDTSDEWITQRTGIKERRIVDGTTSTTDLAVRAAKNAMDKAGILPDDIDLVIVATVTPEMFFPSTACLVQKELKLKNAFAFDISAACSGFIYAMAIATHFIQNGFCKNALVIGAEALSRITNWSDRSTCVLFGDGAGAAILSSSDEQGILGFELGSDGENGLLLYCHAFGLSDVTYSQVKENPNFRKIYMEGNEVYKFAVKIMPYAVEKVLEKVGLSSSDIDVFIPHQANIRIIESAAKRLKIPMEKVFVNLHKYGNTSAASIPIALDEAVEEGRIKKGDKVVLVGFGGGLTW... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
A7ZC01 | MPKASLISIASYVPEKILTNFDFEKMVDTSDEWIVKRTGIEQRHIATTEITSDLGTKAAELAIKRSGLEKSQIDAVICATISPDHLCMPSTACKIAANLGLNFGITAFDISAACTGFIYLLELANSLIVSGAKKNVLIIGAEKLSSIIDYTDRSTCILFGDGAGAAVISASEENEIIDIHTASDGRQAELLITPGCGSAFPASDETLKNRLNFIHMSGNEVFKIAVQTLSKSVIEILHANKMQSEDIDFFIPHQANIRIIDAVKNRLNFTDEQCVLTVAKYGNTSSASIPMAINDAYEDGRIKNGSVLLLDAFGGGFTWG... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q9PIH1 | MLKASLKSIASYIPEKILSNADLEKMVDTTDEWITRRTGIKERRIASENENTSDLGTKAALKAIERANLKPEDIDAILVATLSPDYFTMPSTACKIASNLGLVNISAFDISAACSGFIYLLEQAKALVESGLKKNVLIIGAEKTSSIMDYNDRSICILFGDGAGAGVVSLDNENHILDVHTASNGNYGDLLMTQRSQKSSLCQTLSMQMKGNEVFKIAVNTLSNDVVEILAKNNILAQEIDLFIPHQANLRIIKAVQEKLNLSDEKCVITVQKYGNTSAASIPMAMNDAYEEGRLKKGNLILLDAFGGGFTWGSALLKFG... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q9ZCH1 | MTCKIIGSGGYLPPKIISNDELTKFVDTNDKWIRTRTGILQRHIAGDAEYTSHLAFKSAQKAIEDAMISVDDIDLIIICTTTPDNSFPSVATKLHGYLGLTNIPSFDLQAVCAGFIYGLQLAHSLIVSGKYKTILLIGAEKMTSLLDWNDRSTCVLFGDGAGSVILQRSNDDSGLIDSNIFSSGTDYEILYTSGGTSMNGTSGKIVMQGQKLFRHAIEKMLQSIEDLLYANQFSVSDIDYFIPHQANIRIINKLAELLNIEEHKVVKTVEKHANCSAASIPLALSALKESGKIKKGDILLFSAIGAGLTWGGALIRW | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q1AW87 | MNRAYGKMLGVGRALGGRVVTNRDLEAVLDTSDEWISTRTGIRERRFVAEGQSCVTLAVEAARRALEHAGVPGASVDLVVCATSTNPESMPSVACLVGEAVGAAGVGAMDLSAACAGFAYAASVAGAMLASGLASRVLLVGADEMTSIVNVRDRSTGILFGDGAGAVVLDRGDGSSGFVDHILGADGRMAPLGRAGHPGDGKRPLYQNGREIFRFAVRMFPEMVEKIMARNGISLDEVQYIIPHQANARIIQAAARKLEVPEEKLVVNVDRFGNTSAASIPLSYPDIFDGLEPGKYIITVGFGFGLTWAANLYRI | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q1GI69 | MTRRAVVIGAGHYLPDRIVENAEFEATLDTSDEWIRSRSGIERRHFAAEGETTSHMATRAAEAALKSAGRSADDVDAIVLATSTADLTFPSAATMVQSQLGMTKGFAFDVQAVCAGFVYALSNANALIASGQADRVLVIGAETFSRIMDWTDRSTCVLFGDGAGALLLEAQEGEGTSKDRGILATDLNSDGRYKDLLYVDGGVSTQSTGYLRMQGNQVFRHAVEKLASTAHTALERAGASTDEVDWIVPHQANIRIIQGTAKKMGLPMDKVVVTVQDHGNTSAASIPLALSVGVERGQIKPGDLIVTEAIGGGLAWGAVV... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
O15540 | MVEAFCATWKLTNSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFQLGEEFDETTADDRNCKSVVSLDGDKLVHIQKWDGKETNFVREIKDGKMVMTLTFGDVVAVRHYEKA | Function: B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish ... |
P10790 | MVDAFVGTWKLVDSKNFDDYMKSLGVGFATRQVGNMTKPTTIIEVNGDTVIIKTQSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHVQKWNGQETSLVREMVDGKLILTLTHGTAVCTRTYEKQA | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Sequence Mass (Da): 14779
Sequence Length: 133
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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P05413 | MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Sequence Mass (Da): 14858
Sequence Length: 133
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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O13008 | MAEAFAGTWNLKDSKNFDEYMKALGVGFATRQVGGMTKPTTIIEVAGDTVTLKTQSTFKNTEISFKLGAEFDETTADDRKVKSLITIDGGKMVHVQKWDGKETTLVREVSGNALELTLTLGDVVSTRSYVKAE | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Sequence Mass (Da): 14529
Sequence Length: 133
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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P07483 | MADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTHSTFKNTEISFQLGVEFDEVTADDRKVKSVVTLDGGKLVHVQKWDGQETTLTRELSDGKLILTLTHGNVVSTRTYEKEA | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Sequence Mass (Da): 14775
Sequence Length: 133
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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P12104 | MAFDSTWKVDRSENYDKFMEKMGVNIVKRKLAAHDNLKLTITQEGNKFTVKESSAFRNIEVVFELGVTFNYNLADGTELRGTWSLEGNKLIGKFKRTDNGNELNTVREIIGDELVQTYVYEGVEAKRIFKKD | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fat... |
A6X0K0 | MSDANQTKLEAADIQDLLAVLPHRYPFLLIDRIVDIDGDVSATGIKNVTINEPHFTGHFPEKPIMPGVLIVEAMAQTAGAISLLQRKTGRPGVVYFMTIDNAKFRRPVIPGDRLLLHVKKIKQRANISKYECIAEVDGVKVAEAEVAAMISTAEESQ | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17234
Sequence Length: 157
Subcellular Lo... |
Q8K9S4 | MNSDEYIFNIKDILNILPHRYPFLLIDRILDFKAFQYLKALKNCTVNEPFFQGHFIKEPVFPGVLMIEAMSQAAAVLIFKSIGKLNINQLYYFVGIENTRFKKIVVPGDQIFIEVIYLKSKKNFIKFKIFAIVNKKNVCKSTIIFYKKNIFN | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17857
Sequence Length: 152
Subcellular Lo... |
Q89AN9 | MYNSNITDITTLLPHRYPFLLIDRIIAYQKNFNILTIKNISYSEFCFTGHFYKNPVFPGVLILEAIAQSACLLVYKSFGMSYKNNLFYLTNIIDVKFKKKVIPGDQMLINVFVDKHHHRLIRFVGHVSVSKYIVCKATISCLLTNDVVSR | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs (By similarity).
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17358
Sequence Length: 15... |
B8INJ5 | MEPDAMTETPTELGTADIMRVMELLPHRYPFLLVDRITAINGDDSCIGIKNVTINEPQFTGHFPAMPVFPGVLLVEGMAQTAGAICCAHKLQNNTKPSRVYLMTIDKVKFRKPVVPGDTVEYHMKKVSNRRFMWWFRGEAKVNGVLVAEAEIGAMLVTE | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17765
Sequence Length: 159
Subcellular Lo... |
B0JIT3 | MTIVTEALTELEPVIKTTFTVEEIRQLLPHRYPFALVDRIIDYVPGQKAVGLKNVTINEPFFPGHIPNRPLMPGVLIVESMAQVGGVILTQLPGMKGKFFAFAGIDKTRFRRPVVPGDQLIMTVELLSFKMNKIAKMQGEARVDGQLAAQGEMMFSIFD | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17717
Sequence Length: 159
Subcellular Lo... |
Q2RLY7 | MDWNAIQGILPHRYPFLLVDRVLEVEAGRRAVGQKNVSGNEWYFSGHFPGQPVMPGVLIMEALAQVGAVALLSLPEFQGRLALFGGMDRVRFRRQVVPGDVLRLETEIIKLKGRVGKGYGRAFVGEELAAEGELLFAVGEKIE | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15789
Sequence Length: 143
Subcellular Lo... |
Q1D386 | MDIGEILNLLPHRYPFLLVDRVVEIIPGQKLTAYKNVTINEPFFNGHFPGHPVMPGVLILEALAQATAILAYKSENMDPSRKLTYLMGVDGARFRKPVLPGDRLQLEIEVVRHKGAVWKTKGLATVDGARVAEGEFLATVVDKDADAAESAAS | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 16734
Sequence Length: 153
Subcellular Lo... |
B2A8L3 | MKDINEIKELIPHRYPILMVDRLEELEPGHRAKGVKNVSANEPFLQGHFPDRPLMPGVLQIEAMAQVGACALMSLPENEGKLAVFGGVDKVKFKRQVQPGDVLSIEVELTRVKGSIGKGEGKVYVGDELAAQGQLTFALVEK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15545
Sequence Length: 142
Subcellular Lo... |
Q9SZ42 | MAVSLPTKYPLRPITNIPKSHRPSLLRVRVTCSVTTTKPQPNREKLLVEQRTVNLPLSNDQSLQSTKPRPNREKLVVEQRLASPPLSNDPTLKSTWTHRLWVAAGCTTLFVSLAKSVIGGFDSHLCLEPALAGYAGYILADLGSGVYHWAIDNYGDESTPVVGTQIEAFQGHHKWPWTITRRQFANNLHALAQVITFTVLPLDLAFNDPVFHGFVCTFAFCILFSQQFHAWAHGTKSKLPPLVVALQDMGLLVSRRQHAEHHRAPYNNNYCIVSGAWNNVLDESKVFEALEMVFYFQLGVRPRSWSEPNSDWIEETEISN... | Function: Fatty acid desaturase involved in the production of chloroplast-specific phosphatidylglycerol molecular species containing 16:1(3E). Catalyzes the formation of a trans double bond introduced close to the carboxyl group of palmitic acid, which is specifically esterified to the sn-2 glyceryl carbon of phosphati... |
Q9Y1W0 | MYYSNKMSKVITGKQYSWSELAKHNTENDCWVAVDGKVYDITRWVPLHPGGKEVLLLAAGRDVTNLFESYHPMSDKPTSILKNYEIGYISSYEHPKFVQKSDFYKTLKERVRKHFKATDQDPQMAVSIFSRLALVYLLVFVTYYLAHYTSNNFYLNCFLAIVYALCNSLFSMHMMHDSCHAAISHYPGVWKWMGASFDFVTGASFLSWCHQHVIGHHIYTNVRNADPDLGQGEVDFRIVTPFQTRSWYHKYQHIYAPLLYGIYTLKYRTQDWEAFVKDGKNGAIRVSVATNFDKAAYVIGKLSFVFFRFILPLRYHSFTD... | Function: Specific for desaturation of the 5 position in C16 and C18 fatty acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54005
Sequence Length: 464
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding.
Subcellular Location: Membrane
EC: 1.14.1... |
P46312 | MASRIADSLFAFTGPQQCLPRVPKLAASSARVSPGVYAVKPIDLLLKGRTHRSRRCVAPVKRRIGCIKAVAAPVAPPSADSAEDREQLAESYGFRQIGEDLPENVTLKDIMDTLPKEVFEIDDLKALKSVLISVTSYTLGLFMIAKSPWYLLPLAWAWTGTAITGFFVIGHDCAHKSFSKNKLVEDIVGTLAFLPLVYPYEPWRFKHDRHHAKTNMLVHDTAWQPVPPEEFESSPVMRKAIIFGYGPIRPWLSIAHWVNWHFNLKKFRASEVNRVKISLACVFAFMAVGWPLIVYKVGILGWVKFWLMPWLGYHFWMSTF... | Function: Chloroplast omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 16:3 and 18:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglyce... |
P48629 | MESAITISNHVNLAFSLSRNPSLSTKNSAGISCIKWQRPCLRNLGHVRLNQQRKGTRRKSTLVQAVAVPVAQPSAFPPTDNTEHLKQLAERYGFQQIGEPLPDDVTMRDIITSLPKQVFEINDTKAWGTVLISVTSYALGIFMIAKAPWYLLPLAWAWTGTAITGFFVIGHDCAHKSFSKNKLVEDIVGTLAFMPLIYPYEPWRFKHDQHHTKTNMLREDTAWLPIMKEDIESSPGLRKALIYAYGPLRTWMSIAHWLKVHFNLKDFRQSEVKRATISLAAVFAFMVIGWPLIIYKTGIVGWIKFWLMPWLGYHFWMSTF... | Function: Chloroplast omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 16:3 and 18:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglyce... |
P46313 | MGAGGRMPVPTSSKKSETDTTKRVPCEKPPFSVGDLKKAIPPHCFKRSIPRSFSYLISDIIIASCFYYVATNYFSLLPQPLSYLAWPLYWACQGCVLTGIWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKQKSAIKWYGKYLNNPLGRIMMLTVQFVLGWPLYLAFNVSGRPYDGFACHFFPNAPIYNDRERLQIYLSDAGILAVCFGLYRYAAAQGMASMICLYGVPLLIVNAFLVLITYLQHTHPSLPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHL... | Function: ER (microsomal) omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 18:3 fatty acids, important constituents of plant membranes . Delta(12)-desaturase with regioselectivity determined by the double bond (delta(9) position) and carboxyl group of the substrate. Can use both 16... |
Q39287 | MGAGGRMQVSPSPKKSETDTLKRVPCETPPFTVGELKKAIPPHCFKRSIPRSFSYLIWDIIVASCFYYVATTYFPLLPHPLSYVAWPLYWACQGVVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGKYLNNPLGRTVMLTVQFTLGWPLYWAFNVSGRPYPEGFACHFHPNAPIYNDRERLQIYVSDAGILAVCYGLYRYAAAQGVASMVCLYGVPLLIVNAFLVLITYLQHTHPSLPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHH... | Function: ER (microsomal) omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 18:3 fatty acids, important constituents of plant membranes. It is thought to use cytochrome b5 as an electron donor and to act on fatty acids esterified to phosphatidylcholine and, possibly, other phospholi... |
I6XHI4 | MGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDKAGIQSGLHAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGLPEHVGATTVDCQCGSGQQANHLIAGLIAAGAIDVGIACGIEAMSRVGLGANAGPDRSLIRAQSWDIDLPNQFEAAERIAKRRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQAPVLDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIHTAGTSSQISDGAAAVLWMDEAVARAHGLTPRARIVAQALVGAEPYYHLDGPVQSTAKVLEKAGMKIGDIDIVEINEAFAS... | Function: Involved in the beta-oxidation of the cholesterol side chain . It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection . Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yield 3-oxo-4-pregnene-20-carboxyl-C... |
I6XHJ3 | MPRVDDDAVGVPLTGNGRGAVMTEAYVIDAVRTAVGKRGGALAGIHPVDLGALAWRGLLDRTDIDPAAVDDVIAGCVDAIGGQAGNIARLSWLAAGYPEEVPGVTVDRQCGSSQQAISFGAQAIMSGTADVIVAGGVQNMSQIPISSAMTVGEQFGFTSPTNESKQWLHRYGDQEISQFRGSELIAEKWNLSREEMERYSLTSHERAFAAIRAGHFENEIITVETESGPFRVDEGPRESSLEKMAGLQPLVEGGRLTAAMASQISDGASAVLLASERAVKDHGLRPRARIHHISARAADPVFMLTGPIPATRYALDKTGL... | Function: May be involved in the final steps of cholesterol and steroid degradation . Catalyzes the formation of 4-methyl-5-oxo-octanedioyl-CoA (MOODA-CoA) and acetyl-CoA from 6-methyl-3,7-dioxodecanedioyl-CoA (MeDODA-CoA) and coenzyme A (Probable).
Catalytic Activity: acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA
S... |
P46154 | MSGNRGVVYLGSGKVEVQKIDYPKMQDPRGKKIEHGVILKVVSTNICGSDQHMVRGRTTAQVGLVLGHEITGEVIEKGRDVENLQIGDLVSVPFNVACGRCRSCKEMHTGVCLTVNPARAGGAYGYVDMGDWTGGQAEYLLVPYADFNLLKLPDRDKAMEKIRDLTCLSDILPTGYHGAVTAGVGPGSTVYVAGAGPVGLAAAASARLLGAAVVIVGDLNPARLAHAKAQGFEIADLSLDTPLHEQIAALLGEPEVDCAVDAVGFEARGHGHEGAKHEAPATVLNSLMQVTRVAGKIGIPGLYVTEDPGAVDAAAKIGSL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD(+)-dependent oxidation of formaldehyde and acetaldehyde, and, to a lesser extent, long-chain alcohols, but is inactive against propionaldehyde, butyraldehyde, methanol and ethanol. Can also catalyze the dismutation of a wide range of aldehydes such ... |
P10384 | MSQKTLFTKSALAVAVALISTQAWSAGFQLNEFSSSGLGRAYSGEGAIADDAGNVSRNPALITMFDRPTFSAGAVYIDPDVNISGTSPSGRSLKADNIAPTAWVPNMHFVAPINDQFGWGASITSNYGLATEFNDTYAGGSVGGTTDLETMNLNLSGAYRLNNAWSFGLGFNAVYARAKIERFAGDLGQLVAGQIMQSPAGQTQQGQALAATANGIDSNTKIAHLNGNQWGFGWNAGILYELDKNNRYALTYRSEVKIDFKGNYSSDLNRAFNNYGLPIPTATGGATQSGYLTLNLPEMWEVSGYNRVDPQWAIHYSLAY... | Function: Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48542
Sequence Length: 446
Subcellular Location: Cell outer membrane
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P77712 | MQTQIKVRGYHLDVYQHVNNARYLEFLEEARWDGLENSDSFQWMTAHNIAFVVVNININYRRPAVLSDLLTITSQLQQLNGKSGILSQVITLEPEGQVVADALITFVCIDLKTQKALALEGELREKLEQMVK | Function: Long-chain acyl-CoA thioesterase that could be involved in beta-oxidation of fatty acids . Is most active with 3,5-tetradecadienoyl-CoA, a metabolite of oleic acid that is hydrolyzed during oleate beta-oxidation, but can also use other substrates such as 3,5-dodecadienoyl-CoA, 9-cis-octadecenoyl-CoA, octadeca... |
O32178 | MHKHIRKAAVLGSGVMGSGIAAHLANIGIPVLLLDIVPNDLTKEEEKKGLTKDSSEVRSRLSRQAMKKLLKQKPAPLTSAKNTSYITPGNLEDDAEKLKEADWIIEVVVENLEVKKKIFALVDEHRKTGSIVSSNTSGISVQEMAEGRSDDFKAHFLGTHFFNPARYLKLLEIIPIKETDPDILKFMTAFGENVLGKGVVTAKDTPNFIANRIGTYGLLVTVQEMLKGGYQVGEVDSITGPLIGRPKSATFRTLDVVGLDTFAHVARNVYDKADGDEKEVFRIPSFMNDMLEKGWIGSKAGQGFYKKEGKTIYELDPVTL... | Function: Involved in the degradation of long-chain fatty acids.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Mass (Da): 87085
Sequence Length: 789
Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
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Q2HJ98 | MAASRPLSRFWEWGKNIVCVGRNYADHVREMQSAAPSEPVLFLKPSTAYAPEGSPVLVPAYTRNLHHELELAVVMGKRCRAVSEAAAMDYVAGYALCLDMTARDVQDECKKKGLPWTLAKSFTASCPVSAFVPKEKIPDPHNLKLWLKVNGELRQEGETSSMIFSIPYIISYVSKIMTLEEGDIILTGTPKGVGPVKENDEIQAGIHGVLSMKFKVERPEY | Function: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro. Also has oxaloacetate decarboxylase activity.
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24499
Sequence Length: 221
Subcellular Location: Mitochondr... |
Q86I22 | MNKFWETGRKIVAVGRNYAQHAKELGNEIPSEPFFFLKPTSSYLLQGTGPIEIPLESSDIHHEVELGIVIGKKGRDIDLKSAMDYVSGYTLALDMTSRDQQSIAKAKSLPWTVSKGYDTFCPISGFIPKDKIKDLNNVELWCSVDGQIKQKGNTNQMIFDVPHLIQYISSIMTLESGDLILTGTPSGVGPVKPGQVIKCGITGLDTDMQFDIILRKRN | Function: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro.
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24149
Sequence Length: 218
Subcellular Location: Mitochondrion
EC: 3.7.1.5
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Q6P587 | MGIMAASRPLSRFWEWGKNIVCVGRNYADHVREMRSAVLSEPVLFLKPSTAYAPEGSPILMPAYTRNLHHELELGVVMGKRCRAVPEAAAMDYVGGYALCLDMTARDVQDECKKKGLPWTLAKSFTASCPVSAFVPKEKIPDPHKLKLWLKVNGELRQEGETSSMIFSIPYIISYVSKIITLEEGDIILTGTPKGVGPVKENDEIEAGIHGLVSMTFKVEKPEY | Function: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro . Also has oxaloacetate decarboxylase activity .
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24843
Sequence Length: 224
Subcellular Location: Mitochon... |
Q9LUR3 | MATSMIQRLFKQGTKIVGVGLNYASHAKELGNALPKDPIVFLKPTSSYLENGGTIEIPHPLDSLHHEVELAVVIGQKARDVPERLAMNYIGGYALALDMTARELQVSAMASGLPCTLAKGQDTFTPISSVLPKAMVLDPNNLELWLKVDDETRQKGWTKDMIFKVPYLISYISSVMTLFKGDVILTGTPEGIGPVKIGQKITAGITGLSEVQFDVGRRLKPLLR | Function: Probable acylpyruvase. Binds copper in vitro.
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24417
Sequence Length: 224
Subcellular Location: Mitochondrion
EC: 3.7.1.5
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Q10B63 | MAAAAQRLLAASTKIVGVGRNFVAHAKELGNPVPKEPVLFLKPTSSFLHAGVAGAAIEVPEPVESLHHEVELAVVISQRARDVPEASAMDFVGGYALALDMTARELQSAAKSAGLPWTLGKAQDTFTPISAVIPKSDVANPDDLELWLKVDDELRQKGSTSDMIFKIPSLISYISSIMTLMEGDVILTGTPEGVGPVRPGQKIKAGITGLIDVEFDVQKRKRSFST | Function: Probable acylpyruvase.
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24071
Sequence Length: 226
Subcellular Location: Mitochondrion
EC: 3.7.1.5
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Q8RW90 | MALLKSFIDVGSDSHFPIQNLPYGVFKPESNSTPRPAVAIGDLVLDLSAISEAGLFDGLILKDADCFLQPNLNKFLAMGRPAWKEARSTLQRILSSNEPILRDNDVLRRKSFHQMSKVEMIVPMVIGDYTDFFASMHHAKNCGLMFRGPENAINPNWFRLPIAYHGRASSIVISGTDIIRPRGQGHPQGNSEPYFGPSKKLDFELEMAAVVGPGNELGKPIDVNNAADHIFGLLLMNDWSARDIQAWEYVPLGPFLGKSFGTTISPWIVTLDALEPFGCQAPKQDPPPLPYLAEKESVNYDISLEVQLKPSGRDDSCVIT... | Function: Converts fumarylacetoacetate to acetoacetate and fumarate . Involved in tyrosine catabolic pathway. Catalyzes the final step in the tyrosine degradation pathway .
Catalytic Activity: 4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+)
Sequence Mass (Da): 46095
Sequence Length: 421
Pathway: Amino-acid... |
Q9UTM9 | MSRTIVIVGCGVFGLSTAVELAKNHSFDNIIAIDAEPVPSSMSAANDINKIVRPEYADLKYMKLALEAMEKWRNDPELSSVYFECGRLSTISKDPYRARFDEVAQRNLRKLLGDSALINLSSSEEIRKKYPSLFSNSPLRSDMQAVVNEHAGYANSAASLKLLELKARELGVEFVFGKAGKFKKFVVNHSETDIDKNDNHVSVQTEDGTIYHADTILLAVGAYLNAYLNTSHRVCAKGLPVAHIQLTDEEFKTYKNMPIIFDPDCAYAFPPYPVTKLIKLASTGYEYVCNVETDYDENSKVVSIPHSGPSKSSLPKYAII... | Catalytic Activity: H2O + L-saccharopine + O2 = (S)-2-amino-6-oxohexanoate + H2O2 + L-glutamate
Sequence Mass (Da): 48974
Sequence Length: 433
Subcellular Location: Secreted
EC: 1.5.3.18
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O31724 | MDQQIYSLQKKVEEHKEELIQLAKTLISYQTPAPPARNTEGIQSWIAGYLNELGFSIDKWDVYPGDPNVVGKLKGTDSADYYSLIINGHVDVAEVKEDEEWKHDPFHPIEKNGLLIGRGASDMKGGMACVLFAVKLIREASIELPGDLILQSVIGEEVGEAGTLECCKRGYHADFAIVADTSDMHIQGQGGVITGWIEIKSSQTFHDGTRRNMIHAGGGTFGASAIEKMAKIIAGLGELERHWSIMKSYPGFKPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETHDQVAAEIEDYVNRLSDSDIWLRENRPVFK... | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the deformylation of the formylaminopyrimidine N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) to give the corresponding aminopyrimidine.
Catalytic Activity: H2O + N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine = 4-amino-5-aminomethyl-... |
P21268 | MKTPTRVSFEKKIHTPPSGDRDAERSPPKKFLRGLSGKVFRKTPEFKKQQMPTFGYIEESQFTPNLGLMMSKRGNIPKPLNLSKPISPPPSLKKTAGSVASGFSKTGQLSALQSPVNITSSNKYNIKATNLTTSLLRESISDSTTMCDTLSDINLTVMDEDYRIDGDSYYEEDSPTFMISLERNIKKCNSQFSPKRYIGEKCLICEESISSTFTGEKVVESTCSHTSHYNCYLMLFETLYFQGKFPECKICGEVSKPKDKDIVPEMVSKLLTGAGAHDDGPSSNMQQQWIDLKTARSFTGEFPQFTPQEQLIRTADISCD... | Function: Inhibitor of the cyclin-dependent kinase CDC28. Necessary for cell cycle arrest. Involved in pheromone response. Contributes to mating efficiency. Required for oriented polarization of yeast cells in response to mating pheromones.
PTM: Thought to be phosphorylated by MAP kinase FUS3. Thought to enhance the bi... |
G5EGH6 | MTVKTRASIAKKIEKDGLDSQYLFMDPNEVLQVQEESKKIPYKMEIVWRNVALFAALHVAAAIGLYELVFHAKWQTAVFSFALYVFSGFGITAGAHRLWSHKSYKATTPMRIFLMLLNNIALQNDIIEWARDHRCHHKWTDTDADPHNTTRGFFFTHMGWLLVRKHPQVKEHGGKLDLSDLFSDPVLVFQRKHYFPLVILFCFILPTIIPVYFWKETAFIAFYVAGTFRYCFTLHATWCINSAAHYFGWKPYDTSVSAVENVFTTVVAVGEGGHNFHHTFPQDYRASEYSLIYNWTRVLIDTAAVLGLVYDRKTIADEFI... | Function: Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols . Also acts on palmitoyl-CoA (hexadecano... |
Q42561 | MLKLSCNVTDSKLQRSLLFFSHSYRSDPVNFIRRRIVSCSQTKKTGLVPLRAVVSADQGSVVQGLATLADQLRLGSLTEDGLSYKEKFVVRSYEVGSNKTATVETIANLLQEVGCNHAQSVGFSTDGFATTTTMRKLHLIWVTARMHIEIYKYPAWGDVVEIETWCQSEGRIGTRRDWILKDSVTGEVTGRATSKWVMMNQDTRRLQKVSDDVRDEYLVFCPQEPRLAFPEENNRSLKKIPKLEDPAQYSMIGLKPRRADLDMNQHVNNVTYIGWVLESIPQEIVDTHELQVITLDYRRECQQDDVVDSLTTTTSEIGGT... | Function: Plays an essential role in chain termination during de novo fatty acid synthesis. Possesses high thioesterase activity for oleoyl-ACP versus other acyl-ACPs. Substrate preference is 18:1 > 18:0 > 16:1.
Catalytic Activity: (9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]
Sequence Mass (Da... |
Q42712 | VYPHFKTPIQCRFLTSDSISIRRRTAVSRWRSPTFSANYNGVNAQVLGVLKQEQKEIEEEKRSSSLAEKLRLGSLTEDGLSYKEKFIVRCYEVGINKTATVETIANLLQEVGGNHAQSVGFSTDGFATTPTMRKLHLIWVTARMHIEIYRYPAWSDVVEIETWCQSEGRIGTRRDWIIKDFATDEVIGRATSKWVMMNQDTRRLQKVSDDVRDEYLVFCPKTPRLSFPEENNKSLKKISKLEDPAQHSRLGLSPRRADLDMNQHVNNVAYIGWVLESIPKEVLYTHELETITLDYRRECQHDDVVDSLTSPEVDEDTAVT... | Function: Plays an essential role in chain termination during de novo fatty acid synthesis. High thioesterase activity for oleoyl-ACP versus other acyl-ACPs.
Catalytic Activity: (9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]
Sequence Mass (Da): 42348
Sequence Length: 369
Subcellular Location: Pl... |
P11461 | MTHQVATCHKKQSFSGKPTLSRIALLVALQISASALPISITHAEEQADESITVYGQANEAYAAGKISKASSIGMLGDKDFLDTPFNAIGYTDKHIQDQHAQDISDVISASDPSVFTSGETGLNKESFKIRGFSSDIGDVMFNGLYGIAPYYRSSPEMYQRIDVLKGPASLLNGMPPNGSVGGSINLVTKRAQEAPITSFTGTYMSDSQFGGHIDIGRRFGENEQFGVRFNGVFRDGDASVDGQSRKAQLASLSLDWRNDIALIEADLYFSTERVDGPNRGLSIASGVDVPSPPSSDTLLSPSWAYNDSEDKGMMIRAELD... | Function: Involved in the uptake of iron in complex with the siderophore anguibactin. Binds and transports ferric-anguibactin from the cell surface to the periplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78894
Sequence Length: 726
Subcellular Location: Cell outer membrane
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G3ESV0 | TAASSAFFPVPSADTSSRPGKLGNGPSSFSPLKPKSIPNGGLQVKASASAPPKINGSSVGLKSGGLKTHDDAPSAPPPRTFINQLPDWSMLLAAITTAFLAAEKQWMMLDRKPKRLDMLEDPFGLGRVVQDGLVFRQNFSIRSYEIGADRTASIETVMNHLQETALNHVKTAGLSNDGFGRTPEMYKRDLIWVVAKMQVMVNRYPTWGDTVEVNTWVAKSGKNGMRRDWLISDCNTGEILTRASSVWVMMNQKTRKLSKIPDEVRREIEPHFVDSAPVIEDDDRKLPKLDEKSADSIRKGLTPRWNDLDVNQHVNNAKYI... | Function: Plays an essential role in chain termination during de novo fatty acid synthesis (Probable). Possesses thioesterase activity for medium chain acyl-ACPs. Substrate preference is 14:0 > 16:0 > 16:1 .
Catalytic Activity: H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + tetradecanoate
Sequence Mass (Da): 45564
Seq... |
Q9SJE2 | MVATSATSSFFPVPSSSLDPNGKGNKIGSTNLAGLNSAPNSGRMKVKPNAQAPPKINGKKVGLPGSVDIVRTDTETSSHPAPRTFINQLPDWSMLLAAITTIFLAAEKQWMMLDWKPRRSDMLVDPFGIGRIVQDGLVFRQNFSIRSYEIGADRSASIETVMNHLQETALNHVKTAGLLGDGFGSTPEMFKKNLIWVVTRMQVVVDKYPTWGDVVEVDTWVSQSGKNGMRRDWLVRDCNTGETLTRASSVWVMMNKLTRRLSKIPEEVRGEIEPYFVNSDPVLAEDSRKLTKIDDKTADYVRSGLTPRWSDLDVNQHVNN... | Function: Plays an essential role in chain termination during de novo fatty acid synthesis. Possesses high thioesterase activity for palmitoyl-ACP versus other acyl-ACPs. Substrate preference is 16:0 > 18:1 > 18:0 > 16:1. Plays an essential role in the supply of saturated fatty acids necessary for plant growth and seed... |
Q41635 | MATTSLASAFCSMKAVMLARDGRGMKPRSSDLQLRAGNAPTSLKMINGTKFSYTESLKRLPDWSMLFAVITTIFSAAEKQWTNLEWKPKPKLPQLLDDHFGLHGLVFRRTFAIRSYEVGPDRSTSILAVMNHMQEATLNHAKSVGILGDGFGTTLEMSKRDLMWVVRRTHVAVERYPTWGDTVEVECWIGASGNNGMRRDFLVRDCKTGEILTRCTSLSVLMNTRTRRLSTIPDEVRGEIGPAFIDNVAVKDDEIKKLQKLNDSTADYIQGGLTPRWNDLDVNQHVNNLKYVAWVFETVPDSIFESHHISSFTLEYRREC... | Function: Plays an essential role in chain termination during de novo fatty acid synthesis. High thioesterase activity for lauroyl-ACP versus other acyl-ACPs.
Catalytic Activity: dodecanoyl-[ACP] + H2O = dodecanoate + H(+) + holo-[ACP]
Sequence Mass (Da): 42915
Sequence Length: 382
Subcellular Location: Plastid
EC: 3.1... |
P11460 | MFKSTLNIAVAIVCSSLVTLTGCEPKVAQSQVIQPLETPIVIEHNLGQTVISNRPQRVAALDMNEVDFLDQLNVPIAGMVKDFVPHFLEKYKNTPDISDLGAIVQPNMEKIYALKPDLVLMTPLHANQYEELSKLAPTVHFDIDFRNSHGHHVDIIKQHVIDLGEIFNKQTLAQKKVAEIDAKVDEVQALTAERSEKALVVMHNNGSFSSFGIESRYGFVFDVLGVKPASTEIAASLHGQPISSEFINQANPDILYIIDRTAVMEGKPVIDAEHLANPLLRQTKAWKNGKVIFVDADAWYITSASITSLKIVIDDIIKGY... | Function: Involved in the uptake of iron in complex with the siderophore anguibactin. Binds ferric-anguibactin in the periplasm and mediates its transport into the cytoplasm.
Location Topology: Lipid-anchor
Sequence Mass (Da): 35635
Sequence Length: 322
Subcellular Location: Cell inner membrane
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Q81XB2 | MITLDYRNKENVEVDSSLHNESRSASAFRSKKEARRYWIVLITLIALGLLSSYGLLVYNNPVPIDSPSFIPVVKRRIVAIVAMIIAAVCHSLSTVAFQSITNNKIITPSLLGFESLYSAIQTSTVFFFGASALINFNGIGSFLFQVVVMVFMSLILYGWLLSGKYGNLQLMLLVGIIIGTGLNSVSTFMRKLLAPSEFDILQARLFGSVNHADPAYFPIVIPMIIIVAVLIFAHSKNLNVLSLGKDVATSFGVKYQPSVIYTLVLVAILMSISTALIGPLTFYGFLVATLSYQAAATYDHRYIFPMAFAIGFLIMTSAYF... | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39001
Sequence Length: 354
Subcellular Location: Cell membrane
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P37737 | MTSLNLNFRVSVVLVILLSIAFIFINSGFDLEYIIPRRLIKLSAIIIGGSCVAISAVIFQALARNRILTPSIMGYESIYLVWQALLLLFVGTSGSAVLGVVGNFVVSAVLILLYSFVIQFWVLKRFQHDMHQVLLIGFVLTMVLTTVAQFIQIRISPGEFSIFQGLSYTSFERAKPSTLLFAGTVLSILALFANKWVSELDVIGLGRDQAMSLGLNDAHYIPKYFSVIAILVAISTSLIGPTAFMGVFIANIAYSITGSPQYRHTLPVACTIAIVMFLTAQLMVEHFFNYKTTVSILVNVLCGGYFLIITMRARSQL | Function: Involved in the uptake of iron in complex with the siderophore anguibactin. Responsible for the translocation of ferric-anguibactin across the cytoplasmic membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34930
Sequence Length: 317
Subcellular Location: Cell inner membrane
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Q81XB1 | MISRVENISQPQFYNHNKIWTKPFIIAIIVVIILGIISLFTGVYDIRGQEDGMEMFFITRVPRTVALMLTGAAMAMAGLVMQLITQNRFVEPTTTGTIEWSSLGLLFVYLLFPAPTLVQRMTGAIIFSFIGTMIFFLFLRRVKLRSSLIVPIIGLMLGAVISAVSTFLGLLFQMTQSIETWFVGSFANIQVGRYEYLWLIVIVTLLIFMYANRLTLAGLGEDVATSLGVNYNRIVLFGTALISVAVGIVAAVIGNLPFLGLIVPNIVSMFRGDDLRSNLPWVCVIGMGTITACDIISRTIIKPFELPVSLILASVGAVVF... | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37020
Sequence Length: 334
Subcellular Location: Cell membrane
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P37738 | MTFRMILAFFTLCATSLFFGANQIEWSLLPTFNEKAWLPIIASRLPRLVALILTGSGLAMCGVILQHIVRNRFVEPGTTGSLDAAKLGILVSIVMLPSSDKLERMFFAVLFCFAAGLVYIAIIRKVKFSNTALVPVIGLMFGSVLSALAEFYAYQNNILQSMSGWLMGDFSKVVQEHYEIIFLILPITLLTYLYAHRFTVMGMGEDIASNLGISYAMTAALGLILVSITVAVTVVTVGAIHFVGLVIPNLVALKYGDHLKNTLPIVALGGASLLIFCDVISRVVLFPFEVPVGLTASAVGGVMFLAFLLKGAKA | Function: Involved in the uptake of iron in complex with the siderophore anguibactin. Responsible for the translocation of ferric-anguibactin across the cytoplasmic membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33923
Sequence Length: 314
Subcellular Location: Cell inner membrane
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Q5T0N5 | MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTISASKQESGKMDAKTTVGKAKG... | Function: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization ... |
Q94BQ5 | MGRCLTKKVFLIQSPILFLHLLISLSSGAVKPDLKGVCVSKGGRFPPYELEGKPPKSVGRGSKDLTLCRVFRKKTCCSSVQTNPAFVAVRNLATYGEASQECLELFELLECSICNPNVGIQPGPPRICASFCDRVFEACKDAYFASNALKRVIGPCGVNDDIICIKASNWESNGTSFCEAAGFAVQRNDDSREKPCYGSKASLESVVESWSRDSRKETPLKTETLSCFKDLLQWVREMTTIQKISLGMSFLIAGMFLIRQSNNRNQKQRLAAIQRTARRLRGNGNGDSYSAAINRRTSSD | Function: Folic acid-binding protein involved in salicylic acid- (SA-) induced folate accumulation by triggering uptake and accumulation of folic acid in cells . May be implicated in the transport of the folates from the site of production (leaves) to the site of storage (fruits and seeds) and utilization (roots) (Prob... |
Q8TCJ0 | MPFLGQDWRSPGWSWIKTEDGWKRCESCSQKLERENNRCNISHSIILNSEDGEIFNNEEHEYASKKRKKDHFRNDTNTQSFYREKWIYVHKESTKERHGYCTLGEAFNRLDFSSAIQDIRRFNYVVKLLQLIAKSQLTSLSGVAQKNYFNILDKIVQKVLDDHHNPRLIKDLLQDLSSTLCILIRGVGKSVLVGNINIWICRLETILAWQQQLQDLQMTKQVNNGLTLSDLPLHMLNNILYRFSDGWDIITLGQVTPTLYMLSEDRQLWKKLCQYHFAEKQFCRHLILSEKGHIEWKLMYFALQKHYPAKEQYGDTLHFC... | Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) (By similarity).
Sequence Mass (Da): 43313
Sequence Length: 367
Domain: The F-box is necessary for the interaction w... |
Q9D2Y6 | MPFLGQDWRSPGWSWIKTEDGWKRCDPCSHELRSEDSQYTINHSIILNSGEEEIFNNECEYAAKKRKKEHFGNDTAAHSFYREKWIYVHKESTKERHGYCTLGEAFNRLDFSSAIQDIRRFTYVVKLLQLIAKSQLTSLSGVAQKNYFNILDKIVQKVLDDHQNPRLIKGLLQDLSSTLGILVRGVGKSVLVGNINIWICRLETVLSWQQQLQNLQVTKQVNTGLTLSDLPLHMLNNILYRFSDGWDIVTLGQVTPTLYMLSEDRRLWKRLCQYHFAEQQFCRHLILSEKGHIEWKLMYFTLQKYYPTKEQYGDTLHFCR... | Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT).
Sequence Mass (Da): 41826
Sequence Length: 357
Domain: The F-box is necessary for the interaction with SKP1.
Pathwa... |
Q641X7 | MPFLGQDWRSPGWSWIKTEDGWKRCDPCSHEIRSEDNQYPVNHSIILNSGEEEIFNNDCEYAAKKRKKQHFGNDTAAHSFYREKWIYVHKESTKERHGYCTLGEAFNRLDFSSAIQDIRRFTYVVKLLQLIAKSQLTSLSGVAQKNYFNILDKIVQKVLDDHQNPRLIKDLLQDLSSTLCILVRGVGKSVLVGNINIWICRLETVLNWQEKLQNLQMTKQVNTGLTLSDLPLHMLNNILYRFSDGWDIVTLGQVTPTLYMLSEDRRLWKRLCQYHFAEKQFCRHLILSEKGHIEWKLMYFTLQKYYPTKEQYGDTLHFCR... | Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) (By similarity).
Sequence Mass (Da): 41984
Sequence Length: 357
Domain: The F-box is necessary for the interaction w... |
Q969U6 | MDEGGTPLLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWREQFYRYYQVARDVPRHPAAMSWYEEFQRLYDTVPCVEVQTLREHTDQVLHLSFSHSGYQFASCSKDCTVKIWSNDLTISLLHSADMRPYNWSYTQFSQFNKDDSLLLASGVFLGPHNSSSGEIAVISLDSFALLSRVRNKPYDVFGCWLTETSLISGNLHRIGDITSCSVLWLNNAFQDVESENVNVVKRLFKIQNLNASTVRTVMVADCSRFDSPDLLLEAGDPATSPCRIFDLGSDNEEVVAGPAPAHAKEGLRHFLDRVLEGRAQPQLSE... | Function: Substrate recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. Substrate recognition component of the SCF(FBXW5) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SASS6 during ... |
Q969H0 | MNQELLSVGSKRRRTGGSLRGNPSSSQVDEEQMNRVVEEEQQQQLRQQEEEHTARNGEVVGVEPRPGGQNDSQQGQLEENNNRFISVDEDSSGNQEEQEEDEEHAGEQDEEDEEEEEMDQESDDFDQSDDSSREDEHTHTNSVTNSSSIVDLPVHQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSEYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLL... | Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter brings them to the... |
Q8VBV4 | MNQELLSVGSKRRRTGGSLRGNASSSQVDEGQMNRVVEEDPQQQARHQEEEHTARNGELVGANPRPGDQNDTQQGQVEENNNRFISVDEDSSGNQEEQEEDEEHAGEQEEEEEEEEEEEEMDQESDDFDPSDDSSREDEHTHNSNVTNCSSVSDLPAHQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSDYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAED... | Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter brings them to the... |
Q8N3Y1 | MDDYSLDEFRRRWQEELAQAQAPKKRRRPEAAERRARRPEVGSGRGEQASGDPALAQRLLEGAGRPPAARATRAEGQDVASRSRSPLAREGAGGGEQLVDQLIRDLNEMNDVPFFDIQLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLCQQEGHLPDSSISDYSCWKLIFQECRAKEHMLRTNWKNRKGAVSELEHVPDTVLCDVHSHDGVVIAGYTSGDVRVWDTRTWDYVAPFLESEDEEDEPGMQPNVSFVRINSSLAVAAYEDGFLNIWDLRTGKYPVHRFEHDARIQALALSQDDATVATASAF... | Function: Substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7-RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligas... |
L0N065 | MAKFTVTSLERHLLLISTVIAVLAALIVSRGCNYLLKRWKLSAYPLYEDKKVTPIEELHSSRDLIAKGFAKSQGKEIWRINTTIGEVLVVSPKYIEKFRYGHGCSAAAYTERELPISAPGYEPFTFASNEWRQRNADIILHRLTGLVSNRKIELSEELSNALESRWTNSTDWHAVSLFQTMTAIVAQTTQYFFTNRELCRNDAYIQSLFAYSSLAFTEGRSLMKWPRVLHPLVARFHPASQNLQSALENVNKHIFPFVRERRAEISRRRFEAAQSGKETPLADEWVAWLDEKAGNEDYNPGVAMVSFSVASFHTTTDFMC... | Function: Cytochrome P450 monooxygenase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constrictio... |
H7CE84 | MANVVLDGSAAPAKAGLPLDLSSPSKQTNFPTELESNSNADFWWRLCRPEMAGLFKQAGGYTELQQESHLRFVREHCAPWMGTVPTGHMANEAVAPVEMSVNYISSRDEGVLRFQMEPFTAVSGPHTQADDPSGKKAVCSMLRSFQHALGDVDLTWTWQLVDKFMVTAPDEVARLREAERTSLPPPLDLYQRTPQFNFAFDLSPDKKSMKTYFLPLAKSLVTGSSALDYCLDAVRSLEPHGEGLSPVADLLHQFFNTSCPGHMSCDYLGIDSTNPKRSRVKLYVSSQQHNSFNFIRAVFTLGGIAKDEATLRGLEFLRSI... | Function: O-glucose prenyltransferase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constriction ... |
O87838 | MTAKALEGIRVLDMTHVQSGPSATQLLAWLGADVVKLEAPHGDITRGQLRDLPDVDSLYFTMLNCNKRSITLNTKSERGKEILTELIRRSDVMVENFGPGAVDRMGFTWDRVKEINPRIVYASIKGFGEGPYTAFKAYEVVAQAMGGSMSTTGFEDGPPLATGAQIGDSGTGVHVVAGILAALYQREHTGRGQRVNVAMQHAVLNLCRVKLRDQQRLSHGPLAEYPNEDFGDEVPRSGNASGGGQPGWAVKCAPGGPNDYVYVIVQPVGWQPLSELIGRPELAEDPEWATPRARLPKLNKMFQLIEEWSSTLPKWEVLER... | Function: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate (By similarity).
Catalytic Activity: formyl-CoA + oxalate = formate + oxalyl-CoA
Sequence Mass (D... |
Q47162 | MHSTRNKQLKKLKSWHKNKKAMPAVLASTLLMAAHAQAAETTGADTMIVSANAGESVTAPLKGIVAKESASGTKTSTPLIKTPQSVTVVTRDQMDAQAVSSVSDALNYSSGVVTNYRGSSNRNDEVIARGFRYAPKFLDGLSYGLSGQGSTIGKMNPWLLERVEMVHGPASVLYGQVNPGGLISMTSKRPTAETIRKVQFSAGNQHLGEAAFDFGGALNDDKTLLYRLDGIASTKHEFVKDSKQERIAVAPSLTWLPNPDTSFTLLTSYQNDPKAGYRNFLPKIGTVVEASAGYIPYDLNVSDPNYNQSKREQGSIGYNL... | Function: Involved in the initial step of iron uptake by binding chrysobactin, an iron chelatin siderophore that allows the bacteria to extract iron from the environment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80724
Sequence Length: 735
Subcellular Location: Cell outer membrane
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Q05202 | MNQTISSRAPQKRLAPRLLCVMIGAALGTLSASSWAAAATDSTAENAKKTSATAATAKAEDSKTNDTITVVGAQETFRAGGNDLIPTYLDGQVANGGRIGFLGQQDARNVPFNVIGYTSKMIEDQQANSIADVVKNDASVQNVRGYGNPSQNYRIRGYNLDGDDISFGGLFGVLPRQIVSTSMVERVEVFKGANAFINGISPSGSGVGGMINLEPKRAGDTPLTRVTVDYGSASQVGGALDVGRRYGDDDQFGVRVNVLHREGESAIHDQKERTTAVSTGLDYRGDRARTSLDVGYQKQTIHHMRTDVAIGGATVIPEPP... | Function: Receptor for the hydroxamate siderophore, ferrichrome. Binds also to most other ferrichrome derivatives except enantio ferrichrome and ferric rhodotorulate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81749
Sequence Length: 758
Subcellular Location: Cell outer membrane
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Q12178 | MVTGGMASKWDQKGMDIAYEEAALGYKEGGVPIGGCLINNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGKVYKDTTLYTTLSPCDMCTGAIIMYGIPRCVVGENVNFKSKGEKYLQTRGHEVVVVDDERCKKIMKQFIDERPQDWFEDIGE | Function: Catalyzes the hydrolytic deamination of cytosine to uracil or 5-methylcytosine to thymine. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis.
Catalytic Activity: cytosine + H(+) + H2O = NH4(+) + uracil
Sequence Mass (Da): 17507
Sequenc... |
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