ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6MAT6 | MRLSIIEIINSMFSIRLFSPAKINLFLKVIGKRADGYHELSSLFQTISAGDILTFQRQTIDTLTCSDPYLPTDDSNLVLKAMRLFRSKTGLDLHLRIHLDKRLPSQAGLGGGSSNAATTLWACNQLAGEIVTTEELMQWGSEIGADIPFFFSKGTAHCTGRGECVNSLEPLAHCKIWIVKPPFGLSTPEVYKHLNFSQPNENNNDYASFKEKPYFNDLEASAFEIKPELKILKNTLLSSGFDTVLMSGSGSSFFCIGQGQIPASFKAFSAYFINRSSNRWYSTLPKLT | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 32001
Sequence Length: 288
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q72GN2 | MERLAPAKVNLGLSVRFRREDGYHELHTLFAPFSLADRLVVEPVSSGLHFQGPYGRENLAYRAASLYLEAAGQPGGVRILLEKRIPEGAGLGGGSSDAAQVLLALQALYPAEVDLFALARTLGADVPFFLLGRGAEARGVGERLKPLALPPVPAVVFFPGLRVPTPLVYRAVRPEDFGPDLPVEAILEALARGEEPPYWNSLEGPAFRLFPELKEVRGRMRALGLRGVLMSGSGSAFFGLAEGPDHARRAAEALRAWGRAWAGTLGGGDAGSGPA | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 29253
Sequence Length: 275
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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B5YG57 | MLTCKAFAKINWAISVLKKRDDGYHDIISLMQAIDLHDTLIFKSSQKIEIETDLLIKKENNLVYKAIKALQNYTGIKKGVTVILKKEIPLGAGLGGGSSDAATTLKALNELWQLNLDIKTLHEIGASIGSDIPFFFYLPICIVEGRGDVVKPLKISKSYTLLLVKPDFSISTEWAYKTLDLKTELTTEYEKINNNIWQLYNHLYSGDVDNFYLWNDLEKSVLEKYPEIDKIKRKLIEAGAKSSLLSGSGSTVFGLFNNKTDAQKALKFFEGYWCRVVQTLVEPLK | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 32180
Sequence Length: 285
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q3SLR6 | MSQAFPAPAKLNLFLHVVGRRDDGYHLLQSVFRLIDRADTVHLELRDDGRIVREGALPGVSEDQDLTVRAARLLQPYARPGAGVGIRLDKRLPMGGGLGGGSSDAATVLLALNRLWEVDLPRQRLQALALRLGADVPVFVFGQTAFAEGVGELLQPIGAPVAWYVVLTPPVHVPTAAIFAAPELTRNTPALKIAPFSAGMGHNDLEPVVVGRYPEVGRHLQWLGQFGEARMTGSGACVFASFATEDAARSVLQALPDTMQGFVARGLDKHPLYDFVPE | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 29909
Sequence Length: 278
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q73N18 | MIKSAISLKAHAKINLHLEVLGKRSDGFHDIVSVFAPISLADELLMQRKPDKKECKVLSPLAELPAENTITRAYEEFKNFAGISEGISVRILKRIPEGAGLGGGSSDAASVLRGLNDMFSTGLAEEDLRAIALKIGSDVPFFLGNEAAVVRGRGETIKRVSVFSDYFGILIYPEIKSATPRAYSLLGRKESEILNPAFNPELFCGKDCREWPFFNSFEDVLFTEYPAIKKAKQDLLTNGADFALMSGAGSSVFGLFKNEKTVKNAYSKLLAEYGRCFFFLLLAF | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31226
Sequence Length: 284
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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O83386 | MQSLSLRAHAKVNMHLWVGARRADGLHSIESVMQRITLADSLSLSRLDIPGRCEVCSPYMALPRENTLTRAYARFCQVTGVHDGVRVRVVKRIPAGSGLGGGSADAAALLCGLDTLFGTTLSARVLREVAYSVGSDVPFFLASQAACVLGGGEQLVPLVPKTGYLGLLVWPGLHSGSAQAYEDLDRLRACGVHAADGEQYSLRGATALSAHYAQDCARWRFFNSLDAPVQRRYPVVALARWDLARAGACFTAMSGSGSXVFGLYRDEEELRRAHKLLAKRWCWCVRVRLCG | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31592
Sequence Length: 291
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q83FU3 | MKTDGGNTWRASHSKPLNTANTMGEPFSHSEYSVHADQSEFYLNELTEHSGQDNPCMNTSRLNTNRYGHPVVHPCPKIHCICTQSNIAAIGSDCTGCVDIAQACKMLRGGLGCTQDPCVKNPHTQCFTDVSNHAMRNVLPLNVSNTEQFPIQIEYANGRNPVLNPMDDLAMRAALLLSKDIDLQNTHILPSTRISIEKNIPVAAGLAGGSADAAAVLLGINSAWQTNYSRCDLLGKAGALGADVPFLIWGGAAYGSGTGSCVTFFETQTLYWVLCFSKHPLSTRKVFQELDRQRSGAGCNHHPVFSNPAECAEMLKKAIKRGPEALAALLHNDLTSAAKMLMPEIAERIKAAERCPGILRAIISGSGPTLALLAEDAEAANRACSILKDTGVICKAVSSPAYSSIYWQT | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 43957
Sequence Length: 409
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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B5ZCB5 | MKVKSFAKIDLGYSVYKKRKNITKHDFESIFILVESVYDDIEIIKIDKNVDDVHYYNETNEIYVYSRLVYKTLEWIRQTYRIKNHYRINIKKRIPIGAGLGGGSSNAAVIMKSILELEGIKEINYKDVVNKLGADIPFFLSGYKTAYVSDCGSTLEDLSGQFKLSYEVHLMNVNVNTKLVFEKFDDNQWHVIKNNFKTIIKNLKENIVTNIYNDLQEHCFELYPNIRYKYNELLREGFYTILSGAGSSFICIKLKDKENQVIHEN | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 30978
Sequence Length: 265
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q3ZAD6 | MRIGNGYDVHRLAPGQKLVLGGVEIPFECGLIGWSDADVLTHAIMDSLLGAAALGDIGLYFPPGDPKFKGISSLKLLEQVTALLAEKGFGIINVDSVIVAEEPKLRGHVDTMRKHLAKAMGIDPGRVGIKASTSEQLGFVGREEGMAAWAVALVDEK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 16633
Sequence Length: 157
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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Q9RXS6 | MTGLPFRIGYGEDAHRLAPGLPLVLGGVAIPHAELGAVAHSDGDAVLHAVADALLSGLALGDIGQYFPDTAAEWKGMDSRRILAKALELVEERGYRPVNVALVVTLDRPKLGPLRADIAASVAELLGLPAGEVGVSFKTSEGLALEHVQTRVTVLLGRVDD | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 16816
Sequence Length: 161
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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A9A0H0 | MRIGTGYDLHRLVKGRRLVLGGVALPFEKGLDGHSDADVLVHAVCDALLGAAGLGDIGDHFPDTDARFKGVSSLLLLTETGRMLKEKGFFVVNIDATVLAQAPKLGAHKAAMAANMATALGIDAACVNVKATTTEGLDAVGRGEAMAAMSVALIIEEEARDSRGQGAG | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 17296
Sequence Length: 168
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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B7MZ47 | MRIGHGFDVHAFGGEGPIIIGGVRIPYEKGLLAHSDGDVALHALTDALLGAAALGDIGKLFPDTDPAFKGADSRELLREAWRRIQAKGYALGNVDVTIIAQAPKMLPHIPQMRVFIAEDLGCHMDDVNVKATTTEKLGFTGRGEGIACEAVALLIKATK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 16868
Sequence Length: 159
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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Q8ZMF7 | MRIGHGFDVHAFGGEGPIIIGGVRIPYEKGLLAHSDGDVALHALTDALLGAAALGDIGKLFPDTDPAFKGADSRELLREAWRRIQAKGYTLGNVDVTIIAQAPKMLPHIPQMRVFIAEDLGCHMDEVNVKATTTEKLGFTGRGEGIACEAVALLMKAAK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 16900
Sequence Length: 159
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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Q8EBR3 | MKIRIGHGFDVHKFGEPRPLILCGVEVPYETGLVAHSDGDVVLHAISDAILGAMALGDIGKHFPDTDAAYKGADSRVLLRHCYALAKAKGFELGNLDVTIIAQAPKMAPHIEDMRQVLAADLNADVADINVKATTTEKLGFTGRKEGIAVEAVVLLSRQ | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 16996
Sequence Length: 159
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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Q72CD9 | MLGLPGEMQYVPGIHSPNEGPRPMTIQRKQTREVRIGKVRIGGANPVVVQSMTNTDTRDVEQTVEQIRQLQEAGCEIVRLAVLNEDAAWAIKPIRSQVSVPLVADIHFDHRLAVSALEAGVDALRINPGNIGTRAAVDRVVDAAKAHNAVIRIGVNSGSLETDLIDQYGGPTPEAMVESAFRHIRMLEDRNFGDIKVSLKSSSVSRCIEAYTLLSAKCDYPLHIGVTEAGTVLRGSIKSAVGLGVLLWQGIGDTLRVSLTSDPVAEMAVAWEILRSLGLRSRGPEIIACPTCGRCEIGLIALAEEVERRLEGETESFKVAVMGCVVNGPGEAREADLGIAGGRDKGIIFRKGEIVRTVKGGSNLLAAFMEELDTFLAHRRAERKDD | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin]
Sequence Mass (Da): 41683
Sequence Length: 386
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6.
EC: 1.17.7.3
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Q9PL59 | MRKVIICSPRGFCAGVIRAVQTVERALEKWGAPIYVKHEIVHNRHVVDKLRAKGAIFIEDLQEVPCNSRVIYSAHGVPPSVREEAKERGLITIDATCGLVTKIHSAVKMYARRGYLIILIGKRKHVEVIGICGEAPDKITVVENIAEVEALTFSTKDLLFYVTQTTLSMDDSADMIAALKARYPQIITLPSSSICYATQNRQSALRNILPKVEFVYVIGDPKSSNSNQLKAVAARRGVVARLVNNPEEITDEILQYSGNIGVTAGASTPEDVVQACLTKLQKLIPTLVVETDLFVEEDTIFQLPKELQ | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 34010
Sequence Length: 308
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q9Z6P2 | MRKLILCNPRGFCSGVVRAIQVVEVALEKWGAPIYVKHEIVHNRHVVNALRAKGAIFVEELVDVPEGERVIYSAHGIPPSVRAEAKARKLIDIDATCGLVTKVHSAAKLYASKGYKIILIGHKKHVEVIGIVGEVPEHITVVEKVADVEALPFSSDTPLFYITQTTLSLDDVQEISSALLKRYPSIITLPSSSICYATTNRQKALRSVLSRVNYVYVVGDVNSSNSNRLREVALRRGVPADLINNPEDIDTNIVNHSGDIAMTAGASTPEDVVQACIRKLSSLIPGLQVENDIFAVEDVVFQLPKELRCS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 33935
Sequence Length: 310
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q8KFN9 | MKINLDRTSSGFCIGVQGTIHVAEEKLAQSGELYCLGDVVHNEVEVKRLEALGMETIDIPAFEELRNAEVLIRAHGEPPSTYETARKNNLAITDTTCPVVAKLQRTAKMLHQLGYQVVIYGKKVHPEVIGINGQCDDEGVVIKHPDLSDPEEIAPLDLSRKTALISQTTMDVPGFYELKRNLEKLFAEHGHRNPGTQSGEWMAVRDIDITAEKTGALAMPKLVFKDTICRQVSSRNGKLRDFALANDCIVFAAGRKSSNGQVLYSICKDANPHSYFIEDVDEIRPEWFVGENGKPVESVGICGATSTPMWLLEKVANYIDKTFGDGSSNPNA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36573
Sequence Length: 332
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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O84867 | MRKIILCSPRGFCAGVIRAIQTVEVALEKWGRPIYVKHEIVHNRHVVDKLREKGAIFIEDLQEVPRNSRVIFSAHGVPPSVREEAEERGLIAIDATCGLVTKVHSAVKMYAKKGYHIILIGKRKHVEIIGIRGEAPDQITVVENIAEVEALPFSAQDPLFYVTQTTLSMDDAADIVAALKARYPRIFTLPSSSICYATQNRQGALRNILPQVDFVYVIGDTQSSNSNRLREVAERRGVTARLVNHPDEVTEEILQYSGNIGITAGASTPEDVVQACLMKLQELIPDLSIEMDLFVEEDTVFQLPKEL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 34208
Sequence Length: 307
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q2NVY3 | MRILLANPRGFCAGVDRAISIVERALEIYGAPIYVRHEVVHNRYVVDTLRQRGAIFIEQITEVPDGSILIFSAHGVSQAVRAEARSRDLTVFDATCPLVTKVHMEVARASRKGTEAILIGHTGHPEVEGTMGQYNNPAGGMYLVESPEDVWQLEVKNVDNLCFMTQTTLSVDDTSDVIDALRARFPAIIGPRKDDICYATTNRQEAVRSLAADADVVLVVGSKNSSNSNRLSELAQRVGKPAYLIDSAGDIQESWLQGTQTIGVTAGASAPDILVQQVIERLRLLGAEGAKELIGREENIVFEVPKELRLEVKTVE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 34560
Sequence Length: 316
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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C4XUD2 | MKLLRAQTAGFCMGVDLALKKLAALIDAPAKDAPAKAIVTFGPIIHNPQVLEDYAAKGVGVVNDPAAIAPGTTVVIRAHGIPDPVRRAIADRGAEIVDATCPKVKKAQTLIQAQAKQGRTLLLFGEEDHPEVKGLLSYATAGAHVFGDMEELEKLDLPHGPTYFLAAQTTQDEQEFLRIRDYLRNRFGAGLTVLSTICNATMNRQQEAMDLAAAVDFLVVVGGRDSGNTRRLAQVARSAGTPSVHIETADELSPGMFTGYATIGLTAGASTPKKIIDRVQQVLESY | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 30499
Sequence Length: 286
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q758T2 | MSAWASQEAAKEEEAVGDFARMLERRDAGLLARVLSRAQTGPEAYVRGLWRAEVGLERWRLTRVLGCGSVACVFELGDGALALKVPTSRRKAPVLLHEVLIYSHLAQQAGGRLAERHVVPFHGVAAVTRREYRRLRGGEVVPALVLERMDTTLEAVHRRAAVSKGQWWRYARDLVAALQFLRESCVVHGDIKTANVLVRGQDAFLADFTSAAVCDAAPEPLTTTLEYCAPGLIGGGQPTHSTDVYAAGLCLLALITRFEPFRELSMMKSHSSAPTHSLHETQWLMNAISKGDPIKYNVLSQDLYDRWAEELHFLRRFFVPAAQDALSRWLAESNARVAEHAF | Function: Probable serine/threonine protein kinase which may function redundantly with MPK1-independent branch of the PCK1 pathway.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 37967
Sequence Length: 342
EC: 2.7.11.1
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Q06098 | MNSTPPTSPVTRVSDGSFPSISNNSKGFAYRQPQKHKSNFAYSHLVSPVEEPTAKFSEAFQTDYSSKAPVATSEAHLKNDLDVLFTTPRFYSPENLALMFRLSNTVSSLEFLDEFLMGILLAPEMDFLSNPSYSLPSNKLVGQGSYSYVYPISSSASSRCNNDSGVVLKFAKSQHKSKVILQEALTLAYLQYMSPSTNESHIIPFYGLTYITKSHFRRLRSNECVPGLILPKCEMSLYHFNTAVSHKLSLITKRKIWWRLMKQMIDALKSLKTNGIIHGDIKTANILITEMHVLNGGHCKDFDFYLADFTSAFHINQTPTDLNTTVEYCAPELIDSSSDHVPTFESDLYAVGLCLLSFISQHEPYNELQALVSHGSSPGIGSSSIQQSQWLINALLKKDPINLNMLRNDLFQDWKSELALLSRILVDRLPLENLITILDSNYI | Function: Probable serine/threonine protein kinase which may function redundantly with MPK1-independent branch of the PCK1 pathway that is presumed to be required for the tolerance to high temperatures and staurosporine.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 49736
Sequence Length: 443
EC: 2.7.11.1
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Q9C969 | MGSFGMLSRRTLGTDMPVMAQIRSLMAELTNPMSLAQGVVHWQPPQKALEKVKELVWDPIISSYGPDEGLPELRQALLKKLREENKLTNSQVMVTAGANQAFVNLVITLCDAGDSVVMFEPYYFNSYMAFQMTGVTNIIVGPGQSDTLYPDADWLERTLSESKPTPKVVTVVNPGNPSGTYVPEPLLKRIAQICKDAGCWLIVDNTYEYFMYDGLKHCCVEGDHIVNVFSFSKTYGMMGWRLGYIAYSERLDGFATELVKIQDNIPICAAIISQRLAVYALEEGSGWITERVKSLVKNRDIVKEALEPLGKENVKGGEGAIYLWAKLPEGHRDDFKVVRWLAHRHGVVVIPGCASGSPGYLRVSFGGLQEVEMRAAAARLRKGIEELLHHGMVE | Function: Coordinates and prevents auxin (IAA) and ethylene biosynthesis, thus regulating auxin homeostasis in young seedlings . Shows aminotransferase activity with methionine; can use the ethylene biosynthetic intermediate L-methionine (L-Met) as an amino donor and the auxin biosynthetic intermediate, indole-3-pyruvic acid (3-IPA) as an amino acceptor to produce L-tryptophan (L-Trp) and 2-oxo-4-methylthiobutyric acid (KMBA) . Can also use tryptophan (Trp), phenylalanine (Phe), and tyrosine (Tyr) as substrates. Regulates tryptophan (Trp) homeostasis and catabolism in mature plants. Also possibly involved in the metabolism of other aromatic amino acids and phenylpropanoid homeostasis .
Catalytic Activity: a 2-oxocarboxylate + L-methionine = 4-methylsulfanyl-2-oxobutanoate + an L-alpha-amino acid
Sequence Mass (Da): 43762
Sequence Length: 394
Subcellular Location: Cytoplasm
EC: 2.6.1.27
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P38250 | MSQTITSLDPNCVIVFNKTSSANEKSLNVEFKRLNIHSIIEPGHDLQTSYAFIRIHQDNAKPLFSFLQNLDFIESIIPYHDTELSDDLHKLISISKSKILEAPKQYELYNLSNLTNNPKQSLYFAFLQNYIKWLIPFSFFGLSIRFLSNFTYEFNSTYSLFAILWTLSFTAFWLYKYEPFWSDRLSKYSSFSTIEFLQDKQKAQKKASSVIMLKKCCFIPVALLFGAILLSFQLYCFALEIFIKQIYNGPMISILSFLPTILICTFTPVLTVIYNKYFVEPMTKWENHSSVVNAKKSKEAKNFVIIFLSSYVPLLITLFLYLPMGHLLTAEIRTKVFNAFSILARLPTHDSDFIIDTKRYEDQFFYFIVINQLIQFSMENFVPSLVSIAQQKINGPNPNFVKAESEIGKAQLSSSDMKIWSKVKSYQTDPWGATFDLDANFKKLLLQFGYLVMFSTIWPLAPFICLIVNLIVYQVDLRKAVLYSKPEYFPFPIYDKPSSVSNTQKLTVGLWNSVLVMFSILGCVITATLTYMYQSCNIPGVGAHTSIHTNKAWYLANPINHSWINIVLYAVFIEHVSVAIFFLFSSILKSSHDDVANGIVPKHVVNVQNPPKQEVFEKIPSPEFNSNNEKELVQRKGSANEKLHQELGEKQPASSANGYEAHAATHANNDPSSLSSASSPSLSSSSSSSKTGVVKAVDNDTAGSAGKKPLATESTEKRNSLVKVPTVGSYGVAGATLPETIPTSKNYYLRFDEDGKSIRDAKSSAESSNATNNNTLGTESKLLPDGDAVDALSRKIDQIPKIAVTGGENNENTQAKDDAATKTPLIKDANIKPVVNAAVNDNQSKVSVATEQTKKTEVSTKNGPSRSISTKETKDSARPSNNNTTTTTTTDATQPHHHHHHHRHRDAGVKNVTNNSKTTESSSSSSAAKEKPKHKKGLLHKLKKKL | Function: May be involved in ion homeostasis together with BTN1 or BTN2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105854
Sequence Length: 946
Subcellular Location: Cell membrane
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Q08881 | MNNFILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQVVHDNYLLYVFAPDRESRQRWVLALKEETRNNNSLVPKYHPNFWMDGKWRCCSQLEKLATGCAQYDPTKNASKKPLPPTPEDNRRPLWEPEETVVIALYDYQTNDPQELALRRNEEYCLLDSSEIHWWRVQDRNGHEGYVPSSYLVEKSPNNLETYEWYNKSISRDKAEKLLLDTGKEGAFMVRDSRTAGTYTVSVFTKAVVSENNPCIKHYHIKETNDNPKRYYVAEKYVFDSIPLLINYHQHNGGGLVTRLRYPVCFGRQKAPVTAGLRYGKWVIDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFAAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGENQVIKVSDFGMTRFVLDDQYTSSTGTKFPVKWASPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWKERPEDRPAFSRLLRQLAEIAESGL | Cofactor: Binds 1 zinc ion per subunit.
Function: Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation . Required for TCR-mediated calcium response in gamma-delta T-cells, may also be involved in the modulation of the transcriptomic signature in the Vgamma2-positive subset of immature gamma-delta T-cells (By similarity). Phosphorylates TBX21 at 'Tyr-530' and mediates its interaction with GATA3 (By similarity).
PTM: Phosphorylated at Tyr-512 in the activation loop of the kinase domain by LCK. Subsequent autophosphorylation at Tyr-180 leads to the kinase activation. The autophosphorylated Tyr-180 lies within the substrate binding sequence of the SH3 domain.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 71831
Sequence Length: 620
Domain: The N-terminal PH domain allows ITK to be recruited to the plasma membrane by an activated PI3 kinase. This domain contains also a proline-rich region (PRR). The adjoining domain is a SH3 domain, which binds to PRR (from itself or from other proteins). Next, a SH2 domain is required for binding tyrosine-phosphorylated substrates. In the C-terminal region, the kinase domain is required for tyrosine phosphorylation.
Subcellular Location: Cytoplasm
EC: 2.7.10.2
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O88310 | MTQLGFLLFIMVATRGCSAAEENLDTNRWGNSFFSSLPRSCKEIKQEHTKAQDGLYFLRTKNGVIYQTFCDMTTAGGGWTLVASVHENNMRGKCTVGDRWSSQQGNRADYPEGDGNWANYNTFGSAEAATSDDYKNPGYFDIQAENLGIWHVPNKSPLHNWRKSSLLRYRTFTGFLQHLGHNLFGLYKKYPVKYGEGKCWTDNGPALPVVYDFGDARKTASYYSPSGQREFTAGYVQFRVFNNERAASALCAGVRVTGCNTEHHCIGGGGFFPEGNPVQCGDFASFDWDGYGTHNGYSSSRKITEAAVLLFYR | Function: Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner . Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO). Binds to glycans from Gram-positive and Gram-negative bacteria, including K.pneumoniae, S.pneumoniae, Y.pestis, P.mirabilis and P.vulgaris. Does not bind mammalian glycans. Probably plays a role in the defense system against microorganisms. May function as adipokine that has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May interact with lactoferrin/LTF and increase its uptake, and may thereby play a role in iron absorption (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 34953
Sequence Length: 313
Subcellular Location: Cell membrane
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Q8WWA0 | MNQLSFLLFLIATTRGWSTDEANTYFKEWTCSSSPSLPRSCKEIKDECPSAFDGLYFLRTENGVIYQTFCDMTSGGGGWTLVASVHENDMRGKCTVGDRWSSQQGSKAVYPEGDGNWANYNTFGSAEAATSDDYKNPGYYDIQAKDLGIWHVPNKSPMQHWRNSSLLRYRTDTGFLQTLGHNLFGIYQKYPVKYGEGKCWTDNGPVIPVVYDFGDAQKTASYYSPYGQREFTAGFVQFRVFNNERAANALCAGMRVTGCNTEHHCIGGGGYFPEASPQQCGDFSGFDWSGYGTHVGYSSSREITEAAVLLFYR | Function: Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner . Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO) . Binds to glycans from Gram-positive and Gram-negative bacteria, including K.pneumoniae, S.pneumoniae, Y.pestis, P.mirabilis and P.vulgaris . Does not bind human glycans . Probably plays a role in the defense system against microorganisms (Probable). May function as adipokine that has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes . Increases AKT phosphorylation in the absence and presence of insulin . May interact with lactoferrin/LTF and increase its uptake, and may thereby play a role in iron absorption .
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 34962
Sequence Length: 313
Subcellular Location: Cell membrane
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Q5PPM0 | MLSYSLLLLALAFPAGHAGSCEQASISEKKEKILNLLACWTEGNADNSLSRSGGSPTGDMNYGYRSCNEIKSSDSRAPDGIYTLATEDGESYQTFCDMTTNGGGWTLVASVHENNMFGKCTVGDRWSTQQGNMLQNPEGDGNWANYATFGLPEGATSDDYKNPGYYDIEAKNLALWHVPNKTPMVMWRNSSILRYRTQNGFLTEEGGNLFELYKKYPVKYDIGKCLADNGPAVPVVYDLGSAEKTASLYSPNGRSEFTPGFVQFRAVNSERATLALCAGVKVKGCNVEHHCIGGGGYIPEGSPRQCGDFAALDWDGYGTNLGWSASKQIIEAAVMLFYR | Function: Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner . Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf) and D-phosphoglycerol-modified glycans . Binds to S.pneumoniae serotypes with glycans that contain beta-linked D-galactofuranose (beta-Galf) and with D-phosphoglycerol-modified glycans . Can bind a variety of monosaccharides (in vitro) . Probably plays a role in the defense system against microorganisms (Probable).
PTM: N-glycosylated.
Sequence Mass (Da): 36916
Sequence Length: 339
Subcellular Location: Secreted
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Q9Y287 | MVKVTFNSALAQKEAKKDEPKSGEEALIIPPDAVAVDCKDPDDVVPVGQRRAWCWCMCFGLAFMLAGVILGGAYLYKYFALQPDDVYYCGIKYIKDDVILNEPSADAPAALYQTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKLQRRETIKGIQKREASNCFAIRHFENKFAVETLICS | Function: Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites.
PTM: The ectodomain C-terminal part of the imBRI2 is processed by furin producing a secreted Bri23 peptide and a mature BRI2, membrane form (mBRI2). The remaining part of the ectodomain of mBRI2 containing the BRICHOS domain is cleaved by ADAM10 and is secreted (BRI2C, soluble form). The membrane-bound N-terminal fragment (BRI2C, membrane form) is further proteolytically processed by SPPL2A and SPPL2B through regulated intramembrane proteolysis producing a secreted C-peptide and a BRI2 intracellular domain (BRI2 ICD) released in the cytosol. Shedding by ADAM10 facilitates intramembrane cleavage but is not absolutely required for BRI2 ICD generation.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 30338
Sequence Length: 266
Subcellular Location: Golgi apparatus membrane
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C0HK48 | SVELDSDGEPIRNGGGLYYILPVVQGKGGGLEFAKTGSQS | Function: Inhibits trypsin but not chymotrypsin, papain or porcine pancreatic alpha-amylase. Has insecticidal activity against A.aegypti. Functions by inhibiting the A.aegypti midgut proteases to reduce the survival of larva and adults.
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence Mass (Da): 4097
Sequence Length: 40
EC: 3.4.21.4
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Q90334 | MEEMFKEQDFWSFNESSRNSTVGNETFGGNQTVNPLKRNEEVAKVEVTVLALVLFLALAGNLCVLIAIYTAKHTQSRMYYLMKHLSIADLVVAVFQVLPQLIWDITFRFYGPDFLCRLVKYLQTVGMFASTYMLVLMSIDRCIAICQPLRSLHKRKDRCYVIVSWALSLVFSVPQVYIFSLREIGNGVYDCWGDFVQPWGAKAYITWISLTIYIIPVAILGGCYGLISFKIWQNFKRKTKKDQCITLTTAASKANALARVSSVKLVSKAKITTVKMTFVIVLAYIVCWTPFFFVQMWSAWDPEAPREAMPFIISMLLASLNSCCNPWIYMFFAGHLFHDLKQSLLCCSTLYLKSSQCRCDQEHDSRKSNCSTYVIKSTSSQRSITQSSIT | Function: Binds to isotocin. Can also be activated by vasotocin, mesotocin, oxytocin and Arg-vasopressin, although these have lower potencies than isotocin. Produces an induction of membrane chloride currents indicating that it is coupled to the inositol phosphate/calcium pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44504
Sequence Length: 390
Subcellular Location: Cell membrane
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O13853 | MKIDSNGIVNPHSITNEIPSYDEKQAVDLNGNAFAPNGTFQKKDLISHKNDFERTMRHDVLHTNPKIEVRSETHIYEPNDSLFKENQDFPSNPTAHSPSSSSNDSVITATGVPDGILRDSPIVSALEPPSSNSSSSPQLQNLKHQLSSPQPSRAPIDRSSSNPVTSSQQPPNDRSTLSSSQKAKRPLKRSYSEKNSSNAEPSGSRSGDRGTNVSTSGSLLDGIPPDIGSASWAEAVKQKRVNMRRRREELDDECVLVGTRVSEGHENYVTAYNMLTGIRVGVSRCQAKMDRELTPADFTARHKFTFDITGNELTPSAKYDFKFKDYAPWVFRHLRQLFHLDAADYLVSLTSKYILSELDSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLREILYDYYEHVKNNPNTLISQFYGLHRVKLPFGRKIHFVVMNNLFPPHRDIHQTFDLKGSTLGRELDENQPCQSPMCTMKDTNWIRRNMHLQFGPLKRQIFLTQVKADIDMLSSLGIMDYSLLVGIHDLSRGNRDKIRNSILSVYDPNVSQHRVPSINGNESHSNVHVIRQVVNSTGPVSLDQSCNLLPTDQFVERRNFMFYSDDGGFQATDENNEPGNFIFYIGIIDLLTKYSYVKRVEHLWKGINHSDSVISAVPPAEYASRFYKFVESSIKPTLLVLKPFPLKPQDGQRVNKQQSVNAGNVRTNNKHGSLNNNTAPSSRNAKSTSAHKSPKTEHRFPFPCRNVTTNTSSS | Function: Involved, together with the calcineurin ppb1, in cytokinesis.
PTM: Phosphorylated by casein kinase I. Phosphorylation inactivates the enzyme.
Location Topology: Peripheral membrane protein
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 (Da): 83748
Sequence Length: 742
Subcellular Location: Nucleus
EC: 2.7.1.68
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Q7N7H2 | MQKVVLATGNPGKVRELAQLLADFGLDIVAQTELGVDSAEETGLTFIENAILKARHAAQVTGLPAIADDSGLSVDILGGAPGIYSARYAGENATDQQNLEKLLDTMKDIPDDQRQAQFNCVLVYIRHAEDPTPLVFHGRWPGFIAHKSAGNGGFGYDPIFYIPELGCTAAELTGEQKNAVSHRGQALKMMLDTLRNA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21163
Sequence Length: 197
EC: 3.6.1.66
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Q6L1H9 | MLFITSNRHKYEEAAEFLGNYNIDIKWKNMKYEEIQGDTNKEISMDSCRKLMYKIKDDFFIDDTGLYIDDLNGFPGPYASYVNKTLGNKNIIRLASGSRAHFETVISLFYSGKIYQFSGILNGTISDHESGSMNFGYDPIFIPDGYDKSLAELSISEKNRISHRSKALEIMVEFLKKQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 20477
Sequence Length: 178
EC: 3.6.1.66
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Q7MUC6 | MEKLIFATNNPHKLNEIRHILEGKVEIVGLDEIGCREDIPETADTLQGNALLKAEFVHKRYGLPCFADDTGLEVEALDRAPGVHSARYAGEPTNADANVRKLLEALSSVPHPRKACFRTVIALIDDHGKHFFEGKIEGTIASECRGSGGFGYDPVFIPEGHTLSFAEMGEETKNQISHRALAVAQLRDFLLCAK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21306
Sequence Length: 194
EC: 3.6.1.66
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Q7VDQ7 | MSFNLGKSLTKLIIASNNDGKIEEFIQLLSGIPLVVMGQPKHLEVEETGVSFAENARIKAIAVAKATGEMALADDSGLSVGSLGGAPGVFSARYANTDLERVSRLLKELEMVDDRSAFFSAALCLASSKGEVLLELDGRCDGIITTTPRGKFGFGYDPIFEVKGTGLTFSEMDSKQKRELSHRGLAVKKLIPSLKKILDS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21440
Sequence Length: 200
EC: 3.6.1.66
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Q7V316 | MKKLYLASKNQGKIEEYKKLLLNVNCQLLLQPESIEVEENGITFRENAIKKASEVSKKTRNYAIADDSGICIDALDGRPGIYSSRYAENDQKRIERVLHELDGEKNRGAFFIANVCVCSPSRDVILESEAKCFGNIILSPRGKGGFGYDPIFEERSTRLTFAEMNNVIKDSCSHRGRALKKIIPGLLEIFS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21480
Sequence Length: 191
EC: 3.6.1.66
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Q9I6A8 | MIKLEQLVLASHNAGKLKELQAMLGASVKVRSIGEFSQVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPGIYSARYADGRGDAANNAKLLEAMKDVPDAERGAQFVSVLALVRHADDPLPILCEGIWEGRILREARGAHGFGYDPLFWVPERDCSSAELAPEEKNRLSHRARAMALLKQRLGL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21242
Sequence Length: 197
EC: 3.6.1.66
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Q88CT0 | MMNFQQLVLASHNAGKLKELQAMLGHSVQLHSIGEFSQVEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPGIYSARYADGKGDAANNAKLLEALKDVPEAERSAQFVCVLALVRHADDPLPILCEGLWHGRILFEASGDQGFGYDPLFWVPERNCSSADLAPADKNQLSHRARAMALLRKRLGLA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21303
Sequence Length: 198
EC: 3.6.1.66
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Q8ZVB5 | MRIRLATNNPYKLAEVSHILAPFCIEVERLDAEKVEIQHDDVVVIARKAAEFLCSRYGDFVVVDDTGLYIEALGGFPGPYAEYVYRTIGLKGVLKLLEGAADRRATFKCAAAICIGGRVEVFVGEVRGYIAHEPRGRGGFGYDPIFIPEGMTATYAELGEEVKNKISHRAKAFSQLGAWLTNRNLFK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 20717
Sequence Length: 187
EC: 3.6.1.66
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Q8U446 | MELFFITSNDGKVREAKKFLEPLGINVIKKPLEYPEIQADTLEDVVVFGLNWLKDKVDKPFIIEDSGLFIEALNGFPGVYSAYVYKTIGLDGILKLMEGIENRKAYFKSVIGFYDGEIHLFVGEVRGRISNEKRGLHGFGYDPIFVPDGFDKTFAEMSTEEKNSVSHRGKALKEFYRWMKENLKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21217
Sequence Length: 185
EC: 3.6.1.66
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O59580 | MKIFFITSNPGKVREVANFLGTFGIEIVQLKHEYPEIQAEKLEDVVDFGISWLKGKVPEPFMIEDSGLFIESLKGFPGVYSSYVYRTIGLEGILKLMEGAEDRRAYFKSVIGFYIDGKAYKFSGVTWGRISNEKRGTHGFGYDPIFIPEGSEKTFAEMTIEEKNALSHRGKALKAFFEWLKVNLKY | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21205
Sequence Length: 186
EC: 3.6.1.66
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Q98DN4 | MHTLDGKKIVVASHNAGKLREFADLMGPFGFEAKSAKDYGLPEPDETGTTFEENAYIKALAAAKATGLPALSDDSGLCVDALDGAPGVYTANWAETPDGSRDFAMAMQRTEVALQEVGAASAEQRKGRFVAVICLAFPDGAAEYYRGEAEGTLVWPPRGELGFGYDPVFLPNGFDKTFGEMSAEEKHGWKPGQAAALSHRARAFQKFAQARLDLPRLGSA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 23520
Sequence Length: 220
EC: 3.6.1.66
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Q92SK4 | MRRLIDKTLVVASHNAGKIREIRDLIGPLGFEAKSAADLNFVEPDETGTTFEENATIKALASAKASGLPALSDDSGLAVDALGGAPGVYTANWAEREDGSRDFQMAMEKVEEALRAKGAVKPESRTARFVSVLCLAWPDGHVELFRGEVEGYVVWPPRGTSGFGYDPVFQPKGYDTTFGEMSAEEKHGWKPGDSEALSHRARAFKLFAETCLGA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 23109
Sequence Length: 214
EC: 3.6.1.66
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O49326 | MVQKVEARGGEIGDVWDDGAYDGVRKVYVGQGEDGIAFVKFEYVNGSQEVVGDERGKKTLLGAEEFEVDPDDYIVYVEGYHEKVFGVTTKEIISTLTFKTYKGKTSPPFGIVSGTKFVLQGGKIVGFHGRSTDVLHSLGAYISSPATPKLRGKWIKVEQKGEGPGPRCSHDIAQVGNKIFSFGGELTPNQPIDKHLYVFDLETRTWSISPATGDVPNLSCLGVRMVSIGSSLYVFGGRDASRKYNGFYSFDTTKNEWKLLTPVEQGPTPRSFHSMTADENNVYVFGGVSATVRLKTLDAYNIVDHKWVQCSTPGGSCSVRGGAGLEVVQGKVWVVYGFNGCEVDDVHCYDPAQDKWTQVETFGEKPCARSVFASAVVGKHILVFGGEIAMDPKAHEGPGQLSGGTFALDTETLKWEKLDKLGEEEETPSIRGWSASTTGTIDGKKGLVMFGGKAQTNDRFGDLFFYGVDSA | Function: Specifier protein responsible for constitutive and herbivore-induced simple nitrile formation, especially in seeds . Promotes simple nitriles, but not epithionitrile or thiocyanate formation . Converts allylglucosinolate (allyl-GSL), 2-propenylglucosinolate (sinigrin), indol-3-ylmethylglucosinolate (glucobrassicin), benzylisothiocyanate and benzylglucosinolate (glucotropaeolin) to their corresponding simple nitriles in the presence of myrosinase . Catalyzes mainly the conversion of benzylisothiocyanate when benzylglucosinolate is used as the initial substrate of myrosinase . Involved in the regulation of glucosinolate content in seeds, during stratification and germination .
Catalytic Activity: a (Z)-N-(sulfonatooxy)alkanimidothioate = a nitrile + sulfate + sulfur
Sequence Mass (Da): 51215
Sequence Length: 471
EC: 4.8.1.5
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F4KIX0 | MAERRICLSKEAKDGLEFLKRKKLQKMRSDSVNETVGFSTMARSGGDALRPTSASCGMRLRVTSSDTVSKVHGASTVRGGLMKEKVEKLETDDLKWTERLPECPVYRPTKEEFEDPLTYLQKIFPEASKYGICKIVSPLTATVPAGAVLMKEKSNFKFTTRVQPLRLAEWDSDDKVTFFMSGRTYTFRDYEKMANKVFARRYCSGGSLPDSFLEKEFWKEIACGKTETVEYACDVDGSAFSSAPGDPLGSSKWNLNKVSRLPKSTLRLLETSIPGVTEPMLYIGMLFSMFAWHVEDHYLYSINYQHCGASKTWYGIPGSAALKFEKVVKECVYNDDILSTNGEDGAFDVLLGKTTIFPPKTLLDHNVPVYKAVQKPGEFVVTFPRAYHAGFSHGFNCGEAVNFAMGDWFPFGAIASCRYAHLNRVPLLPHEELICKEAMLLNSSSKSENLDLTPTELSGQRSIKTAFVHLIRFLHLARWSLMKSGLCTGLVSNTYGTIVCSLCKRDCYLAFINCECYSHPVCLRHDVKKLDLPCGTTHTLYLRDNIEDMEAAAMKFEKEDGVSDLITTDEDLYKYPSSITLPAAKEDGYTPYSTIYFDFYTEVEMTSHDQLQSGNPVMSYEANASCISSVADDYECSDYVNRRANCSSSSDSKLSEEVACSSSKKTRFFPVVQDEQLVADQESDGSDSECFRVKRRSSLKFENRTVVLDTRESDHHQELKRLKKSHHHEGRYSSSSSVSRQEEEEDELVISNRKETQQQSDVKMQKKRIENHFGGFKRLKVKGLIKP | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that demethylates 'Lys-27' (H3K27me) of histone H3 with a specific activity for H3K27me3 and involved in the regulation of gene expression . Acts as a temperature and photoperiod dependent flowering repressor .
Catalytic Activity: 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] + succinate
Sequence Mass (Da): 88821
Sequence Length: 787
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q8GUI6 | MDQLASLAESVAMEEDSEKQSIKGESSLEPDSTPSSPKITARWNPSEACRPLVDDAPIFYPTNEDFDDPLGYIEKLRSKAESYGICRIVPPVAWRPPCPLKEKKIWENSKFPTRIQFIDLLQNREPIKKSTKTKKRKRRRISKIGYTRRKRDSGCDTASSGSSDSEGKFGFQTGPDFTLEEFQKYDEYFKECYFQSEDHPGSKASENKKFKPKVKDLEGEYWRIVEQATDEVEVYYGADLETKKFGSGFPKYKPGYPISEADQYSQCGWNLNNLSRLPGSVLAFESCDISGVIVPWLYVGMCFSTFCWHVEDHHLYSMNYLHTGDPKVWYGIPGNHAESFENVMKKRLPDLFEEQPDLLHQLVTQLSPRILKEEGVPVYRAVQRSGEFILTFPKAYHSGFNCGFNCAEAVNVAPVDWLVHGQNAVEGYSKQRRKSSLSHDKLLLGAAMEATYCLWELSLSKKKTPVIARWKRVCSEDGLLTKAVKKRVQMEEERLNHLQDGFSLRKMEGDFDNKRERECFLCFYDLHMSASSCKCSPNRFACLIHAKDLCSCESKDRYILIRHTLDELWALVRALEGDLDAIDLWASKCRDQYPSQHPRAREYAYLKSAPCIKSRGSSKVQQREQNNLQLVSERLQSDLTSNKEVQLKQDGDSDVNRHGHESERNHVHGITDKSAVTDVKLGVGGKFDEKKISVESQNPHSVSDVGCSELAKKVDGCLGGKDQNAATNRLSLSVELLSSGSLVVKKLWCSKQAIYPKGFKSRVKFLSVLDPTNLTNYISEVLDAGLLGPLFRVSVEDYPTENFSNVSAEKCWQMVTQRLKLEIIKKCDQPVSSLTSLQPLESINGLEMFGFLSPHVIKVVEALDPKHQLEEYWNQKAVKLFGAEPIKEGEKDDTEKGGASDPSLDRDTRLLRGLLKKATPEELVMMHGLLCGETRNTELKEELSTLVDKMEISP | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Transcriptional repressor . Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a higher activity for H3K4me3 and H3K4me2 than H3K4me1 . No activity on H3K9me3/2, H3K36me3/2 and H3K27me3/2 . Function as a nocturne 'eraser' to counteract the diurnal 'writer' methylase activity of ATXR3/SDG2 thus orchestrating the circadian rythm of histone modifications (e.g. H3K4me3) and modulating the rythmic expression of diurnal target genes; this mechanism relies also on the circadian clock oscillators CCA1 and LHY . Involved in a negative regulation of root meristem growth upon suboptimal root growth conditions . Represses FT and TSF expression to inhibit the floral transition. Binds around the transcription start site of the FT locus. Involved in the DRM2-mediated maintenance of DNA methylation, but not required for the de novo DNA methylation. Required for demethylating histone H3K4me3 at the target of RNA silencing. Counteracts the DNA methylation of expressed transgenes; specific attenuation of transgene DNA methylation enhances the production of aberrant RNAs (e.g. uncapped and antisense) that readily induce systemic RDR6-dependent post-transcriptional transgene silencing (PTGS) spreading . Together with NAC051/NAC052 and NAC050, regulates gene expression and flowering time, probably by the promotion of RNA-mediated gene silencing . Together with JMJ16 and JMJ17, required for plant growth and development . Promotes local and systemic immunity (especially toward the bacterial pathogen Pseudomonas syringae Pst DC3000 avrRpt2) by regulating positively pathogen-induced H3K4me3 enrichment and expression of defense genes involved in salicylic acid (SA)- and pipecolic acid (Pip)-mediated defense pathways (e.g. PR1, FMO1, ALD1 and SARD4) .
Catalytic Activity: 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + succinate
Sequence Mass (Da): 108156
Sequence Length: 954
Subcellular Location: Nucleus
EC: 1.14.11.67
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O64752 | MEPFSAAQNKEDKDTSVEPPRRRCHRKNKGTNVEPPSSPYHPKVLARWDPANEKRPDIGEAPVFHPTSEEFEDTLAYIEKIRPLAESFGICRIVPPSNWSPPCRLKGDSIWKNKNFPTRVQFVDLLQNRGPVKKKTPKGRKRKRGKYSRTVAPKKRNGSVSKSVSTPKATEEENFGFESGPEFTLEKFEKYAQDFKDSYFERKDNVGDPSVEEIEGEYWRIIEKETNEVKVLYGTDLENPILGSGFSKGVKIPTRRNDMDKYISSGWNLNNLARLQGSLLSFEDCEISGVQVPWLYVGMCFSTFCWHVEDNHLYSLNYHHFGEPKVWYGVPGSHATGLEKAMRKHLPDLFDEQPDLLHELVTQFSPTILKNEGVPVYRAVQNAGEYVLTFPRAYHSGFNCGFNCAEAVNVAPVDWLAHGQNAVEIYSQETRKTSLSHDKILLGAAFEAVKSLSAHGEDNTKRFSWKRFCGKDGIITKAIEARLRMEEKRIEALGNGFSLVKMDKDFDSNCERECISCFSDLHLSATGCKNCSSLEEYGCTKHDICSCEGKDRFIFLRYTIDELSSLVRALEGESDDLKAWLSKVMEGCSETQKGESSGIIVKEKQVQEECFDLNGECNKSSEICEDASIMDLAAYHVEPINLGFLVVGKLWCNKHAIFPKGFKSRVKFYNVQDPMRISYYVSEIVDAGLLGPLFKVTLEESQDESFSYASPQKCWEMVLLRVKEEIMRRSNQKQDVHMLESIDGLKMFGFRSPFIVQATEALDPNHGQVEYWNHKNEKDSLEMKDCFMSNSSQSLSKARLFGVDLN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3 . No activity on H3K4me2, H3K4me1, H3K9me3/2, H3K27me3/2 and H3K36me3/2 . Involved in the control of flowering time by demethylating H3K4me3 at the FLC locus and repressing its expression . The repression of FLC level and reduction in H3K4me3 at the FLC locus results in induction of the flowering activator FT, which is a downstream target of FLC . Promotes salt tolerance by down-regulating the expression of several transcriptions factors involved in stress responses via H3K4me3 and H3K4me2 demethylation .
Catalytic Activity: 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + succinate
Sequence Mass (Da): 91718
Sequence Length: 806
Subcellular Location: Nucleus
EC: 1.14.11.-
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F4I6G4 | MENPPLESEIKEDMSLKNHPPDKDKDKDTIMEQPSSPRHRKVVARWLPDEAQRPIINDAPVFTPSLEEFVDPLAYIEKIRPLAEPYGICRIIPPSTWKPPCRLKEKSIWEQTKFPTRIQTVDLLQNREPMKKKPKSRKRKRRRNSRMGSSKRRSGSSPAESTSSPEAEEKFGFNSGSDFTLDEFEKYALHFKDSYFEKKDSGGDIVKWTPSVDDIEGEYWRIVEQPTDEVEVYYGADLENGVLGSGFYKRAEKFTGSDMEQYTLSGWNLNNLPRLPGSVLSFEDCDISGVLVPWLYVGMCFSSFCWHVEDHHLYSLNYHHFGEPKVWYGVPGSNATALEKAMRKHLPDLFEEQPDLLHGLVTQFSPSILKDEGVQAYRVVQNSGEYVLTFPRAYHAGFNCGFNCAEAVNVAPVDWLAHGQNAVELYSKETRKTSLSHDKLLLGAAYEAVKALWELSASEGKENTTNLRWKSFCGKNGTLTNAIQARLQMEEGRITALGRDSSSLKKMEKDFDSNCERECFSCFYDLHLSASGCKCSPEEYACLKHADDLCSCDVKDGFILLRYTMDELSSLVRALEGESDDLKIWASKVLGIEHSDEDQTKTSSVISEEKKLKEGSFDLNIDLEMDYQEDVKEEASTSGGELTASENLGVSVEPINLGFLIFGKLWCNKYAIFPKGFRSRVKFYNVLDPTRMSNYISEVLDAGLMGPLFRVTLEESPDESFFNVSAQQCWEMVMRRVKDTSTSLGLPILPQFESINGLQMFGFLSPSIVQAIEALDPNHRLVEYWNHKNQTSSDSKDHFISSNCSASLTKGKLFGVDLM | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3 and H3K4me2. No activity on H3K9me3/2, H3K27me3/2 and H3K36me3/2. Involved in the control of flowering time by demethylating H3K4me3 at the FLC locus and repressing its expression. The repression of FLC level and reduction in H3K4me3 at the FLC locus results in induction of the flowering activator FT, which is a downstream target of FLC.
Catalytic Activity: 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + succinate
Sequence Mass (Da): 92809
Sequence Length: 819
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q67ZB6 | MGIQIIGQIERINGKELSYGDFAERYLAKNQPVVISDLTEDWRAREDWVSENGNPNLHVFATHFGKSRVQVADCDTREFTDQKRLEMSVTEFVEQWTNKDSIEESVLYLKDWHFVKEYPDYTAYQTPPLFSDDWLNVYLDNYQMHEDRDSFQKYDQISCSDYRFVYMGGKGSWTPLHADVFRSYSWSANVCGKKRWLFLPPPQSHLVYDRYMKNCVYDIFEEVNETKFPGFKKTTWLECIQEPGEIIFVPSGWHHQVYNLEDTISINHNWLNAYNLSWVWDLLWKDYKDTEESIEDIRDICDDFEAICQRNLAANTGMNLNDFFLFMSRFSLGNMVLLQSYSDKHKNLNSCSLAMAQNLLMNLSTILKVMMKMISAGGVTAEEVYLDLRETLEDPQFLRFVRDMGRTYARIHMEEEDQFLSSKELLQKLSGLAGPNMQICSPKDLVEMINHHNTFSSQIYFI | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that demethylates 'Arg-3' (H4R3me) of histone H4 with a specific activity for H4R3me2 . Involved in the positive regulation of gene expression . Together with JMJ22, regulates positively seed germination by promoting the removal of repressive histone arginine methylations (e.g. H4R3me2) at GA3ox1 and GA3ox2 to trigger gibberellic acid (GA) biosynthesis .
Catalytic Activity: 2-oxoglutarate + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + O2 = CO2 + formaldehyde + N(omega)-methyl-L-arginyl-[protein] + succinate
Sequence Mass (Da): 54358
Sequence Length: 462
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q9M9E8 | MTTLGQRDRRPDALGSLSVLPDETICVLLEYLAPRDIAHLACVSSVMYILCNEEPLWMSLCLRRAKGPLEYKGSWKKTTLHLEGVTQENDAYRKCFHFDGFMSLYLYKRFYRCNTSLDGFSFDNGNVERRRNISLDEFSKEYDAKKPVLLSGLADSWPASNTWTIDQLSEKYGEVPFRISQRSPNKISMKFKDYIAYMKTQRDEDPLYVFDDKFGEAAPELLKDYSVPHLFQEDWFEILDKESRPPYRWLIVGPERSGASWHVDPALTSAWNTLLCGRKRWALYPPGKVPLGVTVHVNEDDGDVSIDTPSSLQWWLDYYPLLADEDKPIECTLLPGETIYVPSGWWHCILNLEPTVAVTQNFVNKENFGFVCLDMAPGYHHKGVCRAGLLALDDENSEDLEEETHDEEDNTLSYSDLTRKEKRTRMNGGGETENREEDVNGVSKRYNMWKNGFSYDIDFLASFLDKERDHYNFPWSMGNSVGQREMRAWLSKLWVLKPEMRELIWKGACIALNAEKWLRCLEEVCTFHNLPLVTEDEKLPVGTGSNPVYLLSDYAIKLFVEGGLEQSMYGLGTELEFYDILGRADSPLKTHIPEVLASGILFFEKGSYKVVPWDGKRIPDIISSSSFDFDASMLNSEFPFGIWNKTLREHKNQGKPAPDSFGSLSSHVWPYIITKRCKGKIFAQLRDDLTWNDAQNLAFFLGQQLRNLHLLPYPPVTRPELLNVNAVHEELNIPAEWKVFVDALCQKKKDVTSRLENWGNPIPRALMTKIDEYIPDDFFVDLLHVFKETNGGDEIKPCTWIHSDVMDDNIHMEPYADDSVDGQHNSWRPSHILDFSDLTIGDPICDLIPIYLDVFRGDADLLKKLLENYGLPLIRSRSSENGTTKTADSTRKKVLSPSYRTMCYCILHEENVLGSIFSIWDELRTAESWEQVEQTVWSLLNTY | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: May function as histone H3 lysine demethylase and be involved in regulation of gene expression.
Sequence Mass (Da): 108505
Sequence Length: 943
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q67XX3 | MPKCKNLLLTSKRRKSKSKRLKLHQHEPESLFPEKEVEEEDEDEGGFKLKIAAPSQEHGVQPLGNLYFNPGAVNVRNTGLGNLQILSDELVLDILGLLGANHLGVLATVTKSFYIFANHEPLWRNLVLEELKGDFLFNGSWRSTYVAAYHPKFKFAGDGESNLKIIDFYSDYLFQSWLCANLEMKPKWLRRDNITRVRGISVEDFITKFEEPNKPVLLEGCLDGWPAIEKWSRDYLTKVVGDVEFAVGPVEMKLEKYFRYSDGAREERPLYLFDPKFAEKVPVLDSEYDVPVYFREDLFGVLGNERPDYRWIIIGPAGSGSSFHIDPNSTSAWNAVITGSKKWVLFPPDVVPPGVHPSPDGAEVACPVSIIEWFMNFYDDTKDWEKKPIECICKAGEVMFVPNGWWHLVINLEESIAITQNYASRSNLLNVLEFLKKPNAKELVSGTTDRENLHDKFKKAIEEAYPGTIQELEKKAEEAKRAEEQRVSFWDSAKTDTFKFSF | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that demethylates 'Arg-3' (H4R3me) of histone H4 with a specific activity for H4R3me2 . Involved in the positive regulation of gene expression . Together with JMJ20, regulates positively seed germination by promoting the removal of repressive histone arginine methylations (e.g. H4R3me2) at GA3ox1 and GA3ox2 to trigger gibberellic acid (GA) biosynthesis .
Catalytic Activity: 2-oxoglutarate + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + O2 = CO2 + formaldehyde + N(omega)-methyl-L-arginyl-[protein] + succinate
Sequence Mass (Da): 57419
Sequence Length: 502
Subcellular Location: Nucleus
EC: 1.14.11.-
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F4HZD1 | MQVNFDETCDSVIRMNANEQTRSANGIGNGNGESIPGIPDDLRCKRSDGKQWRCTAMSMADKTVCEKHYIQAKKRAANSAFRANQKKAKRRSSLGETDTYSEGKMDDFELPVTSIDHYNNGLASASKSNGRLEKRHNKSLMRYSPETPMMRSFSPRVAVDLNDDLGRDVVMFEEGYRSYRTPPSVAVMDPTRNRSHQSTSPMEYSAASTDVSAESLGEICHQCQRKDRERIISCLKCNQRAFCHNCLSARYSEISLEEVEKVCPACRGLCDCKSCLRSDNTIKVRIREIPVLDKLQYLYRLLSAVLPVIKQIHLEQCMEVELEKRLREVEIDLVRARLKADEQMCCNVCRIPVVDYYRHCPNCSYDLCLRCCQDLREESSVTISGTNQNVQDRKGAPKLKLNFSYKFPEWEANGDGSIPCPPKEYGGCGSHSLNLARIFKMNWVAKLVKNAEEIVSGCKLSDLLNPDMCDSRFCKFAEREESGDNYVYSPSLETIKTDGVAKFEQQWAEGRLVTVKMVLDDSSCSRWDPETIWRDIDELSDEKLREHDPFLKAINCLDGLEVDVRLGEFTRAYKDGKNQETGLPLLWKLKDWPSPSASEEFIFYQRPEFIRSFPFLEYIHPRLGLLNVAAKLPHYSLQNDSGPKIYVSCGTYQEISAGDSLTGIHYNMRDMVYLLVHTSEETTFERVRKTKPVPEEPDQKMSENESLLSPEQKLRDGELHDLSLGEASMEKNEPELALTVNPENLTENGDNMESSCTSSCAGGAQWDVFRRQDVPKLSGYLQRTFQKPDNIQTDFVSRPLYEGLFLNEHHKRQLRDEFGVEPWTFEQHRGEAIFIPAGCPFQITNLQSNIQVALDFLCPESVGESARLAEEIRCLPNDHEAKLQILEIGKISLYAASSAIKEVQKLVLDPKFGAELGFEDSNLTKAVSHNLDEATKRPQQNSCT | Function: Binds histone H3 but seems to have lost demethylase activity probably due to its inability to bind iron Fe(2+) . Possesses E3 ubiquitin ligase activity and targets directly CMT3 for proteasomal degradation to initiate destabilization of the heterochromatic state (e.g. CHG cytosine methylation and H3K9me2) of endogenous silenced loci . Required for the removal of repressive H3K9me2 histone marks to facilitate the transcription of AtSN1, AtMu1c, solo LTR and SDC, thus counteracting their transcriptional silencing . Mainly required to promote the basal level transcription of silenced loci such as TE and repeats targeted by RNA-dependent DNA methylation (RdDM) for silencing, a specialized branch of the RNA interference (RNAi) pathway . Cooperates also with RNAi pathways for gene silencing both by contributing to the production of 24-nt siRNA to initiate RdDM and by recruiting RDR2 to enable local transcripts to make dsRNA . Antagonizes histone H3K9 demethylase IBM1/JMJ25 function .
PTM: Self-ubiquitinates.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 107230
Sequence Length: 944
Domain: The RING-type domain is necessary for E3 ubiquitin ligase activity.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q8VYB9 | MEKMRGKRIRPRDSGELVEDGRSESERKTRKKENDVVSKGRIGRGRGRGEVSKRSIEIDISNPEKDIKPDGSRKCLGSTCHHCKILTSESDLIFCSKCNKKCYCFDCIKRSYSERTHEEVRAACPFCMMTCICRACLRLPLVIKPPSEKDTDVKLKQLQYLLVKVLPVLKDIYTEQNRELEIESTIRGHPVTEANIKRCKLDPSERIYCDLCRTSIANFHRSCPNKNCSVDICLSCCKELSEGFHQERDGKKNAEGKGYECRIPAGQGKDSDAYVPLHFSTWKLNSDSSIPCPPKECGGCGTSTLELRRLWKRDWVEKLITNAEKCTLNFRPTDVDIVHECSSCSTNSDSIRRQAAFRKNAHDNFLYSPNAVDLAEDDIAHFQFHWMKAEPVIVRNVLEKTSGLSWEPMVMWRACREMDPKRKGTEEETTKVKALDCLDWCEVEINLHQFFEGYLEGRMHKNGWPEMLKLKDWPPSDLFEKRLPRHNAEFIAALPFFDYTDPKSGILNLATRFPEGSLKPDLGPKTYIAYGFHEELNRGDSVTKLHCDISDAVNVLTHTAKVEIPPVKYQNIKVHQKKYAEAMLQKQQYSGQVKEASELENKSMKEVDESKKDLKDKAANEEQSNNSSRPSGSGEAEKVIISKEDNPTQPAVSTSVESIQEQKLDAPKETDGNTNERSKAVHGGAVWDIFRREDVPKLIQFLKRHEHEFRHFNNEPLESVIHPIHDQTMFLSDSQKKQLKEEFDIEPWTFEQHLGEAVFIPAGCPHQVRNRQSCIKVALDFVAPESVEECLRLTQEFRRLPKDHSSSEDKLELKKIALYAASSAIREVKGLMQSSRRSDT | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that demethylates 'Lys-9' (H3K9me) of histone H3 with a specific activity for H3K9me1 and H3K9me2 . No activity on H3K4, H3K27, H3K36, H3R2 and H4R3 methyl marks, but weak activity on H3K9me3 . Involved in regulation of gene expression . Regulates flowering time by repressing the major flowering regulator CONSTANS (CO) and promoting FLOWERING LOCUS C (FLC) . Exhibits a positive impact on abscisic acid- (ABA), hydrogen peroxide- (H(2)O(2)) and calcium- (Ca(2+)) induced stomatal closure . Promotes stomatal-closure-dependent drought-stress responses through its histone demethylase activity toward at least GOLS2 and RD20 loci, thus protecting them from silencing by removing H3K9me2 marks in drought conditions . Required for plant defenses leading to resistance against the virulent bacterial pathogen Pseudomonas syringae pv. tomato DC3000 (Pst DC3000) via a negative regulation of WRKY25 (a repressor of defense) and by triggering the expression of several pathogenesis-related (PR) proteins (e.g. PR1, PR3, PR4 and PR5) .
Catalytic Activity: 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + succinate
Sequence Mass (Da): 96105
Sequence Length: 840
Subcellular Location: Nucleus
EC: 1.14.11.65
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Q8H1S7 | MSENEIVPDEFRCNRSDGKQWRCKRRALEGKKMCESHHSQQSLKRSKQKVAESSKLVRSRRGGGDEVASSEIEPNESRIRSKRLGKSKRKRVMGEAEAMDEAVKKMKLKRGDLQLDLIRMVLKREVEKRKRLPNSNNKKKSNGGFSEFVGEELTRVLPNGIMAISPPSPTTSNVSSPCDVKVGEEPISMIKRRFRSKNIEPLPIGKMQVVPFKGDLVNGRKEKKMRCHWCGTRGFGDLISCLSCEREFFCIDCIEKRNKGSKEEVEKKCPVCRGSCRCKVCSVTNSGVTECKDSQSVRSDIDRVLHLHYAVCMLLPVLKEINAEHKVEVENDAEKKEGNPAEPQIHSSELTSDDRQPCSNGRDFAVVDLQRMCTRSSSVLRLNSDQDQSQESLSRKVGSVKCSNGIKSPKVCKRKEVKGCSNNLFLSLFPLELTSKLEISAEEVVSCYELPEILDKYSGCPFCIGMETQSSSSDSHLKEASKTREDGTGNFLYYPTVLDFHQNNLEHFQTHWSKGHPVIVRSVIKSGSSLNWDPVALFCHYLMNRNNKTGNTTDCMDWFEVEIGVKQFFLGSLRGKAETNTCQERLKLEGWLSSSLFKEQFPNHYAEILNILPISHYMDPKRGLLNIAANLPDTVQPPDFGPCLNISYRSGEEYAQPDSVKKLGFETCDMVDILLYVTETPVSTNQICRIRKLMKNIGRVRSKNPAKGRESRFDKGKKRDRLDDYSSSDSESSQHCLGAKCRGSEFEGEERESCNYSCEEESLSNTYGAQWDVFQKQDVSKLLEYIKNHSLELESMDSSKKKVSHPLLEQSYYLDEYHKARLKEEFDVEPWSFDQCVGEAVILPAGCPYQIRKNKSCVNAVLKFLSPEHVSESIKRVKELNQLPQSVKSKANKIEVKKMAIHKISEAVKEIRELTSSDSTGALRLYN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: May function as histone H3 lysine demethylase and be involved in regulation of gene expression (By similarity). Regulates flowering time by promoting CONSTANS (CO) and CONSTANS-LIKE genes (e.g. COL2 and COL5) expression via interaction with FBH transcription factors (FBH1, FBH2, FBH3 and FBH4) at their loci to remove H3K9me2 repressive histone marks . Modulates also the expression of several develpmental genes such as MYB30, TFS1, AGL6 and RVE2 .
Sequence Mass (Da): 105143
Sequence Length: 927
Subcellular Location: Nucleus
EC: 1.14.11.-
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C0SV12 | MDSGVKLEHMNCFQLSYQYSWTTRKKRTLKPFMSKGSSPSSSSDSRKRKLSRAEDSDDSAVKRNAKRRRKICKVEEYYEDDDCILSDWVQRNTAKRIDKRNEEVEVMVKIESGDDCTIGKWFSDVSSKRKDKRQVEVDEDEEWEEEVTLCSKIKATSSRSRTHSLSANSPENVTDVISPCRSRSPASNVSDSIQKNDCTSSRKQSGPICHQCLKGERITLLICSECEKTMFCLQCIRKWYPNLSEDDVVEKCPLCRQNCNCSKCLHLNGLIETSKRELAKSERRHHLQYLITLMLPFLNKLSIFQKLEIEFEATVQGKLPSEVEITAAISYTDERVYCDHCATSIVDLHRSCPKCSYELCLKCCQEIREGSLSERPEMKFHYVDRGHRYMHGLDAAEPSLSSTFEDEEANPSDAKWSLGENGSITCAPEKLGGCGERMLELRRILPLTWMSDLEHKAETFLSSYNISPRMLNCRCSSLETELTRKSASRTTSSDNYLFCPESLGVLKEEELLHFQEHWAKGEPVIVRNALDNTPGLSWEPMVMWRALCENVNSTSSSEMSQVKAIDCLANCEVEINTRQFFEGYSKGRTYENFWPEMLKLKDWPPSDKFEDLLPRHCDEFISALPFQEYSDPRTGILNIATKLPEGFIKPDLGPKTYIAYGIPDELGRGDSVTKLHCDMSDAVNILTHTAEVTLSQEQISSVKALKQKHKLQNKVDKQSTEDCNEKEEEEEEELNMPEISSNENEETGSALWDIFRREDVPKLEEYLRKHCKEFRHTYCSPVTKVYHPIHDQSCYLTLEHKRKLKAEYGIEPWTFVQKLGEAVFIPAGCPHQVRNLKSCTKVAVDFVSPENIHECLRLTEEFRQLPKNHKAREDKLEASLLSL | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: May function as histone H3 lysine demethylase and be involved in regulation of gene expression.
Sequence Mass (Da): 101477
Sequence Length: 883
Subcellular Location: Nucleus
EC: 1.14.11.-
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R4GUQ3 | MNFWVTFIRLIVVLSIVFAFQIAVAKAACVTHEDCTLLCYDTIGTCVDGKCKCM | Function: Selectively inhibits Kv7.1/KCNQ1 channel (Kd=11.69 uM) and inhibits Kv1.1/KCNA1, Kv1.2/KCNA2, Kv1.3/KCNA3 with a very low potency.
Sequence Mass (Da): 6006
Sequence Length: 54
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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D9U2A6 | MKSVCGVLIILVVLTTMLSISTFSTVGAEGDCPISEAIKCVEKCKEKVEVCEPGVCKCSG | Function: Weakly inhibits the Kv1.3/KCNA3 channel (1 uM of the toxin inhibits currents by 13.2%) and Kv7.1/KCNQ1 channel (10 uM of the toxin inhibits currents by 27.7%).
Sequence Mass (Da): 6268
Sequence Length: 60
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0DL33 | MNTGFFFFVIMATGLVLTFDTIHAEDKLKCTKTDDCAKYCSQFTDVHPACLGGYCECLRWEGGISS | Function: inhibits Kv1.3/KCNA3 channel (1 uM of the toxin inhibits currents by 64.1%).
Sequence Mass (Da): 7338
Sequence Length: 66
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0DL62 | AGSMDSCSETGVCMKACSERIRQVENDNKCPAGECICTT | Function: Voltage-gated potassium channel inhibitor. 1 uM of the native toxin inhibits rat Kv1.2/KCNA2 (100% inhibition), and drosophila Shaker IR/Sh (100%), human Kv1.3/KCNA3 (83%), rat Kv1.1/KCNA1 (32%) and rat Kv1.6/KCNA6 (21%).
Sequence Mass (Da): 4129
Sequence Length: 39
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P85130 | GSLCGDTCFVLGCNDSSCSCNYPICVKD | Function: Probably participates in a plant defense mechanism.
PTM: This is a cyclic peptide.
Sequence Mass (Da): 2904
Sequence Length: 28
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
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P56254 | MAKFTVCLLLCLLLAAFVGAFGSELSDSHKTTLVNEIAEKMLQRKILDGVEATLVTDVAEKMFLRKMKAEAKTSETADQVFLKQLQLKGLPVCGETCVGGTCNTPGCTCSWPVCTRNGLPSLAA | Function: Probably participates in a plant defense mechanism. Has antibiotic activity. Has a diuretic effect. Has a uterotonic effect in humans. Active against the Gram-positive S.aureus with a minimum inhibition concentration of approximately 0.2 microM. Relatively ineffective against Gram-negative bacteria such as E.coli and P.aeruginosa. Inhibitory effect on the growth and development of larvae from H.punctigera. The unmodified form has hemolytic activity, the oxidized form lacks hemolytic activity. If the protein is linearized, hemolytic activity is lost.
PTM: Kalata-B1 is a cyclic peptide which occurs in three forms: with unmodified Trp-111, with Trp-111 oxidized to form oxindolylalanine and with Trp-111 oxidized to form N-formylkynurenine. Oxidation is enhanced by exposure to sunlight.
Sequence Mass (Da): 13271
Sequence Length: 124
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
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Q8TWH4 | MKIAITGTPGVGKTTVCEALRDLGFDVVHLNKVAREMDAILEEDEQRQAKVVDLHALRRYVEEWEPESDPAFVESHYAHLMPTDLVIVLRLHPSELERRLKEKGYPPEKIAENLEAEFVGVCYGEAVEVRSEGCFIRPPEDVIQVNVTGLSRAEAADRVLEAVNHRRGDDVDWLSDEEAQRTVERYLKYR | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21695
Sequence Length: 190
EC: 2.7.4.3
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Q8PZ69 | MLIGLTGTPGTGKTSVSKLLEKRRGWKVVYLNDLIKEEHLYSEVDEERDSVIADMELIRERLSGILEEEKGQHAEKAKVNGEEKENITIIESHLAHYITDIVIVLRAYPPELKKRLEKRGYSEEKINENAEAESIDLILAEAFEWCKKVFEVNTTGRTAEETLGDVEKIIDYILAGKENELQEYIPGSLDWIDSVP | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22343
Sequence Length: 196
EC: 2.7.4.3
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O27656 | MICITGTPGVGKTTLAGILRERGLEVISLGELIRQKGFVLGRDPIRGYLEADIEAACSHLQEMEGLDVVEGHLSHLCRSCSMVIVLRLHPEVLRGRLEGRGYPEGKVLENLEAEALDVCTVEAFEIHGERVHEVDTTGRSPHEVADIITDIMNGSRVCPPGGVDFSGWLLG | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 18565
Sequence Length: 171
EC: 2.7.4.3
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Q3IRT0 | MRVAVTGTPGTGKTTATEAVETALDVIHLNERIREEGLDAGRDEERDSLVADLDAVEAALAGEDDALIESHLAHHVDADRVVVLRCRPDILQERLVDRGEPAAKAAENAEAEALDVVLSEAVAEHGRESVYEIDTTEASPSAVAEAIEAVIDGERAPAVGTVDFTEHL | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 17825
Sequence Length: 168
EC: 2.7.4.3
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Q8I236 | MKRKVPNIIITGVPGSGKSTLCEELKEIINKELLKRNDMEGFEMTHLNLSNIIKDERLYKEFDDELDASIYSEELLNEYLKKKYKLEKGGYIIDFHDINFVKDVDIIDKIFLLTIQTNFLYERLEKRNYTKEKIKNNIECEIFQVIKEDILDHFPNTNILQEIENNDLQQYDNNLSIIKNWVLSYI | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22173
Sequence Length: 186
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q9UZK4 | MLIAITGTPGVGKTTIAKLLAEKLGYEYVNLRDFALEKGCGREVDGEVEVEIDELAYFVEKELKDRNVVLDGHLSHLMPVDLVVVLRAHPRIIGERLRERGYSKEKIGENVEAELVDAILIEAIDEHENVIEVDTTNKTPEEIVEEIIGLIKSGVKRRVGIVDWSEVYDEIIPYLRLGGE | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20205
Sequence Length: 180
EC: 2.7.4.3
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Q8ZU30 | MFDARRPKALITGTPGVGKTTHCRKLAAFLNTKCISVGELLAGTPYVTYIPELDTYEIVDLDGAVKRVHSVVEPGHIIDTHVVELVPDPEVVIVLRKAPDVLFAELKRRGWPLKKILDNVWAEILDVVLIKARERWGEVAQIDVTRRRPEETFELLKKCVAGGRCHSDVVDWLGYSEESGFLEFIERLSRSESF | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21893
Sequence Length: 194
EC: 2.7.4.3
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Q9TTU2 | MRLPNILLTGTPGVGKTTLGKELASRSGLKYVNVGDLAREGELYDGFDEEYNCPILDEDRVIDELDTQMRDGGVIVDYHGCDFFPERWFHIVFVLRTETSVLYKRLETRGYSEKKLNDNIQCEIFQVLYEEAMESYKEEIVHQLPSNKPEELEENISQILKWIEQWIKDHNS | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. May have a role in nuclear energy homeostasis. Has also ATPase activity. May be involved in regulation of Cajal body (CB) formation.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20079
Sequence Length: 172
Subcellular Location: Nucleus
EC: 2.7.4.3
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Q97ZW3 | MIIIVTGTPGVGKTVASKKLSEALNLNYLSLSQFVIENKLYTEYDELRQSYIIDEDKVKEELEKIISTSHLVIETIYPSLVSTADLVVVLRKNPFSLYNELKGRGWADIKVAENVEAEILGVISQEAREAFKDKVCEVDTTEMSTEQILNKILNKQCDGPIEWLVDTKVQRFLEELDKIISSYENDI | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21247
Sequence Length: 187
EC: 2.7.4.3
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Q9UU88 | MGNEERELPNIIICGTPGTGKTTLAEQVAETTELENICIGDVVKENHLHFGFDEKWKTYDVDEDKVLDYLEPKLLKGGCIIDWHTCGLFSEELIDLVVVLRTDHSKLWERLESRGYSLEKIQENNEAEIMQICLEEARESFDPKIVVELPSESIEEMESNLSRITQWVTNWKKNH | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity. May be involved in rRNA maturation and transcription regulation.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20222
Sequence Length: 175
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q09629 | MYRVLLSGAAGSGKGTIARMLVREFEPLGFNYFAAGDFIRDHIARGTEFGVRAQSFLNKGEHVPDSILNGAILAEMLKAGPRVVLDGYPRNMSQLKMVEEQAPLNLIVELKVPRKVLIDRLSKQLVHPASGRAYNLEVNPPKEEGKDDITGEPLFKRSTDQLEVARRRLEVYDKTENKVLDYYKKQNKCITMSGESSKAVFESVAEVMRRDLLTTTPRTAYA | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24904
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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A9NEF4 | MKTRMIFVGPPGAGKGSQAKIISQTLNIPHISTGDMFRTHIKGSTPLGLEAKKYTDQGLLVPDDVTNQMVKDRLSQKDVEKGFIFDGYPRTPDQAIFLDNLLMVTNQKLDVVLNISSSDEVIVKRITGRRTCPVCGAIYHVDNYPPKVAGICDNDGATLVQRKDDQKETIIRRLSVYKEETFPLIKYYAHKNLLMDVDGNQPLEVITKHVLEILEQK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24354
Sequence Length: 217
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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A0LRP1 | MRLVLVGPPGAGKGTQAQLIASHLHVPKISTGDIFRKNVADDTPLGRLAKQYMDAGDLVPDEVTIAMVRDRLAGDDVRDGFLLDGFPRTVHQAVELDAMLAEAGARLDVVLELVVDDDEVIRRLSGRRTCADCAHVWHVTYDPPTVDGVCDLCGGKLFQREDDREETVRHRLEVYYQQTAPLIDYYAARGILEGIDAMGPVEEVTARAVAALRHWSR | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23941
Sequence Length: 217
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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B3R0X7 | MRLILLGAPGAGKGTQAKFICEKFGIPQISTGDMLRAAVKAGTPLGVEAKKVMDAGGLVSDDIIIGLVKDRLKQDDCKSGYLFDGFPRTIPQAEAMKDAGVAIDYVLEIDVPFDAIIERMSGRRVHVASGRTYHLKYNPPKTEGVDDETGEPLIQRDDDKEETVKKRLDVYSQQTRPLVDYYSAWAANGDPAAKVAPPKYRKILGVGNVDEITARVFEALK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24138
Sequence Length: 221
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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B8HMS3 | MARLILFGPPGAGKGTQAKHLVDLLDIPHISTGDIFRAAVRNQTPLGQQVQAYLDSGRLVPDELTINLIQERLHQSDVQKGWILDGFPRTLAQAEALEKLLHQINQPYDRVLSLTVPEEVLTQRLVLRAEKESRKDDTPEVIQKRLGVYWKDTAPLLDFYRNQQRLATIDGNQPESDVTAQIQHIVDQLKGEKIV | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22025
Sequence Length: 195
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q3Z960 | MYNVIFLGAPGSGKGTQGEVVAKELRLAHMATGDLFRKAIERGDELGDTVKSYMERGELVPDEITISVVLKHLAGLKDVSGIILDGFPRSLRQAEALDEALVKQGEGIGRVIYINVPEDELVRRLSGRWVCRSCQSPYQCGCAEVAEGKCSRCQGELYQRPDDTPETVKERLKVYFSKTAPLIEYYRSKGKLSEIDGMAEITEVTKRIVSAIKCGK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23859
Sequence Length: 216
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q9RSK7 | MTQSKNKVVIFLGPPGAGKGTQAARLAQEHQLVQLSTGDILRDHVARGTALGQQAGPLMEAGQLVPDELLIALIRDRLADMEPVRVIFDGFPRTQAQAEALDLLLEELGAPVSAVPLLEVPDQVLIDRIVDRGRQAVAEGRAPRADDNEETARKRQQVYREQTQPLIDYYARRGHLYTVDGLGTPDEVYERILSGMH | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21692
Sequence Length: 197
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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P0A0U7 | MKALLLGAPGAGKGTQAQFITAAFGIPQISTGDMLRAAIKAGTPLGLEAKKIIDEGGLVRDDIIIGMVKERIAQDDCKNGFLFDGFPRTLAQAEAMVEAGVDLDAVVEIDVPDSVIVDRMSGRRVHLASGRTYHVTYNPPKVEGKDDVTGEDLIQRDDDKEETVKKRLAVYHEQTEVLVDFYSKLEGEHAPKYIKVDGTQAVEAVKAEVLGALGK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23190
Sequence Length: 215
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q2GEB9 | MNLVMFGPPGSGKGTQSSRICSYVSASVVDCGKLLRVAALTMRQSEDLKAGKLLPDELVIGVVREKLRELIKVGDNFILDGFPRSVVQCHALFEMSSELEFEISCLVKFEVSEREIFARLLDRLVCSACGALHDVVLGRCVSCGSVECERRSDDLKVEIIKKRLMLYGAVERDIVNLFRSRSIKVLSIDAGRSVDEVAADLRTQLLMFI | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23174
Sequence Length: 209
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q1QN09 | MRLILLGPPGAGKGTQAQRLVHHHGIVQLSTGEMLRAAVAAGTPVGLKAKDVMASGGLVPDDVVIGIISDRLDQSDAKNGFILDGFPRTVPQAEALDRLLKSKNLKLDAVVELCVNESALLQRVESRVAEMTARGEQVRADDTPEVLSKRLASYRALTEPLIHYYSERGKLLTVDGMMPIEQVTRDIYRVLEEAIGASDVQSRGKGAG | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22376
Sequence Length: 208
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q5Z1Q1 | MRVVLLGPPGAGKGTQAVLLSEKLGVPHISTGDLFRANISQQTPLGREAQKYMDAGDLVPSDVTNRMVEARVNEPDAANGFVLDGYPRTVDQADALEKILGDMNSKLDAVLCFVVPEDTVVERMLARGRNDDTEDVIRNRMRVYREETEPLLDHYDGLVVTVDGVGEVDEVNERALRALGR | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 19859
Sequence Length: 181
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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A5CCJ2 | MILVFIGPPGSGKGTQASLLSEKFSIISVGKVLRTVMESNTAEADVVKKFIKSGKLVPSNITNKIVVNALKNIEQCKSIILDGYPRDIFQADFLQENLQMDFKVLFFDIDDAVVLRRLRGRISCTDCGTIYNKLYCMPKINGVCDICNSSSFQNRVDDDESIIKLRLESYKKETLPLLEFYKAQNKLTLIDANQSTENILKKIKKMSGIY | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23647
Sequence Length: 210
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q31L26 | MARLIFLGPPGAGKGTQAVVVAEQLQLAHISTGELLRAAVTAQTPLGIEAKGYMDRGELVPDSLVLGLVRDRLQQPDTANGWILDGFPRNRSQAEALNLLLTEINQQVDRAVNLDVPDPVIIERMLARGRADDTESVIRRRLEVYREQTAPLIDFFRDRQQLLAIDGNSEVAAVTDRLVSALQVAA | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20357
Sequence Length: 186
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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P23352 | MVPGVPGAVLTLCLWLAASSGCLAAGPGAAAARRLDESLSAGSVQRARCASRCLSLQITRISAFFQHFQNNGSLVWCQNHKQCSKCLEPCKESGDLRKHQCQSFCEPLFPKKSYECLTSCEFLKYILLVKQGDCPAPEKASGFAAACVESCEVDNECSGVKKCCSNGCGHTCQVPKTLYKGVPLKPRKELRFTELQSGQLEVKWSSKFNISIEPVIYVVQRRWNYGIHPSEDDATHWQTVAQTTDERVQLTDIRPSRWYQFRVAAVNVHGTRGFTAPSKHFRSSKDPSAPPAPANLRLANSTVNSDGSVTVTIVWDLPEEPDIPVHHYKVFWSWMVSSKSLVPTKKKRRKTTDGFQNSVILEKLQPDCDYVVELQAITYWGQTRLKSAKVSLHFTSTHATNNKEQLVKTRKGGIQTQLPFQRRRPTRPLEVGAPFYQDGQLQVKVYWKKTEDPTVNRYHVRWFPEACAHNRTTGSEASSGMTHENYIILQDLSFSCKYKVTVQPIRPKSHSKAEAVFFTTPPCSALKGKSHKPVGCLGEAGHVLSKVLAKPENLSASFIVQDVNITGHFSWKMAKANLYQPMTGFQVTWAEVTTESRQNSLPNSIISQSQILPSDHYVLTVPNLRPSTLYRLEVQVLTPGGEGPATIKTFRTPELPPSSAHRSHLKHRHPHHYKPSPERY | Function: Has a dual branch-promoting and guidance activity, which may play an important role in the patterning of mitral and tufted cell collaterals to the olfactory cortex (By similarity). Chemoattractant for fetal olfactory epithelial cells.
PTM: N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76112
Sequence Length: 680
Subcellular Location: Cell membrane
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E3PRK1 | MKSVLKIRMSAHDAHYGGGLVDGARMLQLFGDVATELLIMNDGDEGLFKAYDMVEFMAPVFAGDYIEVEGSITEQGNTSRKMIFEARKVIVPRTDINDSACDVLETPIVVCRASGTCVVPKDKQRK | Function: Involved in the anaerobic fermentation of lysine. Catalyzes the deamination of L-3-aminobutyryl-CoA to produce crotonoyl-CoA.
Catalytic Activity: (3S)-3-aminobutanoyl-CoA = (2E)-butenoyl-CoA + NH4(+)
Sequence Mass (Da): 13845
Sequence Length: 126
Pathway: Amino-acid degradation; L-lysine degradation via acetate pathway.
EC: 4.3.1.14
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Q8RHX1 | MKSLIRLRMSSHDAHYGGNLVDGARMLQLFGDVATELLIQLDGDEGLFKAYDSVEFMAPVFAGDYIEAEGEIVNVGNSSRKMVFEARKVIVPRPDISDSAADVLAEPIVVCRATGTCVTPKDKQRGKK | Function: Involved in the anaerobic fermentation of lysine. Catalyzes the deamination of L-3-aminobutyryl-CoA to produce crotonoyl-CoA.
Catalytic Activity: (3S)-3-aminobutanoyl-CoA = (2E)-butenoyl-CoA + NH4(+)
Sequence Mass (Da): 13960
Sequence Length: 128
Pathway: Amino-acid degradation; L-lysine degradation via acetate pathway.
EC: 4.3.1.14
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O34676 | MKNKWYKPKRHWKEIELWKDVPEEKWNDWLWQLTHTVRTLDDLKKVINLTEDEEEGVRISTKTIPLNITPYYASLMDPDNPRCPVRMQSVPLSEEMHKTKYDLEDPLHEDEDSPVPGLTHRYPDRVLFLVTNQCSMYCRYCTRRRFSGQIGMGVPKKQLDAAIAYIRETPEIRDCLISGGDGLLINDQILEYILKELRSIPHLEVIRIGTRAPVVFPQRITDHLCEILKKYHPVWLNTHFNTSIEMTEESVEACEKLVNAGVPVGNQAVVLAGINDSVPIMKKLMHDLVKIRVRPYYIYQCDLSEGIGHFRAPVSKGLEIIEGLRGHTSGYAVPTFVVDAPGGGGKIALQPNYVLSQSPDKVILRNFEGVITSYPEPENYIPNQADAYFESVFPETADKKEPIGLSAIFADKEVSFTPENVDRIKRREAYIANPEHETLKDRREKRDQLKEKKFLAQQKKQKETECGGDSS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the interconversion of L-alpha-lysine and L-beta-lysine.
Catalytic Activity: L-lysine = (3S)-3,6-diaminohexanoate
Sequence Mass (Da): 54074
Sequence Length: 471
Pathway: Amino-acid degradation; L-lysine degradation via acetate pathway.
EC: 5.4.3.2
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Q9XBQ8 | MINRRYELFKDVSDADWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCVKSLRMAITPYYLSLIDPNDPNDPVRKQAIPTALELNKAAADLEDPLHEDTDSPVPGLTHRYPDRVLLLITDMCSMYCRHCTRRRFAGQSDDSMPMERIDKAIDYIRNTPQVRDVLLSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVNMLKKYHPVWLNTHFNHPNEITEESTRACQLLADAGVPLGNQSVLLRGVNDCVHVMKELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGYCVPTFVVDAPGGGGKTPVMPNYVISQSHDKVILRNFEGVITTYSEPINYTPGCNCDVCTGKKKVHKVGVAGLLNGEGMALEPVGLERNKRHVQE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the interconversion of L-alpha-lysine and L-beta-lysine.
Catalytic Activity: L-lysine = (3S)-3,6-diaminohexanoate
Sequence Mass (Da): 47102
Sequence Length: 416
Pathway: Amino-acid degradation; L-lysine degradation via acetate pathway.
EC: 5.4.3.2
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P25920 | MRRVVGKRVQEFSDAEFEQLRSQYDDVVLDVGTGDGKHPYKVARQNPSRLVVALDADKSRMEKISAKAAAKPAKGGLPNLLYLWATAERLPPLSGVGELHVLMPWGSLLRGVLGSSPEMLRGMAAVCRPGASFLVALNLHAWRPSVPEVGEHPEPTPDSADEWLAPRYAEAGWKLADCRYLEPEEVAGLETSWTRRLHSSRDRFDVLALTGTISP | Function: Specifically methylates the N(1) position of adenine 1408 in 16S rRNA. Confers resistance to various aminoglycosides, including kanamycin, neomycin and apramycin.
Catalytic Activity: adenosine(1408) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(1408) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23664
Sequence Length: 215
EC: 2.1.1.180
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E3PRJ5 | MISVESKLNLDFNLVEKARAKAKAIAIDTQEFIEKHTTVTVERAVCRLLGIDGVDTDEVPLPNIVVDHIKENNGLNLGAAMYIANAVLNTGKTPQEIAQAISAGELDLTKLPMKDLFEVKTKALSMAKETVEKIKNNRSIRESRFEEYGDKSGPLLYVIVATGNIYEDITQAVAAAKQGADVIAVIRTTGQSLLDYVPYGATTEGFGGTYATQENFRLMREALDKVGAEVGKYIRLCNYCSGLCMPEIAAMGAIERLDVMLNDALYGILFRDINMQRTMIDQNFSRIINGFAGVIINTGEDNYLTTADAFEEAHTVLASQFINEQFALLAGLPEEQMGLGHAFEMDPELKNGFLYELSQAQMAREIFPKAPLKYMPPTKFMTGNIFKGHIQDALFNMVTIMTNQRIHLLGMLTEALHTPFMSDRALSIENAQYIFNNMESISEEIQFKEDGLIQKRAGFVLEKANELLEEIEQLGLFDTLEKGIFGGVKRPKDGGKGLNGVVSKDENYYNPFVELMLNK | Function: Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively.
Catalytic Activity: (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
Sequence Mass (Da): 57626
Sequence Length: 519
Pathway: Amino-acid metabolism; lysine degradation.
EC: 5.4.3.3
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Q8RHX7 | MGKLDLDWGLVKEARESAKKIAADAQVFIDAHSTVTVERTICRLLGIDGVDEFGVPLPNVIVDFIKDNGNISLGVAKYIGNAMIETKLQPQEIAEKVAKKELDITKMQWHDDFDIQLALKDITHSTVERIKANRKAREDYLEQFGGDKKGPYIYVIVATGNIYEDVTQAVAAARQGADVVAVIRTTGQSLLDFVPFGATTEGFGGTMATQENFRIMRKALDDVGVELGRYIRLCNYCSGLCMPEIAAMGALERLDMMLNDALYGILFRDINMKRTLVDQFFSRIINGFAGVIINTGEDNYLTTADAIEEAHTVLASQFINEQFALVAGLPEEQMGLGHAFEMEPGTENGFLLELAQAQMAREIFPKAPLKYMPPTKFMTGNIFKGHIQDALFNIVTITTGQKVHLLGMLTEAIHTPFMSDRALSIENARYIFNNLKDFGNDIEFKKGGIMNTRAQEVLKKAAELLKTIETMGIFKTIEKGVFGGVRRPIDGGKGLAGVFEKDNTYFNPFIPLMLGGDR | Function: Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively.
Catalytic Activity: (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
Sequence Mass (Da): 57323
Sequence Length: 518
Pathway: Amino-acid degradation; L-lysine degradation via acetate pathway.
EC: 5.4.3.3
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E3PRJ4 | MSSGLYSMEKKEFDKVLDLERVKPYGDTMNDGKVQLSFTLPLKNNERSAEAAKQIALKMGLEEPSVVMQQSLDEEFTFFVVYGNFVQSVNYNEIHVEAVNSEILSMEETDEYIKENIGRKIVVVGASTGTDAHTVGIDAIMNMKGYAGHYGLERYEMIDAYNLGSQVANEDFIKKAVELEADVLLVSQTVTQKNVHIQNMTHLIELLEAEGLRDRFVLLCGGPRINNEIAKELGYDAGFGPGRFADDVATFAVKTLNDRMNS | Function: Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively.
Catalytic Activity: (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
Sequence Mass (Da): 29224
Sequence Length: 262
Pathway: Amino-acid metabolism; lysine degradation.
EC: 5.4.3.3
|
Q8RHX8 | MSSGLYSTEKRDFDTTLDLTQIRPYGDTMNDGKVQMSFTLPVACNEKGIEAALQLARKMGFVNPAVAFSEALDKEFSFYVVYGATSFSVDYTAIKVQALEIDTMDMHECEKYIEENFGREVVMVGASTGTDAHTVGIDAIMNMKGYAGHYGLERYKGVRAYNLGSQVPNEEFIKKAIELKADALLVSQTVTQKDVHIENLTNLVELLEAEGLRDKIILIAGGARITNDLAKELGYDAGFGPGKYADDVATFILKEMVQRGMNK | Function: Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively.
Catalytic Activity: (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
Sequence Mass (Da): 28990
Sequence Length: 263
Pathway: Amino-acid degradation; L-lysine degradation via acetate pathway.
EC: 5.4.3.3
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A6TV07 | MLLPLIVFLLSVLIHHRIYSSFFLHFYSPQYYMICSRLTLLSSCSWHDFHLKLILLEFASQSTNPVPALHNDPTYEKISRRFHENPEAFADVFARAWFKLLHRDMGPQTRYLGPEVPEEELIWQDPIPAVDYELTDAEIAELKAKILDSGLTVSDLVTTAWASASTFRGSDMRGGANGARIRLAPQKDWEVNQPEQLTKVLTVLEDIQNQLDKKVSIADLIVLGGSAAIEKSAQDAGFDVTVPFALGRGDATQEQTDIESFEVLEPISDGFRNYQKKQYSVSAEELLLDKAQLLNLTAPEMTVLVDGMRVLGTNYNGTQHGVFTDRVGTLTNDFFVNLLDMGVEWKPMDGGLYEARNRKTGEVVRTATRVDLVFGSNSVLRALVEVYAQDDNKEKFVGDFIAAWIKVMNADRFDLD | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Catalytic Activity: AH2 + H2O2 = A + 2 H2O
Sequence Mass (Da): 46834
Sequence Length: 416
EC: 1.11.1.21
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P46817 | MPEQHPPITETTTGAASNGCPVVGHMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGAAFDYAAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIRMAWHAAGTYRIHDGRGGAGGGMQRFAPLNSWPDNASLDKARRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKTFGFGFGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQMGLIYVNPEGPNGNPDPMAAAVDIRETFRRMAMNDVETAALIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGWKSSYGTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQYTAKDGAGAGTIPDPFGGPGRSPTMLATDLSLRVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDMGPVARYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQILASGLTVSQLVSTAWAAASSFRGSDKRGGANGGRIRLQPQVGWEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSFADLVVLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESFAVLEPKADGFRNYLGKGNPLPAEYMLLDKANLLTLSAPEMTVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVNLLDMGITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSELRALVEVYGADDAQPKFVQDFVAAWDKVMNLDRFDVR | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria.
PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Catalytic Activity: AH2 + H2O2 = A + 2 H2O
Sequence Mass (Da): 80562
Sequence Length: 740
EC: 1.11.1.21
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Q5U3S1 | MNLTEICDNAKKGREYALLGNYDSSMVYYQGVIQQIHKHCQSLRDPAQKVKWQQVRQELAEEYEQVKSIVSTLESFKVDKAVDFPNPVPEEGPRDPDVWPPPTPAEHRGPVQVKKPVPLSKPQRKESPGMQHRGAVGRGQANIKPDRPNTRDGRGNKAKEEKSKRNAQEGAADVEQKKFDGTGYDSDLVDALERDIVSRNPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGVGGAQESEDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMAMRRRIQGLSPEEIRALSKDELQMPVTMEDFELALKKISKSVSAADLEKYESWMSEFGSV | Function: Regulates microtubule dynamics in Sertoli cells, a process that is essential for spermiogenesis and male fertility. Severs microtubules in an ATP-dependent manner, promoting rapid reorganization of cellular microtubule arrays (By similarity).
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Sequence Mass (Da): 54891
Sequence Length: 488
Subcellular Location: Cytoplasm
EC: 5.6.1.1
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Q9BW62 | MNLAEICDNAKKGREYALLGNYDSSMVYYQGVMQQIQRHCQSVRDPAIKGKWQQVRQELLEEYEQVKSIVSTLESFKIDKPPDFPVSCQDEPFRDPAVWPPPVPAEHRAPPQIRRPNREVRPLRKEMAGVGARGPVGRAHPISKSEKPSTSRDKDYRARGRDDKGRKNMQDGASDGEMPKFDGAGYDKDLVEALERDIVSRNPSIHWDDIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVGGALENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPTAKGRAELLKINLREVELDPDIQLEDIAEKIEGYSGADITNVCRDASLMAMRRRINGLSPEEIRALSKEELQMPVTKGDFELALKKIAKSVSAADLEKYEKWMVEFGSA | Function: Regulates microtubule dynamics in Sertoli cells, a process that is essential for spermiogenesis and male fertility. Severs microtubules in an ATP-dependent manner, promoting rapid reorganization of cellular microtubule arrays (By similarity). Has microtubule-severing activity in vitro .
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Sequence Mass (Da): 55392
Sequence Length: 490
Subcellular Location: Cytoplasm
EC: 5.6.1.1
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