ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5QM25 | MSRRNAGAMQREGSVKDWEEFDPSPSPKLAYSQSYVAMRGLLTSVASLDLVLMSSSLKSAWAAISSHKHARSLERSRSKGMSLKRAMLQLLVCFMVGIFIGFTPPFSVDLPGKIASENGRLPFDGDAIDRRQMVERQGTKLEPFVAEAESEASSEPQVEEGPPVPAMLDDEADFVEASPIVHSVNDSGIVVRKHLIIITTTSVRPHQAYYLNRLAHVLKDVPPPLLWIVAEWPYQSRETAEILRSSGIMYRHLICNRNTTNIRKIVVCQKNNAIFHIKKHRLDGIVHFADEERAYSADLFEEMRKIRRFGTWPVAIHVGT... | Function: Probable beta-1,4-xylosyltransferase involved in xylan biosynthesis in cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 50318
Sequence Length: 446
Subcellular Location: Golgi apparatus membrane
EC: 2.4.2.-
|
Q9ZQC6 | MGSLERSKKKAQVWKKAVIHFSLCFVMGFFTGFAPAGKASFFSNFETTSYTSTKSPIPPQPFENATYTQHSLLNRTLINSQSQAPAPAESREAEGETRSLSEKEDENQVKVTPRGLVIVVTPIITKDRYKNVLLRRMANTLRLVPPPLLWIVVEKHSDGEEKSSSTMLRKTGIMYRRIVFKEDFTSLESELDHQRNLALRHIEHHKLSGIVHFAGLNNIYDLDFFVKIRDIEVFGTWPMALLSANRKRVVVEGPVCESSQVLGWHLRKINNETETKPPIHISSFAFNSSILWDPERWGRPSSVEGTKQDSIKYVKQVVLE... | Function: Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls . Xylan xylosyltransferase that acts cooperatively with IRX14 to achieve the successive addition of xylosyl residues during xylan backbone elongation .
Catalytic Activity: [(1->4)-beta-D-xylan](n) + UDP-al... |
Q6Z3Y6 | MASAGGCKKKTGNSRSRSPRSPVVLRRAMLHSSLCFLVGLLAGLAAPSDWPAAAGAAVFLRTLRASNVIFSRSSNRPQQPQLVVVVTTTEQSDDSERRAAGLTRTAHALRLVSPPLLWLVVEEAPAEKHAAPPTARLLRRTGVVHRHLLMKQGDDDFSMQISMRREQQRNVALRHIEDHRIAGVVLFGGLADIYDLRLLHHLRDIRTFGAWPVATVSAYERKVMVQGPLCINTSSSSVITRGWFDMDMDMAAGGERRAAADRPPPETLMEVGGFAFSSWMLWDPHRWDRFPLSDPDASQESVKFVQRVAVEEYNQSTTRG... | Function: Probable beta-1,4-xylosyltransferase involved in xylan biosynthesis in cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 37603
Sequence Length: 338
Subcellular Location: Golgi apparatus membrane
EC: 2.4.2.-
|
Q9H1K1 | MAAAGAFRLRRAASALLLRSPRLPARELSAPARLYHKKVVDHYENPRNVGSLDKTSKNVGTGLVGAPACGDVMKLQIQVDEKGKIVDARFKTFGCGSAIASSSLATEWVKGKTVEEALTIKNTDIAKELCLPPVKLHCSMLAEDAIKAALADYKLKQEPKKGEAEKK | Function: Mitochondrial scaffold protein, of the core iron-sulfur cluster (ISC) assembly complex, that provides the structural architecture on which the [2Fe-2S] clusters are assembled . The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the... |
Q9D7P6 | MAAATGAGRLRRAASALLLRSPRLPARELSAPARLYHKKVVDHYENPRNVGSLDKTSKNVGTGLVGAPACGDVMKLQIQVDEKGKIVDARFKTFGCGSAIASSSLATEWVKGKTVEEALTIKNTDIAKELCLPPVKLHCSMLAEDAIKAALADYKLKQESKKEEPEKQ | Function: Mitochondrial scaffold protein, of the core iron-sulfur cluster (ISC) assembly complex, that provides the structural architecture on which the [2Fe-2S] clusters are assembled. The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the ... |
Q4HTS9 | MTTRYRVEYALKTHRRDQFIEWVKGLLAVPFVLYSQPTGVFGDGPSVTQMAEEAHRRYAEIMRDVELMIDDHISRQQDDSMFPSKLRMLIPTAGPFFTRLPLEAAFKYQDRKRYISSRRFVAPSFNDVRQILNSAQSMAVTNGSLQLATFDGDVTLYDDGFNLEPTSPVIPRLLDLLRKNIKIGIVTAAGYTSADRYYERLHGLLDAIAESTDLDPVQKQSIIIMGGEANYLFEYSPSSPCKLAPVPRTQWLTPEMASWSDADITRLLDVAENALRDCVNNLNLPAMIMRKDRAVGIIPKTPGTRIARESLEETVLVVQR... | Function: IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation.
Catalytic Activity: H2O + IMP = inosine + phosphate
Sequence Mass (Da): 49756
Sequence Length: 446
EC: 3.1.3.99
|
Q7SDZ1 | MTTRYRVEYALKTHRRDQFIEWIKALLAVPFVLYSQPHGVLEDPDRSVDTLSQTREEAHRRYSEIFRDIEAMIDDHIAHQNDAENPFPSKLKLLVPSIGPFFTRLPLEAAFKFQDNKRYISSRRFVSPSFNDIRLILNSAQIMAVTTYGTLQLATFDGDVTLYDDGQSLEPTSPVIPRLLDLLRKNVKIGIVTAAGYTTADRYYSRLHGLLDAMANSADLTPSQKQSLVVMGGEANYLFEFDSSSPHLLAPVPRQHWLTPEMAAWNEQDIAQLLDVAEAALRDCIKTLNLPATLMRKDRAVGIIPVSPEIRIPRESLEET... | Function: IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation.
Catalytic Activity: H2O + IMP = inosine + phosphate
Sequence Mass (Da): 48444
Sequence Length: 431
EC: 3.1.3.99
|
A0A144A134 | MKNLDINTFDNIEDIPLGSSEQDPYDFFTLSDRNVMNSDMKKNIVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEMFIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPPTFNEVRHILNLAQILSLEEGLDLLTFDADETLYPDGHDFNDEVLASYISCLLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMGGESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVIKDFGLCAQIQRKEKSIGLVPNKIPSLN... | Function: Specifically, catalyzes the dephosphorylation of inosine monophosphate (IMP) into inosine . By dephosphorylating IMP, plays a role in the purine salvage pathway . Does not have phosphotransferase activity with IMP as phosphate donor and adenosine as phosphate acceptor .
Catalytic Activity: H2O + IMP = inosine... |
O14349 | MASRYRVEYALKQHRKDDFIEWIKGLLSVPFVLQAGTPSQKLVTREKEQETLERYAVILRDVEKLIEAHIQIVSEGGSYSQLKMLVPSITIFWTPLPLVKAMYALEPKLCLAKRSFVAPSFNDVRAILGGAQLNYLADNGLDMVSFDGDVTLYEDGQPLLPDNPVISRLIQLLSRGIYVIILTAAGYPSRTGQEYTDRFSGLLQAIEDSDLKDGQKRKLHVLGGESNYLFAYDPLHGLQWVDADSWMLPVMKTWPHDEILEILDTAEETLRSCIQGLNIDAKIVRKERSVGFVPSLGQKLRREQLEEAVLETQATLQIRN... | Function: IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation.
Catalytic Activity: H2O + IMP = inosine + phosphate
Sequence Mass (Da): 45806
Sequence Length: 405
EC: 3.1.3.99
|
Q99312 | MSSRYRVEYHLKSHRKDEFIDWVKGLLASPFVLHAVSHEGDYNDDLATTQRVRSQYADIFKDIEGLIKDKIEFDSRNMSQDEIEDGASSQSLNILGQSRLNLLVPSIGTFFTELPLEQAFLWEDSQRAISARRMVAPSFNDIRHILNTAQIFHFKKQENLHNGKVLRLVTFDGDVTLYEDGGSLVYTNPVIPYILKLLRCGINVGIVTAAGYDEAGTYENRLKGLIVALHDSTDIPVSQKQNLTIMGGESSYLFRYYEDPEEDNFGFRQIDKEEWLLPRMKAWSLEDVEKTLDFAERTLNRLRKRLNLPSEISIIRKVRA... | Function: IMP-specific 5'-nucleotidase involved in IMP (inosine 5'-phosphate) degradation.
Catalytic Activity: H2O + IMP = inosine + phosphate
Sequence Mass (Da): 51330
Sequence Length: 450
EC: 3.1.3.99
|
D0TZF0 | MASLPHCLSARPLVVAAAPGRPGPGPGPWLRGGARRRNAAFSAGNAGRRVGLRRSVASAVEVGVGEDEEEGVEEEEEEVEAVVMPERYALGGACRVLAGMPAPLGATALDGGVNFAVYSAGASAASLCLFTPDDLEADEVTEEVPLDPLFNRTGNVWHVFIEGELHNMLYGYRFDGMFAPHCGQYFDVSNVVVDPYAKAVISRGEYGVPGPGGDCWPQMAGMIPLPYSTFDWQGDLPLRYPQKDLVIYEMHLRGFTKHSSSNVEHPGTYIGAISKLDYLKELGVNCVELMPCHEFNELEYFSCSSKMNFWGYSTINFFSP... | Function: Starch-debranching enzyme involved in amylopectin biosynthesis in endosperm. Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch . Works as ISA1 homooligomer or together with ISA2 as h... |
Q8L735 | MAAWSPSVGIGSCCLNNGITRTWKFPSARLFTGRKNKIKLGSETLMFTRKRFMGDLVTSALQSYQFSKICASKTSIELREALSSRRAEADDLKKVTSYSFRTKAGALVKVKVEKKREKYSILVYVSSLELSGDDKSRLVMVWGVYRSDSSCFLPLDFENSSQDSQTHTTETTFVKSSLSELMLGLEFDGKESPFYLSFHLKLVSGRDPDGQEMLTHRDTDFCIPVGFTAGHPLPLGLSSGPDDDSWNFSFFSRSSTNVVLCLYDDSTTDKPALELDLDPYVNRTGDVWHASVDNTWDFVRYGYRCKETAHSKEDVDVEGE... | Function: Involved in the trimming of pre-amylopectin chains. Accelerates the crystallization of nascent amylopectin molecules during starch synthesis. ISA1 and ISA2 work exclusively together as a multimeric holoenzyme. ISA1-ISA2 removes preferentially branches that are very close to other branches.
Sequence Mass (Da):... |
Q6AU80 | MASLPAPPTPLGSCPRGRGGGRVVARPRRAGLACAARSCYRFRTDDDGVVDVAVSGEDGDGGGGGYAVSVEVPGTRGREGGLVLRASGSGEGVPLAPAAGGASLAAELSFDPTRAPFYLSFLLTDASGAEIRTHRKTSFRVPVGVGPGSPAPLGMSISGDGAVNFAVYSKNANAVSLYLYAAAVGGGGGDEPALEIDLDPYIHRTGNVWHVSLASVDGYVSYAFCCGGIRRPLLDPYAKVIGDFVSSNSVYDEGVTAPSMRCFASLAIAPSYNWGRDRHPRLPLEKLVVYRANVALFTKDRSSGLPDDAAGTFTGLSAKV... | Function: Starch-debranching enzyme involved in amylopectin biosynthesis in endosperm. Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch . Works together with ISA1 as heterooligomer. The heter... |
Q9M0S5 | MLTSPSSSSTYDPFSSNFSPSLTNAFSSSFTIPMGLKLSRRVTRARIFSRKIKDRSTLKVTCRRAHERVVEEEASTMTETKLFKVSSGEVSPLGVSQVDKGINFALFSQNATSVTLCLSLSQSGKDDTDDDGMIELVLDPSVNKTGDTWHICVEDLPLNNVLYGYRVDGPGEWQQGHRFDRSILLLDPYAKLVKGHSSFGDSSQKFAQFYGTYDFESSPFDWGDDYKFPNIPEKDLVIYEMNVRAFTADESSGMDPAIGGSYLGFIEKIPHLQDLGINAVELLPVFEFDELELQRRSNPRDHMVNTWGYSTVNFFAPMSR... | Function: Involved in starch catabolism. ISA3 removes different branches than ISA1-ISA2, namely short chains that prevent amylopectin crystallization. May be the debranching enzyme required to assist beta-amylases for starch degradation in leaves at night.
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic bra... |
P10342 | MKCPKILAALLGCAVLAGVPAMPAHAAINSMSLGASYDAQQANITFRVYSSQATRIVLYLYSAGYGVQESATYTLSPAGSGVWAVTVPVSSIKAAGITGAVYYGYRAWGPNWPYASNWGKGSQAGFVSDVDANGDRFNPNKLLLDPYAQEVSQDPLNPSNQNGNVFASGASYRTTDSGIYAPKGVVLVPSTQSTGTKPTRAQKDDVIYEVHVRGFTEQDTSIPAQYRGTYYGAGLKASYLASLGVTAVEFLPVQETQNDANDVVPNSDANQNYWGYMTENYFSPDRRYAYNKAAGGPTAEFQAMVQAFHNAGIKVYMDVV... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.
Sequence Mass (Da): 83627
Sequence Length: 776
Subcellular Location: Secreted
EC: 3.2.1.68
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Q2SWT6 | MTSRLFALIPCAGTGSRSGSALPKQYRTLAGRALLHYTLAAFDACSEFAQTLVVISPDDAHFDARRFAGLRFAVRRCGGASRQASVMNGLIQLAEFGATDADWVLVHDAARPGITPALIRTLIGALKDDPVGGIVALPVADTLKRVPAGGDAIERTESRNGLWQAQTPQMFRIGMLRDAIQRAQLEGRDLTDEASAIEWAGHTPRVVQGSLRNFKVTYPEDFDLAEAILAHPARAS | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25393
Sequence Length: 236
Pathway: Isoprenoid bi... |
B9MJW2 | MKTCAILCAAGKGTRFGGNTPKQFLFLKNKMIIEYSLEVFEKSHFIDGIVLLVPQGFEDIARYLKDKFSKVIFWDYGGNERADTVKRGLEILKGECDIVAIHDSARPFITLELLEKLIADVETHFAVAPGILANDTVKFVVDGHIQNTLPRSNICLIQTPQVFKFDLIYRGYEMFKNELFTDDLQYVERLGIKPKIIENSRINFKITTKEDLLIAEAIVEKGYW | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25602
Sequence Length: 224
Pathway: Isoprenoid bi... |
Q3A9N7 | MEKIGVIVTAGGAGRRFGGEKPKQFLELSGIPVIIITLKRMVNLPIVGQVVLTVPENYIEVAGDLLSRYNLAGIKLTAGGTTRRESVLRGIRALTGNFSIIAVHDGVRPFFPKGALSEGVKKLSEGYGGAILAVPLRDTVKEVKDNVVISTLDRSRLYAVQTPQIFRREALLKGHALGEKQHLDAVDDSILVELCGETVAVIPGDYKNLKITWPEDLEFAEFLFTRYFAKELL | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25501
Sequence Length: 233
Pathway: Isoprenoid bi... |
Q3J2K9 | MTTAAIIVAAGRGTRAGGDLPKQWQPLAGRPVLAHTLAAFRAAAGVSRTLLVIHPDDRARAEALPGVAEGKVELVEGGASRDASVRNALEALAGAGIERVLIHDGARPLVAPELIARTLAALETAPGAAPAVPVSDALWRGEGGRVVGTQDRTGLFRAQTPQAFRYEAILAAHRAHPGGAADDVEVARAAGLEVAIVEGCEDNLKVTYPGDFARAERLLALAAGL | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 23098
Sequence Length: 225
Pathway: Isoprenoid bi... |
Q824I4 | MDPKCSLILLSGGKGERFGANQPKQYLPFQGEPLILHALKTALHIPEITEVIVVCDVSYRHIFEGFPVKFAESGKRRQDSVFSGLQHVSNPWVLIHDGVRPFIYPDEVTELIAVAQQTGAATLVSNVPYTIKQRHPVKTLDRDALSIVHTPQCVKTEILSAGLEFASREGITLVDDTQAAELLDIPVSLVSSKHPQIKITYPEDLTIAHALL | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 23379
Sequence Length: 212
Pathway: Isoprenoid bi... |
Q746Z9 | MAVFALVPAAGMGKRMGASINKQYLILAGRPILAHTLSVFEGASFVDGIFVITPEDEIPFCRDHVVERYGFTKVRGIVAGGAERQHSVLNGLRAMEGTVADDDVILIHDGVRPFVSTDVLARATAVAREDDGALVAVPAKDTVKTVEDGIITGTPPRETLWLAQTPQAFRYAVIRAAHEIADAERFLGTDDAMLVERLGRSVRIVVGDYRNIKITTPEDMVLAEAFLKELAA | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25084
Sequence Length: 232
Pathway: Isoprenoid bi... |
Q2SKW7 | MFVDSMEEHKLWVIVPAAGVGSRMGGERPKQYLKLIDRSVLEHTLDRLLSAPGISQIYLPLHPQDKWWPEIADKYTGKVISVAGGEERSTSVLNALEKIESHAAIEDWVLVHDVARPCFRISDISNLMRLLWNTQPGGLLGVPVADTVKRTNEKGEVLATVSRANLWRAYTPQMFRFGALLSALRQGSEKGVHITDEASAIEAQGLKPVMVEGHSDNIKITHPQDLPLAEIFLRRIMQEEE | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 26948
Sequence Length: 241
Pathway: Isoprenoid bi... |
Q9KGF8 | MEYSVVIPAAGQGKRMRAGHNKQFIELGGKPILAHTLAVFEQDDWCTNVVIVANEQEIEEMGELANRYQISKAKKIVAGGRERQESVFAGLKALSQDGLVLIHDGARPFVTEKEIHSLVETAAKTHAAVLAVPVKDTIKRVEGEAVLETMPREELWAVQTPQAFDLALIKQAHQKAENEQMLGTDDASLMEWLGYSVAVVQGSYFNFKLTTPEDLLFAEAILAEKERR | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25270
Sequence Length: 228
Pathway: Isoprenoid bi... |
A1WWZ0 | MGRYWAVIPAAGVGRRMGGGDRPKQYRLLLGRPVIGWALERLLGHPKVAGAVVALAADDPHWDALGLDRQVAGKPVHRVEGGAERRDSVRAALAYLGGIANPEDRVLVHDAVRPCLSAAELDRLIDEGGAAVDGALLATPVRDTLKRADGDCVGATVSREGLWQAQTPQLFPLRRLSAALDAALAAGVAVTDEAQAVEWHDGQPRLVTGEAGNLKITHQADLDLAAAVLTAQRAATEREQTA | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25520
Sequence Length: 242
Pathway: Isoprenoid bi... |
A4D126 | MEAGPPGSARPAEPGPCLSGQRGADHTASASLQSVAGTEPGRHPQAVAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRISLVEAGVTRHRSIFNGLKALAEDQINSKLSKPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERARHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTECLQLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKERISQEICVVMDTEEDNKHVGHLLEEVLKSELNHVKVTSEAL... | Function: Cytidylyltransferase required for protein O-linked mannosylation . Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate . CDP-ribitol is a substrate of FKTN during the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-be... |
Q5QUC3 | MKSESESHAQSQIDSLMAVIPAAGSGSRMQANIPKQFLMVANRTLLEYSIEAVLKDARVEQVFVAVSDSNAEYLIELKKSLPTKVHFVTGGNSRAESVLAGVKVAVSQGATHVLVHDAARPCLPKKALTAVINTGLKDPQGAILAIPVRDSLKRAVISVNDETGVTHIESSVDREALWQAQTPQVFNAERLQQAIEHMGALNPQLTDEASAMQWCGFQPALIPGSIRNLKVTHPEDFECVRDWLLADNNDHKN | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 27506
Sequence Length: 253
Pathway: Isoprenoid bi... |
C4Z312 | MNTAIVLAGGSGKRMHSEIPKQYMQLNGKPVIYYSLKAFEESEHVDEIILVTAKEYIEYVRNEIAGSQFAKLTKIIEGGKERFDSVWAGLQQISEKGYVYIHDGARPCINQNIINACWETVVQTDACVAAAPVKDTIKVADADEYAINTPDRKTLWQIQTPQVFSADVIKEAYSRLYEQNCFDGVTDDAMVVERYGNSKIKLVNCGYCNIKITTPEDMEIAGIFLKG | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25421
Sequence Length: 227
Pathway: Isoprenoid bi... |
A9KSU6 | MEKVTAIVLAAGQGKRMKSSVSKQYMLLKDKPVLYYSLKAFENSLVTDIIVVVGNDEISYVKEEIIKPYGFRKVTHVVEGGSERYLSVLNGLNKIKDSDYVLVHDGARPLIKTNTINTVISEVEEKKACIVGVASKDTVKISTHDGIIDSTPDRNQVYTIQTPQAFEYSILREAYDNLASYQGAMITDDAMIVECLNRYPIYLVQGEYTNIKITTPEDLIFAEAILREHQDFI | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 26195
Sequence Length: 233
Pathway: Isoprenoid bi... |
C1D558 | MSRCLALVPAAGGGSRMGADRPKQYLDLAGAPLLAHTLRRLLAEPRLARVLVVLAPDDVWFDRFDWPRDVRLEILRVGGATRAESVRNGLLHAGAAADDWVLVHDAARCCLPPDALDRLIDTLQADPVGGLLALPVADTLKRETSGQRVAQTVSREGLWLAQTPQMFRAGMLALALDRPLDRAVTDEASAIERLGLVPRLVTGDALNFKVTWPHDLVLARAVLGLDNAGK | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 24849
Sequence Length: 230
Pathway: Isoprenoid bi... |
Q8ZBP6 | MSNFAVSLPEVIAVLPAAGIGSRMLVDCPKQYLTVGGKTIIEHAIFSLLHHPRIQRVIVVIHPQDTQFSRLSVAQDPRISTVYGGDQRANSVMAGLQLAGQAEWVLVHDAARPCLHLDDLSRLLSITECSQVGGILAAPVRDTMKRAEPGIQAIAHTVDRQDLWHALTPQLFPLELLKLCLSRALREGVAVTDEASALEHCGYHPILVTGRSDNIKVTRPEDLALAEFYLTQRQSLNNDSL | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 26401
Sequence Length: 241
Pathway: Isoprenoid bi... |
A3DI26 | MESISLKAHAKINLSLDVIGKRQDGYHEVRMIMQSIALHDEVVIEKRAAGIKVECDKPWVPEGSGNIAYKAANLMMERYKIESGVGIKILKRIPVAAGLAGGSADAAAVIKGMNELFNLNADEAELMDIGKQVGADVPFCIKGGTMLSEGIGEKLTKIPSFEGVNIVLVKPKVGVSTAWVYSNLKLNEISSRPDTELLIKAIYEKNIGCLAQNMTNVLETVTIKKYGVINDIKNELLRLGALGSMMSGSGPSVFGIFENEKQACLAYEGLKNSEWECFVTQTI | 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): 30680
Sequence Length: 283
Pathway: Isoprenoid biosynthesis; isopente... |
A1TT72 | MRTLHDLPAPAKLNLFLHITGRRPDGYHLLQSVFMLIDWCDTLHIELRPDGGISREDMGAGLPADDLCTRAARALQAATGTRQGAHIVLEKSIPAQAGMGGGSSDAATTLLALNRLWGLGLGRTALERIGLSLGADIPFFLRGRNAWVEGIGETIMPLENVHALPQSRFVVVKPEAGLDTKSIFSSPSLERNSERATISGFAAAHYQFGKNVLQPVAETLCPEVSEAIRWLEHKGLQARMTGSGSAVFAQMTHAIDLFDLPTGWRAKVCDNLRLHPLAGWAADED | 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): 30829
Sequence Length: 285
Pathway: Isoprenoid biosynthesis; isopente... |
Q6F8J0 | MIRVASPAKINLFLHITGRRNDGYHELQSIFQLIDLYDWMTFTPRTEAEDNLSITGIEQVDLEQNLIFRAAQLLKLYAKKYCGLNIQIEKQIPMGAGLGGGSSNAATTLLVLNQLWDCGLNLDQLAALGVKLGADVPIFIYGKNAWAEGIGEKLTFVDLDQKQYIILKPDCFISTQLLFSQKTLTRDSNRTTFCAYQLKPSDFGNNFEALARSLYPEVEEAMQYLDQFGQAKLTGTGACVFTEVTPEMNVSEIVQHAPCKSYVVHSLNKSPLSHFMTDI | 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): 31173
Sequence Length: 279
Pathway: Isoprenoid biosynthesis; isopente... |
A3N0D8 | MTEKIILPSPAKLNLFLYITNKRADGYHELQTLFQFLDFGDDISLEVNESGEIELLNAIEGVAKEQNLIYRAAKLLQNHTACSKGAKIGVTKRLPMGGGVGGGSSNAATVLVGLNHFWQTGLSLEQLAELGLSLGADVPIFVRGFAAFAEGVGEKLVACQPRESWYVVLKPNVSISTAAVFQDPNLPRNTPKRTLSRLLSEEWTNDCEKVVRDHYFEVEDLIAELLQYATFRLTGTGACIFAEFESEAEAKAVFAHKPHNIFGFIAKGQNRSPLHQMLNLTTSPQ | 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): 31309
Sequence Length: 285
Pathway: Isoprenoid biosynthesis; isopente... |
Q8FI04 | MRTQWPSPAKLNLFLYITGQRADGYHTLQTLFQFLDYGDTISIELRDDGDIRLLTPVEGVEHEDNLIVRAARLLMKTAADSGRLSTGSGANISIDKRLPMGGGLGGGSSNAATVLVALNHLWQCGLSMDELAEMGLTLGADVPVFVRGHAAFAEGVGEILMPVDPPEKWYLVAHPGVSIPTPVIFKDPELPRNTPKRSIETLLKCEFSNDCEVIARKRFREVDAVLSWLLEYAPSRLTGTGACVFAEFDTESEARQVLEQAPEWLNGFVAKGVNLSPLHRAML | 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): 30973
Sequence Length: 283
Pathway: Isoprenoid biosynthesis; isopente... |
B9DSY9 | MVSIIERAPAKINLGLDVLGKREDGYHDLEMVMISIDLCDYVTVSPLKDDVIMIESDCPKMPINEKNDVYKVAKLIKSRYAISEGVSILLNKKIPVCAGMGGGSSDAAATIRALNQLWDLKLSMEEMIAIGIAIGSDVPYCIQAGCAKIGGKGDRIELIDGKLSSWVVLVKPDFGISTRTVFPEIDCDVISRVDISAIVNALEGNNYSDLITHMGNALEDISIARKPFIQKVKDKMVAAGADVALMTGSGPTVFALCQTEKQANRVFNSVKGFCKEVYKVRTL | 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): 30678
Sequence Length: 283
EC: 2.7.1.148
|
Q30TG0 | MKMKLYRAYAKVNIFLKIQGSRGNYHEIVSRFMRVPSLYDELSFVPKESSEEFELIGSFSCKREQNTIYKAYRALLEFLDEASGLHVENLMQKYAVKVTKNIPTFAGLGGGSSDAATFLKMCNEVLHLGLSQNELALIGLHVGADVPFFIYGYNSANVSGIGEVVEEFKEELLDIEVFTPQLEISTPKVYNLYRENFYNPVDGFEVERLKKISSKDALSAMSAAEANDLFAPAIQLYKELKNHYKYGYYFSGSGSSFFRVKEKENI | 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): 30163
Sequence Length: 266
Pathway: Isoprenoid biosynthesis; isopente... |
A6Q782 | MYSINAHAKVNIFLKITGHENGYHTLLSRFMRVDDLYDTITLVPGTFDSFTLEGCKGVPLHFNTIYKAYEALLEPFPKLEDFFKSHKVVVEKSIPSQAGLGGGSSDAGAFMRLINSLSQNPLSTDALAKLGSSIGADVPFFVYNYPSANVRGFGEIVEPFRETPLKLELFTPDIGCDTAKVYQTYHKYLLRTLDPKSFFGWENMDSGTLLQLIADPVALNDLYPAALSTCPALEKLDTKGWFFSGSGSTFFRVKD | 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): 28268
Sequence Length: 255
Pathway: Isoprenoid biosynthesis; isopente... |
Q67JC2 | MEIECHAKVNLTLDVLGRRPDGYHEIRSVMVPVSLHDRLVLEPAEEEIVLESRPPATDRLEENLAYRAAALLREATGCSRGAVIRLQKTIPVAAGLAGGSTDAAGVLTGLNRLWGTGLSDGELADLAIRLGSDVPFFIWSRPARVEGIGERVTPLPVAGPLWMVVATPDVPKSTGQVYRWFDELADVGPRPDAGAMEAALARGDAAAVGRALCNVFEQVMLPRHPEIARLKEAMLAAGALGAVMSGAGPSVLGVVPDREAGGRLLERIRPLSRDAWVVRTLV | 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): 30064
Sequence Length: 282
Pathway: Isoprenoid biosynthesis; isopente... |
B9MRD4 | MFKVGIGYDVHRFVEGRKLILGGVEIPFEKGLLGHSDADVLVHAIIDAILGAMGENDIGRLFPDSSPNYKDISSLVLLKEVAKLLEEKNMKIVNIDSTVVSQRPKISPYTNEMKNKIADCLKIESTQVNIKGKTTEGLGFEGREEGISAYAVVLICE | 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-meth... |
A9BHL8 | MLKIGFGYDVHPFAENRRLILGGVVINHPKGYGLLGHSDGDVFFHALIDSLLGMCGLGSIGEYFPESKEFENISSSILLEKTIDLINKRYIVKINNIDVVIISKSVNISSITGQIKNNTSCILNLEVSRINLKGKSGNGLGVGGNDQGIEVYCTILGEIDEI | 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-meth... |
P62368 | MFLKGYTSNVVLIILTFFILLTKEEKNIKNNISGYCFLNFGLKKNAIIKKREKQNLKLFCYNGIRIGQGYDIHKIKVLDEEYNTYANNDFNKNEQSFKTLTLGGVKINNVLVLSHSDGDIIYHSIVDSILGALGSLDIGTLFPDKDEKNKNKNSAIFLRYARLLIYKKNYDIGNVDINVIAQVPKISNIRKNIIKNISTVLNIDESQISVKGKTHEKLGVIGEKKAIECFANILLIPKNS | Cofactor: Binds 1 divalent metal cation per subunit.
Function: In the mevalonate-independent isoprenoid biosynthetic pathway, converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate into 2C-methyl-D-erythritol 2,4-cyclodiphosphate and CMP.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methy... |
B2RGP8 | MKKPFRIGFGFDVHRLSEGYPLWMGGVRLEHSKGLEGHSDADVLIHAICDALLGAAALRDIGYHFPPSDPQYKGIDSKILLARAMELVRSQGYELGNIDATIAAEQPKLNPHIPDMQRVLAEVIQVEVSDISLKATTTEKLGFTGREEGISAYAVALLIAAV | 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-meth... |
Q8K9P4 | MNKYKNIKRRKSNRIYVGNVPIGDGAPISVQSMTNTQTTNIEETIKQIIKLKKVGVDIVRISVPTLEAAESFKIIKLNVDVPLIADIHFDYRLAIKSIKYGADCLRINPGNIGNKRRILDIVNCAKDKNIPIRIGVNAGSLENDLLKKYKSPIPEALVESAIRHIEYLDSLNFNQFKVSVKTSDVFSAIEANEILAKKTVQPIHIGITESGALRNGIVKSSIGITSLLLSGIGDTLRISLAADPVEEVKVGYDILKTLGIRFRGVNFIACPTCSRQEFNVIDVVNQLEKNLEDLSTPMNVSIIGCIVNGIGEAKVSTLGI... | 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 + ... |
B4EAW9 | MQSEAQSPRSSQICSTEPVFGGHQPRRVSHAVDVRWGGQLVTIGGDAPVRVQSMTNTDTADAIGTAIQIKELANAGSELVRITVNTPEAAAAVPAIREQLDRMGVTVPLVGDFHYNGHLLLRDYPGCAESLSKYRINPGNVGQGAKRDTQFAQMIEAAAKYDKPVRIGVNWGSLDQDLLARMMDENGARAQPWDAQSVMYEALIQSAIGSAERAVELGLGRDRIVLSCKVSGVQDLIAVYRELGRRCGFALHLGLTEAGMGSKGIVASTAALGVLLQEGIGDTIRISLTPEPGASRTGEVIVGQEILQTMGLRSFAPMVI... | 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 + ... |
Q7NBH3 | MYTRTKTKKVFVGDVQIGGQNKIVLQSMTIAKTKHVKKSLKEINDLVKEGADLVRIAVFDDADKRAIRKVVDQSPCPIIADIHFNPDYAIAAIKAGCKKIRLNPGNIKSKEKLREICLLANQYNIPIRVGVNSGSIPYDLMREYGVTSTAMIIAAQRYVRMLKRFGFDNIVISLKTSSALLSMQAYELGAKKFSYPLHLGITEAGTLINGTIKSVAGLTPLLLKGIGDTIRISLSTNPVDEIKVAKKMLNSLGLYENLVDVVACPTCGRLNFDLFKVTKEIEEFVKDLHFPLKVSILGCSVNGPGEAKEADIGIAGGKQE... | 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 + ... |
Q73VS3 | MTTGLGMPQTPAPTLAPRRRTRQLMVRDVGVGSDYPISVQSMCTTKTHDVNSTLQQIAELTAAGCDIVRVACPRQEDADALAEIARHSQIPVIADIHFQPKYIFAAIDAGCAAVRVNPGNIKEFDGRVGEVAKAAAAAGIPIRIGVNAGSLDKRFMAKYGKATPEALVESALWEASLFEEHGFSDIKISVKHNDPVVMVAAYEQLAEQCDYPLHLGVTEAGPAFQGTIKSAVAFGALLSRGIGDTIRVSLSAPPVEEVKVGIQILESLNLRPRSLEIVSCPSCGRAQVDVYTLANEVSAGLDGLDVPLRVAVMGCVVNGP... | 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 + ... |
Q89QW7 | MEVYLAQPRGFCAGVVRAIEIVERALEKFGPPVYVRHEIVHNKYVVESLKNKGAIFVEELSEVPPKAVTVFSAHGVARSVEEEAAARDLPVLNATCPLVTKVHNQGKRYITKGRTLILIGHAGHPEVEGTMGQVPAPVLLVQSVEEVNALTLPADTPVAYITQTTLSVDDTRDIISALQARFTDIQGPDIRDICYATQNRQSAVRDLSKLVDVILVVGAANSSNSNRLREIGTEAGVASYLIADGSELNPEWLKDARTVGVTAGASAPEVLVDDVIEAMRRIGPVKVQVLPGREENIEFRLPAELAAS | 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.
Cat... |
Q7NG74 | MQSKNYFRKGFGLKAEVQDDLKAEYESSLIHEIRANGYTLRRGGVTVRLAEAFGFCWGVDKAVSMAYETHRMFAGRQLWITNEIIHNPLVNQHLRAMGIRFLDEDESGRRVPKDFERVSEKDVVILPAFGASTQEMQILDEKNCVIVDTTCPWVSAVWNRVGKYDRAEFTSIIHGKYQHEETVATASRARRYLVVLNLEEAQQVCDYILHGGDRRAFLAHFGMAACEGFDPDRDLVRVGIANQTTMLKGETERIGKLFERTMMRRYGPANLADHFMSHDTICDATQERQDAMFKLVEEPLDLLVVIGGYNSSNTTHLQEI... | 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.
Cat... |
Q5FUH7 | MSEQTTFAPSRTDGVEAHKTLRVLLAGPRGFCAGVDRAIRVVEEALRRYGAPVYVRHEIVHNRTVVEGLEAKGAIFVEELDEVPEDGHVVFSAHGVPKAVPAEAQRRNLLYLDATCPLVSKVHREAERHFAGGGPDQRHILMIGHAGHPEVVGTMGQLPPGAVTLINDAEEARTIQPEDPTKLAFITQTTLSVDDTAEIVDILRSRFPLIEGPKREDICYATTNRQEAVKAIAPESDLVIVIGSPNSSNSQRLREVAERSGARRALLVPKLENLDWSVLEGVETLGISAGASAPESLVQEMVTALAGKYTLKIEERIVKE... | 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.
Cat... |
C4K4R2 | MKILLANPRGFCAGVYRAISIVESALKIYGPPIYVRHEVVHNRYVVEDLRKRGAIFIEHISQVPDGSVLIFSAHGVSQAVKAQAKARQLKILFDATCPLVTKVHMEVLRASRKGQEAILIGHAGHPEVEGTMGQYDNASAGVYLVESVEDVNQLKVKDENNLCFMTQTTLSVDDTLEITSALQKRFPKIIGPRKDDICYATTNRQQAVRELSEKSDMVLVVGSKNSSNSNRLAELAKRMGKPAYLIDSDADIHADWLKNIKYIGVTAGASAPDVLVQKVIITLQSLGADESIEMMGQEENIVFEIPKQLRIHATEISCS | 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.
Cat... |
Q83GJ0 | MEIFSVDWTGQTPPHIPRKSLPRHVAVVMDGNGRWANQRNLPRIEGHKAGESALIDVVAGAVQVGVPYLSLYVFSTENWLRAPDEVRFLLRFTRDVIARRRELFAHWGVRVRWSGVPNRLGKVLVKELRDTEEITKKNTAMNLNVCLNYGSRQEIVNAIKSIVSDVNSGLISAKSVNEKIISRRMYMPDFPDVDLFLRSSGENRMSNFMLWQSAYAELIFMSKLWPDFRRDDFWAALRAYSGRSRRFGR | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 28731
Sequence Length: 249
EC: 2.5.1.-
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Q89KP7 | MSNAAAPATEGPDRSDAPAHVAIIMDGNGRWAAARGLPRAEGHRRGVEALRRVVRASHELGIRYLTIFSFSSENWSRPASEIGDLFGLLRRFIRNDLASLHRDGVKVRIIGERDGLESDICALLNEAEELTRDNSRLTLVVAFNYGSRQEIAKAAQKLAREVAEGRRDPATIDAETLGAHLDAPDIPDPDLIIRTSGEQRLSNFLMWQAAYSELVFVPIHWPDFDKAALEGAIAEFARRERRFGGLVAKTAS | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27807
Sequence Length: 252
EC: 2.5.1.-
|
Q8FNG2 | MSELVPPNIPAEFLPRHIALVMDGNGRWATEKGMKRTEGHRRGEAVLLDVVDACLALGVPYLSAYAFSTENWRRSTEEVRFLMGFNRDVLRRQRDGLHEKGVRVRWVGRRPRLWRSVIRELEAAEELTKDNTNMTLAMCVNYGGRAEIIDAAREIARQAAAGQLRPEQINEKTFPDFLDEPDMPDVDLFLRPSGEKRTSNFLLWQSAYAEMVYQDKLFPDFTPQDLFDAVEEYARRDRRFGTA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 28052
Sequence Length: 243
EC: 2.5.1.-
|
Q8NNC1 | MSEFQVPEIPAQFLPKHIALVMDGNGRWATERGMKRTEGHKRGEAVLLDVVDACIELGVPYLSAYAFSTENWRRSTDEVRFLMGFNRDVLRRQRDDLHEKGVRVRWVGRRPRLWRSVIRELETAEELTKDNTTMTLAMCVNYGGRAEIIDAARDIARLAAEGKLRPEQITEKTFPNFLDEPDMPDVDLFLRPSGEKRTSNFLLWQSAYAEMVYQDKLFPDFTQQDLYDAVLEYAKRDRRFGSA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 28226
Sequence Length: 243
EC: 2.5.1.-
|
Q82BS5 | MVVRGILGRQRREYRAPEPHPSGARAPKLPGELIPNHVACVMDGNGRWAKERGLPRTEGHKVGEGVVMDVLKGCIELGVKNLSLYAFSTENWKRSPEEVRFLMNFNRDVIRRRRDEMDALGIRIRWVGRMPKLWKSVVQELQIAQEQTKDNDAMTLYFCVNYGGRAELADAAKAMAEDVAAGRLDPAKVSEKTIQKYLYYPDMPDVDLFLRPSGEQRTSNYLLWQSSYAEMVFQDVLWPDFDRRDLWRACVEYASRDRRFGGAVPNEQLLEMERDMKGSEGVQDA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 32730
Sequence Length: 285
EC: 2.5.1.-
|
Q9XA06 | MRAKVRAALDALYMKRLVRELEGRPRPQHIGIMLDGNRRWAKMSGIDDPREGYRAGGAKVLDFLRWCDSAQIEHVTLFMLSDDNLARPEEQLNPLIDIIAEVVEQLAAPGNPWPVEAVGALDLLPAESASRLKTATAATQGRKGGTKVDVAVGYGGRREIVDAVRSALTEHSSQGGDIDEFIETFTMEHISKHLYSKTRSESDLIIRTSGEQRLSGFLLWQSAYAEVHFCETYWPDFREIDFLRALRSYSLRERRYGR | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 29164
Sequence Length: 258
EC: 2.5.1.-
|
Q83GG2 | MGGKMLRSVSELIYKVYARYLLGQINLNNLPGHVALIVDGNRRWARKEKRDRISDGHRAGAGKAVDFLHWCDELDINIVTLYLLSNDNLKNRNRQELNDLVQVICDLIAQVSKRWKVNHVGSCENLPELLGNSLEGVKSSTKTNRYSERSMTVNLAIGYSGRAEITEAVRKIVNTYPIGDLPEKITEEVISANLYTGGLSDPDLIIRTSGEQRLSDFMPWQSTHSEFYFLEALGPDLRKVDFLRAIRDFSIRRRSFGA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 29284
Sequence Length: 258
EC: 2.5.1.-
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O67291 | MSLKLPEHVAIIMDGNGRWARQRGLPRVAGHYRGAEVAEDIIEYCIELGIKHLTLFAFSTENWNRPKEEVKALFELMENYIRSKREKLYSLGVRVRLIGRRDRLSRGLVNLMEELESDSKDFKNLFLNVAIDYGGRDDILRAVKKIMEVQPSKLDEETFSQFLDLSCSPDPDLLIRTAGEKRISNFLLWNLAYTELYFTDTLWPDFTREEFMKALEDYSRRKRKFGRVLDE | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27148
Sequence Length: 231
EC: 2.5.1.-
|
Q8GLK9 | MSLKIPEHVAIIMDGNGRWARKRGLPRIAGHYKGAEVAEDIVEFAIELGIKHLTLFAFSTENWNRPKGEVEALFELLRRYLQTKKDKLYKLGIRVRFIGRRDRINKELVKLMQEIEEESKKFKNLFLNLAVDYGGRDDILRAVKKAVKLQREEITEELFSSLLDLSCSPDPDLLIRTAGEKRISNFLLWNLAYTELYFSETLWPDFSREEFLKALEDFSRRKRKFGRVLDE | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27154
Sequence Length: 231
EC: 2.5.1.-
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A0A221J5X6 | MSLSWWRAGAAKKRMDDDESLLVKQQQQQCVALIVGVTGLVGNSLAEMLPLPDTPGGPWKVYGVARRARPSWNEDQPMTYISCDVSNTGEVEAKLSPLSDVTHIFYATWTSRSTEEENCEANGKMLKNVLDAMIPNCPNLKHICLQTGRFHYVASVVDWKINGSHDTPLTEDLPRLKTNNFYYTQEDILLEEVKRKEGLTWSVHRPGTIFGFSPYSMMNLVGTLCVYAAICKQEGAVLRFPGCKGAWDGHSDCADADLIAEQQIWAALDPHAKNQAFNVSNGDLFKWKHLWKVLADQFGVECGDYEEGQQLRLQDVMKDK... | Function: Iridoid synthase that catalyzes the first step in generation of the iridoid ring scaffold using the linear monoterpene (6E)-8-oxogeranial as substrate . Iridoids comprise a large family of distinctive bicyclic monoterpenes that possess a wide range of pharmacological activities, including anticancer, anti-inf... |
P15884 | MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSSDPWSSSSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQT... | Function: Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcript... |
P26771 | QRRCPRIYMECKHDSDCLADCVCLEHGICG | Function: Strong inhibitors of trypsin.
PTM: LLTI-III seems to differ from LLDTI-I by the absence of cyclization of Gln-1.
Sequence Mass (Da): 3455
Sequence Length: 30
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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A3LVK6 | MSTVTFVTGNANKLKEVIAILSGSQSEGGESKVGNFTIVNKSLDLDELQGSIEEVTIHKAKSAAEILGGPVLVEDTCLGFTAFNDLPGPYIKWFVKSVGLQGLVDMLYKFEDKSAKAICTFGYCEGPGKPVQLFQGITKGSIVESRGPTNFGWDSIFQPDGFDKTYAELDKEIKNSISHRFRALDKLRDFLVSQ | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enz... |
Q8IBP3 | MEIYLVTGNMNKKEEFLKMMDEELNVEFVNINLEEIQAQDIVEINEHKVKTAYNILKKQDNNKNKKRYVITDDTGLFISKLNNFPGPYIKWMQKALGSKGIADVVSRLDDNTCHAICTYSVYDGKDVHSFKGITNGKIVEPRGNNKFGWDNIFQPESLSKTFGEMTFDEKQNLSPRFKAFVQLKEFLMNEHKKYNNEF | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enz... |
B2B5Q3 | MTEARHQVNFITGNANKLSEVKAILEPAISVTNQSLDLVEIQGTLEEVTIDKCRRAAELVGGPVLVEDTCLCFDALQDLPGPYIKWFLGSIGHEGLNNMLLAYEDKGAKAVCTFGYSAGPGHEPILFQGITHGKIVPARGPSNFGWDPIFEYEGKTYAEMDKAEKNKISHRSRALAKLQEWFAKEMTA | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enz... |
E3KAB5 | MGALKLVFVTGNANKLREVKKILSTDVSSEDSLKIEVDSKALDLPEVQGSTQDVAREKSRAAAKLIGGPCITEDTALCFKAMGGLPGPYIKWFLEKLGLDGLNKMLQGFSSTEATALCTFAYCEPGKEPILFEGATEGNIVPARGPTNFGWDPIFEVSGTGMTYAEMPAEQKNSLSHRSKALDKLRQHFSRR | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enz... |
Q9UU89 | MTILQSILFVTGNKHKLADVKNILGDRFEIKNHDYDLPEIQGSVKEVVLEKCKAAAEIVKGPVLVEDTWLGYKAMNGLPGPYVKWFLNSVGPDGLYRMVSAFDTKEAQAGCTFGYTKGPGKPIHLFEGILDGQVVPPRGSNGFGWNSIFQPNGHKHTYAEMTDEERNSCSHRYLAAMKLRDFLESEKN | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enz... |
Q4PD06 | MSNPTLTFVTGNANKLREVQQIFSLTPNFPYELTNKDLDLPEIQGTTRDVAQAKCAAAAKALGGACITEDTALGFHALGGLPGPYIKDFMKTIGHDGLNKMLDGFEDRTASAICTFAYCAGPDEQVHLFEGRTEGVIVPPRGPTHFGWDPILEIKGTGLTYAEMDPKQKNTLSHRYKALTLLQDYLVGLSKQN | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enz... |
F6HS55 | MAAAGASASGLILSRPVTFVTGNAKKLEEVRYILGQSIPFNSLKLDLPELQGEPEDISKEKARLAAIQVNGPVLVEDTCLCFNALKGLPGPYIKWFLQKIGHEGLNNLLMAYEDKSAYALCAFSFALGPDAEPVTFLGKTPGKIVPPRGPNDFGWDPIFQPDGYEQTYAEMPKEEKNKISHRYKALALVKSHFAKAGYVFQTDSPI | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enz... |
Q6CDL9 | MSVVFVTGNAGKLRETNHILAPTGIELTSHKLDLEETQGTIEEVSIAKAKAAAKILNKPVLVEDTALGFAALKGLPGVYIKWFLDSLGHEGLNKMLAGFEDKSATAWCTFAYCGGPDEDVLLFQGTCEGTIVPPRGENNFGWNAVFEPKGYTETFAEMSEETKNAISHRFKALEKLKVFLAEKAEQSK | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enz... |
P47119 | MSNNEIVFVTGNANKLKEVQSILTQEVDNNNKTIHLINEALDLEELQDTDLNAIALAKGKQAVAALGKGKPVFVEDTALRFDEFNGLPGAYIKWFLKSMGLEKIVKMLEPFENKNAEAVTTICFADSRGEYHFFQGITRGKIVPSRGPTTFGWDSIFEPFDSHGLTYAEMSKDAKNAISHRGKAFAQFKEYLYQNDF | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and 5-bromodeoxyuridine 5'-t... |
Q9SBA5 | MSDSIQERYLVGYALAAKKQHSFIQPSLIEHSRQRGIDLVKLDPTKSLLEQGKLDCIIHKLYDVYWKENLHEFREKCPGVPVIDLPEAIERLHNRVSMLEVITQLRFPVSDSERFGVPEQVVVMDSSVLSGGGALGELKFPVIAKPLDADGSAKSHKMFLIYDQEGMKILKAPIVLQEFVNHGGVIFKVYVVGDHVKCVKRRSLPDISEEKIGTSKGSLPFSQISNLTAQEDKNIEYGEDRSLEKVEMPPLSFLTDLAKAMRESMGLNLFNFDVIRDAKDANRYLIIDINYFPGYAKMPSYEPVLTEFFWDMVTKKNHV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor ... |
Q89WK5 | MHRRITGKLVIATHNPGKLAEMKELLAPYGIEAVSAGELGLSEPDETGNDFRSNAAIKAIAAAHASKLPSFADDSGIVVDALDGAPGIYSARWAGPTKDFTAAMTRIERLLQERGATAPDKRKAHFVSALCVAWPDDHLEEVEARVDGTLVWPPRGTAGFGYDPMFRPDGHTRTFGEMTSIEKHGLPPLGLALSHRARAFVKLAEICLEPR | 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 ... |
A5E8I8 | MSSSHRKLSGRIVIATHNPGKLAEMRELLAPYGVEAVSAGELSLGEPDETGETFQANARIKAVAAADAAQLPAFADDSGIVVHALDGAPGIYSARWAGPDKDFTAAMTRIERLLQERGATGPDKRGAHFVSALCVAWPDGHVEEVEARVDGTLVWPPRGSAGFGYDPMFLPEGHDRTFGEMTSLEKHGLPPLGLGLSHRARAFVKLAEICLDQR | 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 ... |
P64305 | MRMLEKGKLIVASHNAGKLREFDGLIGPFGFEVSSVAALGLPEPDETGTTFEENAYIKALAAAKATGFPALSDDSGLMVDALDGEPGVYTANWAETEDGKRDFDMAMQKVENLLQEKGATTPDKRKARFVSVICLAWPDGEAEYFRGEVEGTLVWPPRGNIGFGYDPVFLPDGYGKTFGEMTAEEKHGWKPGDASALSHRARAFKLFAEKALNVVSAPAE | 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 ... |
Q62HZ7 | MTMSHASPDAARSRIVLASNNPGKLREFAALFSTAGIDIVPQGELGVSEADEPHATFVENALAKARHASRATGLPAVADDSGLCVPALLGAPGVYSARYAQRAGREKSDAANNAYLVEQLREVADRRAYYYCVLALVRHADDPEPLIAEGRWAGEIVDAPRGAHGFGYDPHFFVPALGATAAELDPAAKNAASHRALALKALVARLGEIR | 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 ... |
Q8RC29 | MLRLIVATHNPNKAKEIKDFFKGYPVEVVSMKELGIEEDIEEYGNTIEENALIKARFLRDKVKEGIVISDDTGLFVEYLGGQPGVYSARFAGENATYEENNRKLLKLLEGVPYEKRKAYFKTIIAVIEGEKEVLLEGVLEGHILDHLQGENGFGYDPVFFVDGIGKTLAELSLEEKNKISHRGKALLKLKEYILKRLEEN | 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 ... |
Q9PMS6 | MKIILATSNKHKVLELKEILKDFEIYAFDEVLMPFEIEENGKTFKENALIKARAVFNALDEKQKKDFIALSDDSGICVDVLEGNPGIYSARFSGKGDDKSNRDKLVNEMIKKGFKQSKAYYVAAIAMVGLMGEFSTHGTMHGKVIDTEKGENGFGYDSLFIPKGFDKTLAQLSVDEKNNISHRFKALELAKIILKILNKG | 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 ... |
Q9ABS4 | MGAKLVAATHNPGKVPEIAALLDGRFEIVTAGQLGLPEPDETESTFVGNALLKARHAADLSGLPALADDSGLSVTALDGAPGIFSARWAGPGKDFALAMKKVEERLEETASDDRTAWFTSALAVAWPNGPAVVVEGRVDGTLVFPGRGTRGFGYDPIFVPEGHALTFGEMEPAAKDAMSHRARAFAKLKAALFD | 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 ... |
Q8DCB9 | MKKIVLATGNQGKVREMADLLADFGFDVVAQSEFNVSEVAETGTTFIENAIIKARHAAKETGLAAIADDSGLEVDFLQGAPGIYSARYAGEKASDQENLEKLLTAMEGVPEAQRTARFHCVLVLMRHENDPTPIVCHGKWEGRILTQAHGDNGFGYDPIFFVPEDNCASAELEPVRKKQLSHRGKALKQLFATLREQPLV | 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 ... |
Q8D3C3 | MKKIILATSNKNKIIEFKKILSELNINTISQKDLGICSIEENKSTFLENALIKARNASKYGFPALSDDSGLIIKTLNGEPGVYSSRFSGNQSNDIKNINMVLKKMLPFKKMDRQACMHCVLIYIRNPNDPIPIISSGTIYGKISNSISKINFGFGYDSIFFLPKKKKTISELTLEEKIKISHRGIAMKKMIKFLKNEKY | 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 ... |
Q8PH61 | MKQLVLASGNAGKLEELRAMLAGLPLRVVAQGELGVEDVPETGLTFVENALIKARHASAVTGLPALADDSGLIVDALDGAPGLYSARYAGSPTNALANNAKLLDAMREVPSDRRSARFYAVIVLLRHPEDPQPLIAEGSWEGVITTQPRGDGGFGYNPVFLDPVYGLTAAEMDTALKNRLSHRAVALATLQHKLHAMSL | 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 ... |
Q9PD73 | MKQLVLASGNAGKLGELRAMLAGVALQITAQSEFGVQDVPETGLTFIENALIKARHACLMTGFPALADDSGLIVDALGGAPGLYSARYAGTPTDAAANNAKLLEMLRDVPVGRRSARFYAVIVLLRHAEDPQPLIADGCWEGEIVFEPCGSGGFGYNPIFFDPLYGMTAAQMGAELKNKISHRARALEQLRDCLHTFMA | 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 ... |
Q8ZHF4 | MQKIVLATGNPGKVRELANLLADFGLDVVAQTELGVESAEETGLTFIENAILKARHAAQTTGLPAIADDSGLAVDALGGAPGIYSARYAGTDASDQENLEKLLVALQNVPDEKRGAQFHCVLVYMRHAEDPTPLVFHGQWPGVIAHQPAGAAGFGYDPIFYVPALGKTAAELTREEKHAVSHRGQALKLMLDALRDA | 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 ... |
Q5NRL7 | MTQTHSSEKRRRLEPGRLVLASHNQGKLREIRELLSPFGLETVSAAELGLPEPVEDGNSFIANAEIKARFVAEKTGSVALADDSGLCVEALDEAPGIYSARWAGEPRDFDKAMEKVHQELTAKGAEASKRAHFVCALSLCWPDGHVENFEGHVWGNLIWPPRGDRGFGYDPMFVADGHQQSFAEIGAEAKKAISHRSEAFKQLLAACLR | 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 ... |
P34273 | MKKHTHHKAYGDSTGKEPLIDLQSIKLWLNSFGNQGHSSEAVLNVLFTLGVILFVIYQVASLLHRMNKRVEKQLESRTKQRKVEVADKHVGDEMVFTDLHENVIRERMIPYRMPVINDDITLRNSQIFYEEMKMRRSCRQFSSRDVPLKVIQNLLKTAGTSPSVGNLQPWTFCVVSSDSIKTMIRKILEADERDNYVSRKKGASWVVDVSQLQDTWRRPYITDAPYLLIVCHEIFRDVHSKTERVFHYNQISTSIAVGILLAAIQNVGLSTVVTSPLNAGPDISRILRRPENESILLLLPLGYASEDVLVPDLKRKPVEH... | Function: May contribute to coordination of muscle contraction as regulatory subunit of the nonessential sup-9 potassium channel complex. May act downstream of sup-10.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37261
Sequence Length: 325
Subcellular Location: Membrane
EC: 1.21.1.-
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Q6PHW0 | MYFLTPILVAILCILVVWIFKNADRSMEKKKGEPRTRAEARPWVDEDLKDSSDLHQAEEDADEWQESEENVEHIPFSHNHYPEKEMVKRSQEFYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNCGPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRKPLDQIMVTV | Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine . During thyroid hormone biosynthesis, facilitates iodide salvage by catalysing the oxidative NADPH-dependent deiodination of the halogenated by-products of thyroid hormon... |
Q9DCX8 | MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV | Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (By similarity). During thyroid hormone biosynthesis, facilitates iodide salvage by catalysing the oxidative NADPH-dependent deiodination of the halogenated by-products of... |
Q6TA49 | MFLLTPVLVAVVCILMVWIFKNADGATKRREEEPRARAEARPWVDEDLKDSTDVLQVEEDADEWQESEEEVEHVPFSHTRYPEKEMVRRSQEFYELLNKRRSVRFISNERVPMEVIDNVIKAAGTAPSGAHTEPWTFVVVKDPDVKHRIREIMEEEEKINYLKRMGPRWVTDLKKLRTNWIKEYWDTAPVLILIFKQVHGFAANGKKKIHYYNEISVSIACGIFLAALQNAGLVTVTTTPFNCGPRLRVFLNRPANEKLLMFLPVGYPSKEATVPDLPRKPLDQIMVTV | Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (By similarity). During thyroid hormone biosynthesis, facilitates iodide salvage by catalysing the oxidative NADPH-dependent deiodination of the halogenated by-products of... |
Q5REW1 | MYFLTPILVAILCILVVWIFKNADRSMEKKKGEARTRAEARPWVDEDLKDSSDLHQAEEDADEWQESEENVEHIPFSHTHYPEKEMVKRSREFYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEGEEEINYMKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFVANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNCGPRLRVLLGRPAHEKLLMLLPVGYPSKEAMVPDLKRKPLDQIMVMV | Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine. During thyroid hormone biosynthesis, facilitates iodide salvage by catalysing the oxidative NADPH-dependent deiodination of the halogenated by-products of thyroid hormone... |
E7FDV5 | MAVFSSLTPVFVAVLCVIIGFLFKNSQRKESRSKQKPSDQTARPWVDEDLQDDTEISTKDNEENNEDWMDTTDEENLPHVPYSPVQYSVSEMLDRSERFYTLMNLRRSVRFISPEPVPKEVIDNVIRTAGTAPSGAHTEPWTFVVVSDTDVKHRIREIIEEEEEINYKQRMGNKWVQDLKRLRTNWVKEYLDVAPYLILVFKQAYGILPSGKKKTHYYNEISVSISCGILLAALQNAGLVTVTTTPLNCGPQLRSLLQRPANEKLLMLLPVGFPASDAKVPDLKRKDLNDIMVLV | Function: Catalyzes the dehalogenation of halotyrosines such as 3,5-diiodo-L-tyrosine . Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity).
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine +... |
Q5XJX0 | MASRAGPRAAGTDGGDFKHREKVASHYQMSASSKSEIKKLTVVHFLIWILVAAQVAVSHLNLVSHDLVAMPYQWEYPYLLSLVPSFIGALAMPKNNISYLVISMISAGLFSVAPLIFGAMEMFPLAQQLYRHGKAYRFIFGFSAVSVMYLLMVIAIQVHAWQIYYSKKLLDAWFNSTLEKKKK | Function: Endoplasmic reticulum transmembrane protein involved in vesicle-mediated transport, which is required for neutrophil function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20578
Sequence Length: 183
Subcellular Location: Endoplasmic reticulum membrane
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Q767F1 | MNNADLYRKSNSLQKRDALRCLEEHANKIKWKKIGDRVIDLGCADGSVTDILKVYMPKNYGRLVGCDISEEMVKYANKHHGFGRTSFRVLDIEGDLTADLKQGFDHVFSFYTLHWIRDQERAFRNIFNLLGDEGDCLLLFLGHTPIFDVYRTLSHTEKWHSWLEHVDRFISPYHDNEDPEKEVKKIMERVGFSNIEVQCKTLFYVYDDLDVLKKSVAAINPFNIPKDILEDFLEDYIDVVREMRLLDRCNNNVGESVSIKFNYKVISVYARKLCLSLM | Function: O-methyltransferase that transfers a methyl group from S-adenosyl-L-methionine (SAM) to the carboxyl group of juvenile hormone acids to produce active juvenile hormones in the corpora allata, the last step during juvenile hormone biosynthesis . Also able to methylate farnesoate to methyl farnesoate .
Catalyti... |
Q9VJK8 | MNQASLYQHANQVQRHDAKLILDEFASTMQWRSDGEDALLDVGSGSGNVLMDFVKPLLPIRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGCERLPEELSGRFDHVTSFYCLHWVQNLKGALGNIYNLLKPEGGDCLLAFLASNPVYEVYKILKTNDKWSTFMQDVENFISPLHYSLSPGEEFSQLLNDVGFVQHNVEIRNEVFVYEGVRTLKDNVKAICPFLERMPADLHEQFLDDFIDIVISMNLQQGENNEDQKFLSPYKLVVAYARKTPEFVNNVFLEPTHQNLVKGIN | Function: O-methyltransferase that transfers a methyl group from S-adenosyl-L-methionine (SAM) to the carboxyl group of juvenile hormone acids to produce active juvenile hormones in the corpora allata, the last step during juvenile hormone biosynthesis . Also able to methylate farnesoate to methyl farnesoate .
Catalyti... |
Q75AL5 | MLQQVTSTTVTGADIQLRAKLLLFSMTDDQCVYCKGKMEHRMWVQCEACPQWVHVQCIPEECLSGGEYPSRSSDIAAFECSAHGTARARLALKGKRRRVEAKEEPERAGTRRYRLRKRGPLDYIALNEGQDVRLRHEHPHRAAFQGCFTKWSGLGRTVTSAELQQSFAELREPVLVADPEHSGMQTPAMDEQVLADVLGADYSLDVMDVQSQQNERWTMGQWKEYMHTARGVRDRIRNVISLEVSHVPEFGQRIRRPRAVEDNDLVDLVWPVQPAPEIGAKPKVQKYVLMSAANAYTDFHLDFAGTSVYYSLLRGAKQFL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.
Catalytic Activity: 2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2... |
Q5A847 | MPINSESCPLCKVHSNTIKKEDEDEEDNKTSWIQCSKCKVWYHVHCLDLPTDEIDQIVIYHCPECVPKYGESTYKRKSKRARVSIDYQSLNEGDTFAIDKSSHFHLHNFLNFKGETNINVIDKLTKTYALNTQMEKPILIPQADLSKNGMQLPIEKNEITIDYITDCCGEDTPLEVMDVISQQGISPPWKLKQWREYFKTNEEKRDRIRNVISLEISDVAKLGVDFTRPKCVRDMDVVDRVWIEEDEQKRSKVTKYCLMSVKNSFTDFHIDFGGTSVYYTVLSGAKTFLFFPPTDNNLELYKSWCLEPSQNFIWYPEYTI... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.
Catalytic Activity: 2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2... |
P0CO40 | MSEQVGQREAVDSPQATGVKTPPEPCPLCRETGPPQPPSITEEGKTNEDIDFIWVACNKCDEWYHSACLFLGDEKWRGTIPKEIISTVETNFGDEGAWTNWVEWIGKWYCAPCLARSTSPSNPRPPRHPLVATMKRASIQPKDIDQAGKPLKRSASTSAPLLKSNIKRPRTSTKGQETASPEIDMKSEREQQAESTAGTPASDAPQGRPKRKTAQIDYRNLNNSIATPTHQWLELIADPEKYGRTILDANYPALPGKLLTRAWLESQPLPGQPSSISPDLLPTRFWGPDREPLIVRPENGGFSSLGGHLPSKDLTVQDVA... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.
Catalytic Activity: 2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2... |
Q6BXJ4 | MPDIDTCPICVESPLEDSTTFNNIAWLQCDICNQWFHASCLKIPKIEVNNLHSYHCEGCSKSHGPSIPKRKSKRSKVQIDYVALNDGDVFAVDKSSHPHVDKFLSFEVNANEIDDKINPYIDFRKDITADYALDTRLTRPVLIPRADLDIVDMKLPIEGKEITIDYIANEVGDDTPLDVMDVLTQQGVNPGWNLGKWRDYYNTDELSRDRIRNVISLEISDVDSFGKSFRRPRIVRDMDLVDKVWNDKSPRPKVTKYCLMSVTGSFTDFHIDFSGTSVYYTVCSGSKTFLMYPPTEQNLDIYTSWCLQPDQNYMWFGDFT... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.
Catalytic Activity: 2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2... |
Q8RWR1 | MSGATTASSGDHNNLRLPTPTLDAESQTLLQSISAEGGYAYARMAVLAVAGDQSAAEAARDMAWEQLHSGPWHSVLPVWRDAYSMACLHVAKIHFAAGEFGEALGALDMGLIMGGMLLRKDLHDSVLLVSSEARKMTKSLEEASGDFKGERLVPEVPVDVNEVRHVLANLQLLVLKILPCRSLTCKRVEKRSGLSLEGFLRDYYLPGTPVVITNSMAHWPARTKWNHLDYLNAVAGNRTVPVEVGKNYLCSDWKQELVTFSKFLERMRTNKSSPMEPTYLAQHPLFDQINELRDDICIPDYCFVGGGELQSLNAWFGPAG... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that demethylates 'Lys-36' (H3K36me) of histone H3 with a specific activity for H3K36me3 and H3K36me2 . Also active on 'Lys-27' (H3K27me) of histone H3 with a specific activity for H3K27me3 and H3K27me2 . No activity on H3K36me1 and H3K27me1 . Invo... |
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