ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q5QM25 | MSRRNAGAMQREGSVKDWEEFDPSPSPKLAYSQSYVAMRGLLTSVASLDLVLMSSSLKSAWAAISSHKHARSLERSRSKGMSLKRAMLQLLVCFMVGIFIGFTPPFSVDLPGKIASENGRLPFDGDAIDRRQMVERQGTKLEPFVAEAESEASSEPQVEEGPPVPAMLDDEADFVEASPIVHSVNDSGIVVRKHLIIITTTSVRPHQAYYLNRLAHVLKDVPPPLLWIVAEWPYQSRETAEILRSSGIMYRHLICNRNTTNIRKIVVCQKNNAIFHIKKHRLDGIVHFADEERAYSADLFEEMRKIRRFGTWPVAIHVGTKYRVVLEGPVCKGNQVTGWHTNQRRGVSRRFPIGFSGFAFNSTILWDPQRWNSPTLESIIVHSGGRGGLQESRFIEKLVEDESQMEGLGDNCTRVMVWNFELEPPQVNYPIGWLLQRNLDAVVPIT | 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.-
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Q9ZQC6 | MGSLERSKKKAQVWKKAVIHFSLCFVMGFFTGFAPAGKASFFSNFETTSYTSTKSPIPPQPFENATYTQHSLLNRTLINSQSQAPAPAESREAEGETRSLSEKEDENQVKVTPRGLVIVVTPIITKDRYKNVLLRRMANTLRLVPPPLLWIVVEKHSDGEEKSSSTMLRKTGIMYRRIVFKEDFTSLESELDHQRNLALRHIEHHKLSGIVHFAGLNNIYDLDFFVKIRDIEVFGTWPMALLSANRKRVVVEGPVCESSQVLGWHLRKINNETETKPPIHISSFAFNSSILWDPERWGRPSSVEGTKQDSIKYVKQVVLEDDTKLKGLPAQDCSKIMLWRLKFPTRTRLST | 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-alpha-D-xylose = [(1->4)-beta-D-xylan](n+1) + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 40059
Sequence Length: 351
Subcellular Location: Golgi apparatus membrane
EC: 2.4.2.24
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Q6Z3Y6 | MASAGGCKKKTGNSRSRSPRSPVVLRRAMLHSSLCFLVGLLAGLAAPSDWPAAAGAAVFLRTLRASNVIFSRSSNRPQQPQLVVVVTTTEQSDDSERRAAGLTRTAHALRLVSPPLLWLVVEEAPAEKHAAPPTARLLRRTGVVHRHLLMKQGDDDFSMQISMRREQQRNVALRHIEDHRIAGVVLFGGLADIYDLRLLHHLRDIRTFGAWPVATVSAYERKVMVQGPLCINTSSSSVITRGWFDMDMDMAAGGERRAAADRPPPETLMEVGGFAFSSWMLWDPHRWDRFPLSDPDASQESVKFVQRVAVEEYNQSTTRGMPDSDCSQIMLWRIQTTL | 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.-
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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 mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (Probable). Exists as two slow interchanging conformational states, a structured (S) and disordered (D) form . May modulate NFS1 desulfurase activity in a zinc-dependent manner . Modulates the interaction between FXN and the cysteine desulfurase complex .
PTM: Phosphorylation at Ser-14 is required for ISCU protein stabilization in the cytosol, whereas dephosphorylation of Ser-14, due to the inhibition of mTORC1 (mammalian target of rapamycin complex 1) complex, leads to degradation of the precursor form and ultimately to a decrease in the mitochondrial mature form.
Sequence Mass (Da): 17999
Sequence Length: 167
Subcellular Location: Mitochondrion
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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 mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5. Exists as two slow interchanging conformational states, a structured (S) and disordered (D) form. May modulate NFS1 desulfurase activity in a zinc-dependent manner. Modulates the interaction between FXN and the cysteine desulfurase complex.
PTM: Cysteine persulfide is reduced by thiol-containing molecules such as glutathione and L-cysteine.
Sequence Mass (Da): 18098
Sequence Length: 168
Subcellular Location: Mitochondrion
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Q4HTS9 | MTTRYRVEYALKTHRRDQFIEWVKGLLAVPFVLYSQPTGVFGDGPSVTQMAEEAHRRYAEIMRDVELMIDDHISRQQDDSMFPSKLRMLIPTAGPFFTRLPLEAAFKYQDRKRYISSRRFVAPSFNDVRQILNSAQSMAVTNGSLQLATFDGDVTLYDDGFNLEPTSPVIPRLLDLLRKNIKIGIVTAAGYTSADRYYERLHGLLDAIAESTDLDPVQKQSIIIMGGEANYLFEYSPSSPCKLAPVPRTQWLTPEMASWSDADITRLLDVAENALRDCVNNLNLPAMIMRKDRAVGIIPKTPGTRIARESLEETVLVVQRILELSSLGSSEERPTKHRPSSPPIPPSVASQSRRVPFCAFNGGNDVFVDIGDKSWGVTVCQQWFGSKENGGAIRGENTLHVGDQFLSAGSNDFKARSVGTTAWIASPAETVELLDELADMMQKKLS | 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 | MTTRYRVEYALKTHRRDQFIEWIKALLAVPFVLYSQPHGVLEDPDRSVDTLSQTREEAHRRYSEIFRDIEAMIDDHIAHQNDAENPFPSKLKLLVPSIGPFFTRLPLEAAFKFQDNKRYISSRRFVSPSFNDIRLILNSAQIMAVTTYGTLQLATFDGDVTLYDDGQSLEPTSPVIPRLLDLLRKNVKIGIVTAAGYTTADRYYSRLHGLLDAMANSADLTPSQKQSLVVMGGEANYLFEFDSSSPHLLAPVPRQHWLTPEMAAWNEQDIAQLLDVAEAALRDCIKTLNLPATLMRKDRAVGIIPVSPEIRIPRESLEETVLLVQKILELSTVGRSRRVPFCAFNGGRDVFVDIGDKSWGVTVCQRWFSQKEGPHGVIKGENTLHVGDQFLSAGANDFRARSVGTTAWIASPVETVELLDELAELMGKKMS | 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 | MKNLDINTFDNIEDIPLGSSEQDPYDFFTLSDRNVMNSDMKKNIVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEMFIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPPTFNEVRHILNLAQILSLEEGLDLLTFDADETLYPDGHDFNDEVLASYISCLLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMGGESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVIKDFGLCAQIQRKEKSIGLVPNKIPSLNIKNEQKNYMIKYEVLEEAVIRIKKEIIKNKITAPYCAFNGGQDLWVDVGNKAEGLLILQKLLKIQKKKCCHIGDQFLHSGNDFPTRFCSLTLWVSNPQETKACLKSIMHLNIKSFIPEVLYENQ | 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 + phosphate
Sequence Mass (Da): 51907
Sequence Length: 444
Subcellular Location: Cytoplasm
EC: 3.1.3.99
|
O14349 | MASRYRVEYALKQHRKDDFIEWIKGLLSVPFVLQAGTPSQKLVTREKEQETLERYAVILRDVEKLIEAHIQIVSEGGSYSQLKMLVPSITIFWTPLPLVKAMYALEPKLCLAKRSFVAPSFNDVRAILGGAQLNYLADNGLDMVSFDGDVTLYEDGQPLLPDNPVISRLIQLLSRGIYVIILTAAGYPSRTGQEYTDRFSGLLQAIEDSDLKDGQKRKLHVLGGESNYLFAYDPLHGLQWVDADSWMLPVMKTWPHDEILEILDTAEETLRSCIQGLNIDAKIVRKERSVGFVPSLGQKLRREQLEEAVLETQATLQIRNFSVPFTAFNGGNDIWCDIGDKKLGVLCLQHFFNISHPSRCLHVGDQFLSAGNNDYKARAAATTVWVSSPHETIEFLDYYFSFLKK | 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
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Q99312 | MSSRYRVEYHLKSHRKDEFIDWVKGLLASPFVLHAVSHEGDYNDDLATTQRVRSQYADIFKDIEGLIKDKIEFDSRNMSQDEIEDGASSQSLNILGQSRLNLLVPSIGTFFTELPLEQAFLWEDSQRAISARRMVAPSFNDIRHILNTAQIFHFKKQENLHNGKVLRLVTFDGDVTLYEDGGSLVYTNPVIPYILKLLRCGINVGIVTAAGYDEAGTYENRLKGLIVALHDSTDIPVSQKQNLTIMGGESSYLFRYYEDPEEDNFGFRQIDKEEWLLPRMKAWSLEDVEKTLDFAERTLNRLRKRLNLPSEISIIRKVRAVGIVPGERYDEASKRQVPVKLDREQLEEIVLTLQNTLESFAPSRRIQFSCFDGGSDVWCDIGGKDLGVRSLQQFYNPESPIQPSETLHVGDQFAPVGSANDFKARLAGCTLWIASPQETVNYLHRLLETD | 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
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D0TZF0 | MASLPHCLSARPLVVAAAPGRPGPGPGPWLRGGARRRNAAFSAGNAGRRVGLRRSVASAVEVGVGEDEEEGVEEEEEEVEAVVMPERYALGGACRVLAGMPAPLGATALDGGVNFAVYSAGASAASLCLFTPDDLEADEVTEEVPLDPLFNRTGNVWHVFIEGELHNMLYGYRFDGMFAPHCGQYFDVSNVVVDPYAKAVISRGEYGVPGPGGDCWPQMAGMIPLPYSTFDWQGDLPLRYPQKDLVIYEMHLRGFTKHSSSNVEHPGTYIGAISKLDYLKELGVNCVELMPCHEFNELEYFSCSSKMNFWGYSTINFFSPMIRYSSGGIRNCGRDAINEFKTFVREAHKRGIEVIMDVVFNHTAEGNEKGPILSFRGIDNSTYYMLAPKGEFYNYSGCGNTFNCNHPVVREFIVDCLRYWVTEMHVDGFRFDLASIMTRGCSLWDPVNVYGSPVEGDMTTTGTPLATPPLIDMISNDPILGDVKLIAEAWDAGGLYQVGQFPHWKIWSEWNGKYRDIVRQFIKGTDGFAGGFAECLCGSPHLYQAGGRKPWHSINFVCAHDGFTLADLVTYNKKYNSSNGEDNRDGENHNLSWNCGEEGEFAGLSVKRLRKRQMRNFFVSLMVSQGVPMFYMGDEYGHTKGGNNNTYCHDHYVNYFRWDKKEESSDLQRFCSLMTKFRKQCESLGLADFPTAQRLHWHGHQPGKPDWSETSRFVAFSTKDETKGEIYVAFNASHLPAVVGLPERPGYRWEPLVDTGKPAPYDFLTDDLPDRAHAVHLFSHFLNSNLYPMLSYSSIILELQPDD | 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 heterooligomer. The heterooligomer ISA1 and ISA2 possesses higher affinity than the ISA1 homooligomer for various branched polyglucans in vitro, but no marked differences exist in chain preferences for debranching of amylopectin and phytoglycogen between these forms .
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.
Sequence Mass (Da): 89661
Sequence Length: 803
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 3.2.1.68
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Q8L735 | MAAWSPSVGIGSCCLNNGITRTWKFPSARLFTGRKNKIKLGSETLMFTRKRFMGDLVTSALQSYQFSKICASKTSIELREALSSRRAEADDLKKVTSYSFRTKAGALVKVKVEKKREKYSILVYVSSLELSGDDKSRLVMVWGVYRSDSSCFLPLDFENSSQDSQTHTTETTFVKSSLSELMLGLEFDGKESPFYLSFHLKLVSGRDPDGQEMLTHRDTDFCIPVGFTAGHPLPLGLSSGPDDDSWNFSFFSRSSTNVVLCLYDDSTTDKPALELDLDPYVNRTGDVWHASVDNTWDFVRYGYRCKETAHSKEDVDVEGEPIVLDPYATVVGKSVSQKYLGSLSKSPSFDWGEDVSPNIPLEKLLVYRLNVKGFTQHRSSKLPSNVAGTFSGVAEKVSHLKTLGTNAVLLEPIFSFSEQKGPYFPFHFFSPMDIYGPSNSLESAVNSMKVMVKKLHSEGIEVLLEVVFTHTADSGALRGIDDSSYYYKGRANDLDSKSYLNCNYPVVQQLVLESLRYWVTEFHVDGFCFINASSLLRGVHGEQLSRPPLVEAIAFDPLLAETKLIADCWDPLEMMPKEVRFPHWKRWAELNTRYCRNVRNFLRGRGVLSDLATRICGSGDVFTDGRGPAFSFNYISRNSGLSLVDIVSFSGPELASELSWNCGEEGATNKSAVLQRRLKQIRNFLFIQYISLGVPVLNMGDECGISTRGSPLLESRKPFDWNLLASAFGTQITQFISFMTSVRARRSDVFQRRDFLKPENIVWYANDQTTPKWEDPASKFLALEIKSESEEEETASLAEPNEPKSNDLFIGFNASDHPESVVLPSLPDGSKWRRLVDTALPFPGFFSVEGETVVAEEPLQQLVVYEMKPYSCTLFETINTTA | 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): 98884
Sequence Length: 882
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
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Q6AU80 | MASLPAPPTPLGSCPRGRGGGRVVARPRRAGLACAARSCYRFRTDDDGVVDVAVSGEDGDGGGGGYAVSVEVPGTRGREGGLVLRASGSGEGVPLAPAAGGASLAAELSFDPTRAPFYLSFLLTDASGAEIRTHRKTSFRVPVGVGPGSPAPLGMSISGDGAVNFAVYSKNANAVSLYLYAAAVGGGGGDEPALEIDLDPYIHRTGNVWHVSLASVDGYVSYAFCCGGIRRPLLDPYAKVIGDFVSSNSVYDEGVTAPSMRCFASLAIAPSYNWGRDRHPRLPLEKLVVYRANVALFTKDRSSGLPDDAAGTFTGLSAKVEHFRSLGVNAILLEPVFPFHQVKGPYFPYHFFSPMNLYSSKGLSVSAIKSMKDMVRVMHRNGIEVLLEVVFTHTAEGESECQTISMRGIDNSSYYIANGIAGCKASILNCNHPVTQKLILDSLRHWVLDFHVDGFCFINAPFLVRGPGGEYLSRPPLLEAITFDPVLSMTKIIADPWSPLDISNVQFPFPHWKRWAEVNTRFSIDVRKFLKREALISDLATRLCGSGDLFSTRGPAFSFNHVSRNSGLSLVDLVSFSNDDLLSESSWNCGEEGPSENSAVLQTRLRQIRNFLFILFVSLGVPVLNMGDECGHSAAGSVSYKDRGPLNWRGMKTTFVKEVTGFISFLTALRSRRGDIFQRREFLKLENIHWYGSDLCEPGWDDPTSNFLCMHINAEVDEMAADSVRGDLYICFNANEESVSAALPALAEGSVWLRLVDTSLAFPGFFATESNPKVQQVPGLSSYHVEAHTCVLFESKSALA | 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 heterooligomer ISA1 and ISA2 possesses higher affinity than the ISA1 homooligomer for various branched polyglucans in vitro, but no marked differences exist in chain preferences for debranching of amylopectin and phytoglycogen between these forms .
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.
Sequence Mass (Da): 86530
Sequence Length: 800
Subcellular Location: Plastid
EC: 3.2.1.68
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Q9M0S5 | MLTSPSSSSTYDPFSSNFSPSLTNAFSSSFTIPMGLKLSRRVTRARIFSRKIKDRSTLKVTCRRAHERVVEEEASTMTETKLFKVSSGEVSPLGVSQVDKGINFALFSQNATSVTLCLSLSQSGKDDTDDDGMIELVLDPSVNKTGDTWHICVEDLPLNNVLYGYRVDGPGEWQQGHRFDRSILLLDPYAKLVKGHSSFGDSSQKFAQFYGTYDFESSPFDWGDDYKFPNIPEKDLVIYEMNVRAFTADESSGMDPAIGGSYLGFIEKIPHLQDLGINAVELLPVFEFDELELQRRSNPRDHMVNTWGYSTVNFFAPMSRYASGEGDPIKASKEFKEMVKALHSAGIEVILDVVYNHTNEADDKYPYTTSFRGIDNKVYYMLDPNNQLLNFSGCGNTLNCNHPVVMELILDSLRHWVTEYHVDGFRFDLASVLCRATDGSPLSAPPLIRAIAKDSVLSRCKIIAEPWDCGGLYLVGKFPNWDRWAEWNGMYRDDVRRFIKGDSGMKGSFATRVSGSSDLYQVNQRKPYHGVNFVIAHDGFTLRDLVSYNFKHNEANGEGGNDGCNDNHSWNCGFEGETGDAHIKSLRTRQMKNFHLALMISQGTPMMLMGDEYGHTRYGNNNSYGHDTSLNNFQWKELDAKKQNHFRFFSEVIKFRHSHHVLKHENFLTQGEITWHEDNWDNSESKFLAFTLHDGIGGRDIYVAFNAHDYFVKALIPQPPPGKQWFRVADTNLESPDDFVREGVAGVADTYNVAPFSSILLQSK | 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 branch linkages in glycogen, amylopectin and their beta-limit dextrins.
Sequence Mass (Da): 86322
Sequence Length: 764
Pathway: Glycan degradation; starch degradation.
Subcellular Location: Plastid
EC: 3.2.1.68
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P10342 | MKCPKILAALLGCAVLAGVPAMPAHAAINSMSLGASYDAQQANITFRVYSSQATRIVLYLYSAGYGVQESATYTLSPAGSGVWAVTVPVSSIKAAGITGAVYYGYRAWGPNWPYASNWGKGSQAGFVSDVDANGDRFNPNKLLLDPYAQEVSQDPLNPSNQNGNVFASGASYRTTDSGIYAPKGVVLVPSTQSTGTKPTRAQKDDVIYEVHVRGFTEQDTSIPAQYRGTYYGAGLKASYLASLGVTAVEFLPVQETQNDANDVVPNSDANQNYWGYMTENYFSPDRRYAYNKAAGGPTAEFQAMVQAFHNAGIKVYMDVVYNHTAEGGTWTSSDPTTATIYSWRGLDNATYYELTSGNQYFYDNTGIGANFNTYNTVAQNLIVDSLAYWANTMGVDGFRFDLASVLGNSCLNGAYTASAPNCPNGGYNFDAADSNVAINRILREFTVRPAAGGSGLDLFAEPWAIGGNSYQLGGFPQGWSEWNGLFRDSLRQAQNELGSMTIYVTQDANDFSGSSNLFQSSGRSPWNSINFIDVHDGMTLKDVYSCNGANNSQAWPYGPSDGGTSTNYSWDQGMSAGTGAAVDQRRAARTGMAFEMLSAGTPLMQGGDEYLRTLQCNNNAYNLDSSANWLTYSWTTDQSNFYTFAQRLIAFRKAHPALRPSSWYSGSQLTWYQPSGAVADSNYWNNTSNYAIAYAINGPSLGDSNSIYVAYNGWSSSVTFTLPAPPSGTQWYRVTDTCDWNDGASTFVAPGSETLIGGAGTTYGQCGQSLLLLISK | 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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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A4D126 | MEAGPPGSARPAEPGPCLSGQRGADHTASASLQSVAGTEPGRHPQAVAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRISLVEAGVTRHRSIFNGLKALAEDQINSKLSKPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERARHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTECLQLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKERISQEICVVMDTEEDNKHVGHLLEEVLKSELNHVKVTSEALGHAGRHLQQIILDQCYNFVCVNVTTSDFQETQKLLSMLEESSLCILYPVVVVSVHFLDFKLVPPSQKMENLMQIREFAKEVKERNILLYGLLISYPQDDQKLQESLRQGAIIIASLIKERNSGLIGQLLIA | 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-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity . Shows activity toward other pentose phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively . Not Involved in dolichol production .
Catalytic Activity: CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol + diphosphate
Sequence Mass (Da): 49873
Sequence Length: 451
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cytoplasm
EC: 2.7.7.40
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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 biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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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; 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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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; 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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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; 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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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; 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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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; 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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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
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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; 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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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; 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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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; 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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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-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): 17205
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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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-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): 17567
Sequence Length: 162
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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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-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 27161
Sequence Length: 240
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Subcellular Location: Plastid
EC: 4.6.1.12
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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-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): 17622
Sequence Length: 162
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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Q8K9P4 | MNKYKNIKRRKSNRIYVGNVPIGDGAPISVQSMTNTQTTNIEETIKQIIKLKKVGVDIVRISVPTLEAAESFKIIKLNVDVPLIADIHFDYRLAIKSIKYGADCLRINPGNIGNKRRILDIVNCAKDKNIPIRIGVNAGSLENDLLKKYKSPIPEALVESAIRHIEYLDSLNFNQFKVSVKTSDVFSAIEANEILAKKTVQPIHIGITESGALRNGIVKSSIGITSLLLSGIGDTLRISLAADPVEEVKVGYDILKTLGIRFRGVNFIACPTCSRQEFNVIDVVNQLEKNLEDLSTPMNVSIIGCIVNGIGEAKVSTLGIVGGSKTSALYKDGIRQKNKLKNQEIIKELEIKIRKKAKSLDKLKKII | 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): 40440
Sequence Length: 367
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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B4EAW9 | MQSEAQSPRSSQICSTEPVFGGHQPRRVSHAVDVRWGGQLVTIGGDAPVRVQSMTNTDTADAIGTAIQIKELANAGSELVRITVNTPEAAAAVPAIREQLDRMGVTVPLVGDFHYNGHLLLRDYPGCAESLSKYRINPGNVGQGAKRDTQFAQMIEAAAKYDKPVRIGVNWGSLDQDLLARMMDENGARAQPWDAQSVMYEALIQSAIGSAERAVELGLGRDRIVLSCKVSGVQDLIAVYRELGRRCGFALHLGLTEAGMGSKGIVASTAALGVLLQEGIGDTIRISLTPEPGASRTGEVIVGQEILQTMGLRSFAPMVIACPGCGRTTSTLFQELAMQIQTYLREQMPVWRKEYPGVEKMNVAVMGCIVNGPGESKHANIGISLPGSGENPAAPVFIDGEKVKTLRGERIAEEFQQIVSDYVARNYGRTEALN | 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): 46602
Sequence Length: 434
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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Q7NBH3 | MYTRTKTKKVFVGDVQIGGQNKIVLQSMTIAKTKHVKKSLKEINDLVKEGADLVRIAVFDDADKRAIRKVVDQSPCPIIADIHFNPDYAIAAIKAGCKKIRLNPGNIKSKEKLREICLLANQYNIPIRVGVNSGSIPYDLMREYGVTSTAMIIAAQRYVRMLKRFGFDNIVISLKTSSALLSMQAYELGAKKFSYPLHLGITEAGTLINGTIKSVAGLTPLLLKGIGDTIRISLSTNPVDEIKVAKKMLNSLGLYENLVDVVACPTCGRLNFDLFKVTKEIEEFVKDLHFPLKVSILGCSVNGPGEAKEADIGIAGGKQEGIIFKKGVVVKSVKQEYLVDELKQMILEEYELFKKKNGK | 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): 39607
Sequence Length: 359
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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Q73VS3 | MTTGLGMPQTPAPTLAPRRRTRQLMVRDVGVGSDYPISVQSMCTTKTHDVNSTLQQIAELTAAGCDIVRVACPRQEDADALAEIARHSQIPVIADIHFQPKYIFAAIDAGCAAVRVNPGNIKEFDGRVGEVAKAAAAAGIPIRIGVNAGSLDKRFMAKYGKATPEALVESALWEASLFEEHGFSDIKISVKHNDPVVMVAAYEQLAEQCDYPLHLGVTEAGPAFQGTIKSAVAFGALLSRGIGDTIRVSLSAPPVEEVKVGIQILESLNLRPRSLEIVSCPSCGRAQVDVYTLANEVSAGLDGLDVPLRVAVMGCVVNGPGEAREADLGVASGNGKGQIFVRGEVIKTVPESQIVETLIEEAMRIAAQMNSEGGPEATSSGSPVVTVS | 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): 40808
Sequence Length: 388
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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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.
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): 33269
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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Q7NG74 | MQSKNYFRKGFGLKAEVQDDLKAEYESSLIHEIRANGYTLRRGGVTVRLAEAFGFCWGVDKAVSMAYETHRMFAGRQLWITNEIIHNPLVNQHLRAMGIRFLDEDESGRRVPKDFERVSEKDVVILPAFGASTQEMQILDEKNCVIVDTTCPWVSAVWNRVGKYDRAEFTSIIHGKYQHEETVATASRARRYLVVLNLEEAQQVCDYILHGGDRRAFLAHFGMAACEGFDPDRDLVRVGIANQTTMLKGETERIGKLFERTMMRRYGPANLADHFMSHDTICDATQERQDAMFKLVEEPLDLLVVIGGYNSSNTTHLQEIAVERGLPSFHIDGADRLVSAQFIEHRDLHSKSLVRTKNWLPAGEVTVGVTAGASTPDRVVAEVIARIFELKGVGESGATGAISSPVLSSAEGGPSLS | 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): 46492
Sequence Length: 417
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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Q5FUH7 | MSEQTTFAPSRTDGVEAHKTLRVLLAGPRGFCAGVDRAIRVVEEALRRYGAPVYVRHEIVHNRTVVEGLEAKGAIFVEELDEVPEDGHVVFSAHGVPKAVPAEAQRRNLLYLDATCPLVSKVHREAERHFAGGGPDQRHILMIGHAGHPEVVGTMGQLPPGAVTLINDAEEARTIQPEDPTKLAFITQTTLSVDDTAEIVDILRSRFPLIEGPKREDICYATTNRQEAVKAIAPESDLVIVIGSPNSSNSQRLREVAERSGARRALLVPKLENLDWSVLEGVETLGISAGASAPESLVQEMVTALAGKYTLKIEERIVKEENINFRLPGPLAGEDD | 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): 36555
Sequence Length: 336
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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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.
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): 35154
Sequence Length: 319
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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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.-
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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.-
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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.-
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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.-
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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.-
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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.-
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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 | MSLSWWRAGAAKKRMDDDESLLVKQQQQQCVALIVGVTGLVGNSLAEMLPLPDTPGGPWKVYGVARRARPSWNEDQPMTYISCDVSNTGEVEAKLSPLSDVTHIFYATWTSRSTEEENCEANGKMLKNVLDAMIPNCPNLKHICLQTGRFHYVASVVDWKINGSHDTPLTEDLPRLKTNNFYYTQEDILLEEVKRKEGLTWSVHRPGTIFGFSPYSMMNLVGTLCVYAAICKQEGAVLRFPGCKGAWDGHSDCADADLIAEQQIWAALDPHAKNQAFNVSNGDLFKWKHLWKVLADQFGVECGDYEEGQQLRLQDVMKDKGPVWDKIVAENGLSNTKLEDVGKWWFSDTILWNECRLDSMNKSKEHGFLGFRNSKNCFLYWIHKVKAYNLVPSTYT | 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-inflammatory, antifungal and antibacterial activities (Probable). Catalyzes the conversion of the linear monoterpene (6E)-8-oxogeranial to (S)-8-oxocitronellyl enol, a precursor of nepetalactones, which are metabolites that are both insect-repellent and have euphoric effect in cats .
Catalytic Activity: (S)-8-oxocitronellyl enol + NADP(+) = (6E)-8-oxogeranial + H(+) + NADPH
Sequence Mass (Da): 44843
Sequence Length: 396
EC: 1.3.1.122
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P15884 | MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSSDPWSSSSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAMPGGHGDMHGIIGPSHNGAMGGLGSGYGTGLLSANRHSLMVGTHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDASNHMGQM | 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 transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'.
Sequence Mass (Da): 71308
Sequence Length: 667
Domain: the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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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 enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21181
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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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 enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 23080
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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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 enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 20698
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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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 enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 20845
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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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 enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 20978
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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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 enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21018
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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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 enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 22547
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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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 enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 20483
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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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'-triphosphate (BrdUTP) to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 22093
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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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 of plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is not (By similarity). Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway .
Catalytic Activity: 1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+)
Sequence Mass (Da): 36220
Sequence Length: 319
EC: 2.7.1.134
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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 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): 22761
Sequence Length: 211
EC: 3.6.1.66
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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 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): 22849
Sequence Length: 214
EC: 3.6.1.66
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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 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): 23795
Sequence Length: 220
EC: 3.6.1.66
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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 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): 22179
Sequence Length: 210
EC: 3.6.1.66
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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 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): 22691
Sequence Length: 200
EC: 3.6.1.66
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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 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): 22375
Sequence Length: 200
EC: 3.6.1.66
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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 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): 20299
Sequence Length: 194
EC: 3.6.1.66
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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 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): 21924
Sequence Length: 200
EC: 3.6.1.66
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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 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): 22534
Sequence Length: 199
EC: 3.6.1.66
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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 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): 21088
Sequence Length: 199
EC: 3.6.1.66
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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 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): 21238
Sequence Length: 199
EC: 3.6.1.66
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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 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): 20906
Sequence Length: 197
EC: 3.6.1.66
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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 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): 22937
Sequence Length: 209
EC: 3.6.1.66
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P34273 | MKKHTHHKAYGDSTGKEPLIDLQSIKLWLNSFGNQGHSSEAVLNVLFTLGVILFVIYQVASLLHRMNKRVEKQLESRTKQRKVEVADKHVGDEMVFTDLHENVIRERMIPYRMPVINDDITLRNSQIFYEEMKMRRSCRQFSSRDVPLKVIQNLLKTAGTSPSVGNLQPWTFCVVSSDSIKTMIRKILEADERDNYVSRKKGASWVVDVSQLQDTWRRPYITDAPYLLIVCHEIFRDVHSKTERVFHYNQISTSIAVGILLAAIQNVGLSTVVTSPLNAGPDISRILRRPENESILLLLPLGYASEDVLVPDLKRKPVEHITKLY | 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 hormone production, monoiodotyrosine (L-MIT) and diiodotyrosine (L-DIT) . The scavanged iodide can then reenter the hormone-producing pathways . Acts more efficiently on 3-iodo-L-tyrosine than 3,5-diiodo-L-tyrosine .
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33360
Sequence Length: 289
Subcellular Location: Cell membrane
EC: 1.21.1.1
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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 thyroid hormone production, monoiodotyrosine (L-MIT) and diiodotyrosine (L-DIT) . The scavanged iodide can then reenter the hormone-producing pathways (By similarity). Acts more efficiently on 3-iodo-L-tyrosine than 3,5-diiodo-L-tyrosine (By similarity).
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32814
Sequence Length: 285
Subcellular Location: Cell membrane
EC: 1.21.1.1
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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 thyroid hormone production, monoiodotyrosine (L-MIT) and diiodotyrosine (L-DIT) . The scavanged iodide can then reenter the hormone-producing pathways (By similarity). Acts more efficiently on 3-iodo-L-tyrosine than 3,5-diiodo-L-tyrosine (By similarity).
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33462
Sequence Length: 289
Subcellular Location: Cell membrane
EC: 1.21.1.1
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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 production, monoiodotyrosine (L-MIT) and diiodotyrosine (L-DIT). The scavanged iodide can then reenter the hormone-producing pathways. Acts more efficiently on 3-iodo-L-tyrosine than 3,5-diiodo-L-tyrosine.
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33365
Sequence Length: 289
Subcellular Location: Cell membrane
EC: 1.21.1.1
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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 + H(+) + 2 NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33685
Sequence Length: 295
Subcellular Location: Membrane
EC: 1.21.1.1
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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 .
Catalytic Activity: (2E,6E)-farnesoate + S-adenosyl-L-methionine = methyl (2E,6E)-farnesoate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32546
Sequence Length: 278
EC: 2.1.1.325
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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 .
Catalytic Activity: (2E,6E)-farnesoate + S-adenosyl-L-methionine = methyl (2E,6E)-farnesoate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34065
Sequence Length: 297
EC: 2.1.1.325
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Q75AL5 | MLQQVTSTTVTGADIQLRAKLLLFSMTDDQCVYCKGKMEHRMWVQCEACPQWVHVQCIPEECLSGGEYPSRSSDIAAFECSAHGTARARLALKGKRRRVEAKEEPERAGTRRYRLRKRGPLDYIALNEGQDVRLRHEHPHRAAFQGCFTKWSGLGRTVTSAELQQSFAELREPVLVADPEHSGMQTPAMDEQVLADVLGADYSLDVMDVQSQQNERWTMGQWKEYMHTARGVRDRIRNVISLEVSHVPEFGQRIRRPRAVEDNDLVDLVWPVQPAPEIGAKPKVQKYVLMSAANAYTDFHLDFAGTSVYYSLLRGAKQFLLFPPTPANLGAYKAWCADDNQGLIFLGDRLQDGVSFSLRPGDLFMIPSGFIHAVYTPEDSFVVGGNYLCLRDLSTHIRIVRIEQETQVPKKFTFPKFERVMGLTAEWLLEGLPERLQLITHEHAVALLDYLRDTRLKYKPAHYHTKSTMLASLEKALEGCEPASGP | 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 succinate
Sequence Mass (Da): 55050
Sequence Length: 486
Domain: The JmjC domain mediates the demethylation activity.
Subcellular Location: Nucleus
EC: 1.14.11.27
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Q5A847 | MPINSESCPLCKVHSNTIKKEDEDEEDNKTSWIQCSKCKVWYHVHCLDLPTDEIDQIVIYHCPECVPKYGESTYKRKSKRARVSIDYQSLNEGDTFAIDKSSHFHLHNFLNFKGETNINVIDKLTKTYALNTQMEKPILIPQADLSKNGMQLPIEKNEITIDYITDCCGEDTPLEVMDVISQQGISPPWKLKQWREYFKTNEEKRDRIRNVISLEISDVAKLGVDFTRPKCVRDMDVVDRVWIEEDEQKRSKVTKYCLMSVKNSFTDFHIDFGGTSVYYTVLSGAKTFLFFPPTDNNLELYKSWCLEPSQNFIWYPEYTITKNKKKIKPTGGFKVDLQPGDLFIIPSGWIHAVHTPQDSIVIGGNYLTIRDMVMQLKINEIERETKVPTKFRFPMFNKVLWLTAWYYYNHQNEFQSDIGEDEDGNAILTRLIGHLQGHLELSKTNATAKRSIPKTIGKPMVFINKLLAWKEDLYGTAV | 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 succinate
Sequence Mass (Da): 55460
Sequence Length: 478
Domain: The JmjC domain mediates the demethylation activity.
Subcellular Location: Nucleus
EC: 1.14.11.27
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P0CO40 | MSEQVGQREAVDSPQATGVKTPPEPCPLCRETGPPQPPSITEEGKTNEDIDFIWVACNKCDEWYHSACLFLGDEKWRGTIPKEIISTVETNFGDEGAWTNWVEWIGKWYCAPCLARSTSPSNPRPPRHPLVATMKRASIQPKDIDQAGKPLKRSASTSAPLLKSNIKRPRTSTKGQETASPEIDMKSEREQQAESTAGTPASDAPQGRPKRKTAQIDYRNLNNSIATPTHQWLELIADPEKYGRTILDANYPALPGKLLTRAWLESQPLPGQPSSISPDLLPTRFWGPDREPLIVRPENGGFSSLGGHLPSKDLTVQDVANLVGPDRMVDVIDVSSQHSSQWTLQKWAEYIQSSSGNTSVRNPKVYNVISLEISGTELAKKVKPPKIVREIDWVDNFWRFNAGAGGKDVKEKGRGNDSREGSEIRKEGSHLTEGDNAGGEIEEDLEGLKEKTNTPYPKVQLYCLMGMKGAWTDWHVDFAASSVYYTIHSGAKVKLSCFVSFFSPGSYHSQVFFFVKPTEQNLKAYAEWSGSYEKQQDTWLGDMVDEVRKVELHAGDTMIIPTGYIHAVYTPMDSIVFGGNFLHSYNVDTQLRLRQIEIDTKVPQRFRFPMFDRLCWYVAEKYCSDLRHLRAYRPRATTTPKPPHFRVLQCLSYLANFLVSQTGILEDPEAEDKARKLVHDRIPGDIVKDPEGLAKELKWRVERELGALGLLGEEASGVEAEEFKSNGTANGSVKIKGKEVSRKRDRLSKVFDKKAISRTWDFHPPAWSENRQSPQIETTTVQLPRPSTSSSDAISGSGPGASPGASANGGANENEQAELTTMLVKQTRKRMRELDDGTVIEESQETTFVEKKTIWGPKLDKEKISQPQGKVEEDMDIDH | 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 succinate
Sequence Mass (Da): 98240
Sequence Length: 879
Domain: The JmjC domain mediates the demethylation activity.
Subcellular Location: Nucleus
EC: 1.14.11.27
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Q6BXJ4 | MPDIDTCPICVESPLEDSTTFNNIAWLQCDICNQWFHASCLKIPKIEVNNLHSYHCEGCSKSHGPSIPKRKSKRSKVQIDYVALNDGDVFAVDKSSHPHVDKFLSFEVNANEIDDKINPYIDFRKDITADYALDTRLTRPVLIPRADLDIVDMKLPIEGKEITIDYIANEVGDDTPLDVMDVLTQQGVNPGWNLGKWRDYYNTDELSRDRIRNVISLEISDVDSFGKSFRRPRIVRDMDLVDKVWNDKSPRPKVTKYCLMSVTGSFTDFHIDFSGTSVYYTVCSGSKTFLMYPPTEQNLDIYTSWCLQPDQNYMWFGDFTKAFKGKGCTPSGGFKVTLSPGDLFIIPSGWIHAVFTPEDSLVIGGNFLTLMDLSMHLRIYEIEKVTRVPAKFRFPMFNRVLWLTSWYYYNNKSQFLKDLGQDAHIKNEAHIKSEAHSRGEVHTKTETHAVKDEPQPDQSVQYKTLSCLVSHLQSHYESSKINKVARNTIPAGLIGKDIPGYLAKLQSWLDELSP | 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 succinate
Sequence Mass (Da): 58685
Sequence Length: 514
Domain: The JmjC domain mediates the demethylation activity.
Subcellular Location: Nucleus
EC: 1.14.11.27
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Q8RWR1 | MSGATTASSGDHNNLRLPTPTLDAESQTLLQSISAEGGYAYARMAVLAVAGDQSAAEAARDMAWEQLHSGPWHSVLPVWRDAYSMACLHVAKIHFAAGEFGEALGALDMGLIMGGMLLRKDLHDSVLLVSSEARKMTKSLEEASGDFKGERLVPEVPVDVNEVRHVLANLQLLVLKILPCRSLTCKRVEKRSGLSLEGFLRDYYLPGTPVVITNSMAHWPARTKWNHLDYLNAVAGNRTVPVEVGKNYLCSDWKQELVTFSKFLERMRTNKSSPMEPTYLAQHPLFDQINELRDDICIPDYCFVGGGELQSLNAWFGPAGTVTPLHHDPHHNILAQVVGKKYIRLYPSFLQDELYPYSETMLCNSSQVDLDNIDETEFPKAMELEFMDCILEEGEMLYIPPKWWHYVRSLTMSLSVSFWWSNEAESSSS | 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 . Involved in the control of flowering time by demethylating H3K36me2 at the FT locus and repressing its expression . Acts within the central clock and contributes, in parallel with LUX, to temperature compensation, probably as a component of the evening complex, to maintain circadian period at increasing temperatures; this mechanism involves binding to and regulation of CCA1 and PRR7 promoters . Works in concert with TOC1 to promote the morning-phased clock genes CCA1 and LHY which function as components of the central oscillator . Together with JMJ32, regulates the flowering-repressor FLOWERING LOCUS C (FLC) locus by removing the repressive histone modification H3 lysine 27 trimethylation (H3K27me3), especially at elevated temperatures (e.g. 29 degrees Celsius), thus preventing extreme precocious flowering . JMJ30 and JMJ32 are regulators involved in the integration of abscisic acid (ABA) and brassinosteroids (BR) signaling pathways . Together with JMJ32, controls ABA-mediated growth arrest during the post-germination stage in unfavorable conditions, and responses to ABA during root development, via the removal of repressive histone mark (H3K27me3) from the SnRK2.8 promoter, thus promoting SnRK2.8 expression and subsequent kinase-dependent ABI3 activation . In addition, removes the repressive histone marks (H3K27me3) from the BZR1 locus in response to stress and ABA, thus activating the BR signaling pathway which, in turn, inhibits the ABA signaling pathway . Able to drive tissue identity changes to promote callus formation form somatic cells via a massive genome-wide chromatin remodeling (e.g. H3K9me3 demethylation) leading to the induction of Lateral organ Boundaries-Domain (LBD) genes (e.g. LBD16 and LBD29) that establish root primordia; when in complex with ARF proteins (e.g. ARF7 and ARF19), recruits ATXR2 which promotes the deposition of H3K36me3 at LBD genes promoters, thus ensuring their stable activation during callus formation .
Catalytic Activity: 2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(36)-[histone H3] + 2 succinate
Sequence Mass (Da): 48075
Sequence Length: 429
Subcellular Location: Nucleus
EC: 1.14.11.27
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