ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B8NI20 | MIENLRKRSTIEVEWRKQPVHMDIDLDQVDNPEAYPITVSVETSKDGSDPGLLWQPMHAERDSIVKETIHAKYVLGCDGARSWIRQRLGVSFIGDLTDSTWGVMDIVPKTSFPDIRKVAVIHSSKGTVMSVPREDKLVRFYIQIDAVNPNAASGLARRDLKVEDLLDAARAIMFPYTMEAAECAWWSAYRVGQRVANEFARHDRIFLAGDSVREYCLEVIRCQ | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination . ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors . N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline . Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation . The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH . Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins .
Sequence Mass (Da): 25367
Sequence Length: 223
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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B8NI21 | MTAPADSTEKSETSETTTLQTTEVSTVDVDPDLPRVLAKVPGTVWVVAFIAAAERFTYWGITTPWQLHAKPPQASEFARCIRPRRSESIHDIQCLHVFLLFNTNSFRDNLGRLSRSLSDIAPEFDKRFRKLPPTGNILPKAGSVLSCAIRGRFQLDAAMPSYQREHFAKEVSWDETFVNEIRRGLVACRVILGFILFFTCLSQASNNLISQAGQMKTYGIPNDTITAMNPIFCVIMGPVIQKGLYPLLNKNNVKFQSITRMATGFIMMSASMAFAAGVQKIIYDTGPCYDRPLTCPGAENGRIPNQVNVFLQTPTYIILAVAEIFSFVTLSEYTYTKAPTDMKAVVQALGQLGAAAGSAIGIAITPLAHDPSLIWMYTGLAVAMFLVAVVFWILFKKYNAIDREDK | Function: Peptide transporter; part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44932
Sequence Length: 406
Subcellular Location: Membrane
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B8NI22 | MTMLSDLPKIPTLDWADFAEGDTDQRLKLAQGLVQGFKRFGFVKLVNHGLSDELIQQLFAEVKRFYRLPDELKQKAAHPPGPNPQRGWSGIGVESTSKLYGEQTERPSGKLKDAKVGTDFSSSKLSRELTHMKEHYDIGPPTDTQFPTRWPDEQDIPGWRAFMESYYARGQSFCLDLMEALEIGLELPKNTLRSMCIPDGSELRLLHYPEIPAAELRTGDTARIWPHTDFGLITLLFQDGVGGLEVEDPLQQGHYIEVAREQPYEMIVNVSATFERWMNGVIKAAVHRVNITPEGKHVEDAVVPERWSAAYFFKAHKMAHAGPLPAFVTPERPALYDNITALEFQKRRTDLVYTGQQLKVEEAA | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination . ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors . N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline . Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation . The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH . Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins .
Sequence Mass (Da): 41194
Sequence Length: 364
Pathway: Secondary metabolite biosynthesis.
EC: 1.14.-.-
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B8NI23 | MMTEAQGPVVSIGSATVTYDHPPIISPVSYPKARPTQILDIRKRTSRIDLYHEILAGLRAKDKELPSLLLWNDRGLDLFSEILNSDEYYPRRRETQLLQTHVNEFTRSISSGERLIELGAGNLQKTVSVLRCLEQSRKHVEYCALDVSHAALQASITELKAQLPFASYVTIRGLLGTYNDCASWLKQSGATVRTTFLWLGNSIANFEPEDATSILADFLQTKASPSHSPQMIIAVDGCQDVEQILEAYDMPNKLSQKFVFNGLSHANQILGSEVFRPQHWTFEGKWNPVKSMHESFYVAKKPMSLDIGNERFHVHAGEKIRAITSGKWPKDKVTSICQSAGIKVLKGWTDEEGSYGKRVTQVYSRGSSC | Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination . ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors . N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline . Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation . The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH . Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins .
Sequence Mass (Da): 41349
Sequence Length: 369
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
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B8NI24 | MTATTTTTSQIFVSEDYNQDPNWYAVDNYTLSHLQPPTRPNHASLHQTLENSAKRGLEDISAFPTQAKFMALQCQLGGVKHALEVGTLGGYTAIYIASLNPDIRIVSIEIDPKSAEVAKENIAAAGYQDRIEVLVGAAIDLLPILQAKVENGEQERFGFTFIDANKDNGWDYFDYAVKMSRPRASIIVDNVVRAGKLVQEDYIKNDINVRGSRRTVENVGKDDRVDAVVLQTLSEKSYDGFLMAVVK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination . ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors . N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline . Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation . The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH . Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins .
Sequence Mass (Da): 27359
Sequence Length: 247
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
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B8NI25 | MPAPKSIIIVGSGVFGLSTAHAMSQNNEFASSKITLIDSWNFEPSGPSASAPNPSAANFDTSRIIRSDYSHRTYATLAREAQQKWKADWGADGRYRNQSIVMIGEGHSMKQPMKALESINYVKHAYAQSYERAGRNSDIVHILDSESAVWEALGLGTPDEASKAGPNASELRGYRNHNCGWAESGATMAWLRQKTIHSDRIDIHIGQVVGLRVCSDSPSESHVNAEPRVCGVILDDGSQLTADLTVLAAGAMTPRLLGSPTLCDVYSETVAYVQLTEMERRELVRREFPLIVNVARKIFAIGPDNQGFLKLARFSWSGYRDVQKFAGVDVGPRSQAAPQEEDGYGACGDLDQTKLSPDVESTLQDYRGFLRELFRSGDGGDLGGLRNIATRPFAQVRRCWYADTVSTDFIVDYHPAYGKSLFIATGGSDHAFKFLPVLGERICELILQSDNGKAGPSESIQELQRLWKFPGGDSHAKL | Function: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination . ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors . N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline . Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation . The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH . Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins .
Sequence Mass (Da): 52382
Sequence Length: 478
Pathway: Secondary metabolite biosynthesis.
EC: 1.5.3.-
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B8NI27 | MVNQAFMLWCYITPVLGAVVAEQYIGRVKTIIFSSSVYLCGLVTLFLSSLPTAYAMGISLPGLLVSLFLIGIGTGGIKTNVSSLIAEQYTGPKESRRILKSGEEVIVDRDLTIQRIFTTFFLYINIGSFSPLLITIIEKEYGFSAAFSLSAITFSIGFIIVLVSRHLYISRDPDSSIIFNACKAFWIAIKHKGNLDYARPSYQTEQAATRRLSWDDSFIDDLRRAIASCKIFILYPIYWAAYSQFLTNFISQAATMETHGVPNDIMTNIDPITVLILLPVLDRIVFPFLRRQGVPVRHVDRITIGMPDFQPFVQESYQICQRTCFQIISAIELGLGLQAGRLTQCCQPAASEIRLLYYPPTTKNLFDEGLKKRAWPHTDLGIITLLFQDMVGGLEVEDRAAGKPRSFIPVKRVSPNEMIVNTSDSLQRWTNNVIRAGLHQVTAPDAAKLSNGVDMLPARCSSVFFFKAGRDTSVGPLPEFVTEDRPAAFEDMTALQYQQLKTRILHGVEG | Function: Peptide transporter; part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56962
Sequence Length: 510
Subcellular Location: Membrane
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A0A0D4BS77 | MTRTDFAQSAVASIFTGAIASHAAVLADDLGLFDALAKGKLRNRDLDRSPWLRNRIRISGALEALCRVGAVQRCTDGYELTDVGTELAGQVPVFRLWLGGYASVLAGQISIGADPATGVHGGIVAESSGAIGARYLDETIVNLLESLRPEGRICDIGCGTGARLLRVCRRVNQPGIGYDLSAKAVEAARETVDEARRIGVDIDVRQGDATALTQDHPDVDIVTQAFMTHHIAPDEYCAAVLRSYRSRFPRARYLVIFDTVPSQDSEEPEIFAPGFDYIHALQNMEPRSRGAARRMFTEAGYICREEVELAVPNSYAWVLEMRDREGPAS | Function: Involved in the biosynthesis of the antibiotic indolmycin, an inhibitor of the bacterial tryptophan-tRNA synthetases. Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to position 3 of the aliphatic side chain of (indol-3-yl)pyruvate to yield 3-methylindolepyruvate.
Catalytic Activity: indole-3-pyruvate + S-adenosyl-L-methionine = (R)-3-(indol-3-yl)-2-oxobutanoate + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35840
Sequence Length: 329
EC: 2.1.1.47
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Q6CE48 | MRGFRLIAPIQRSIAIISRLQPITANFHSSPALRSHENPLGIPKSPASAPRIPRKTTRRPEPIAGVKKTIVVSSAKGGVGKSTVSVNTALSLAKRGLRVGLLDVDIFGPSIPTMFGLSGEPRMTHEGKLIPMSKFGIQVMSMGFLVDPNKAVAWRGLLVQKALEQLLQDVDWGTLDVLVMDLPPGTGDVQLTIAQTVKIDGAIIVSTPQDVALVDVVRGLDLFEKTYTKVLGLVQNMSVFVCPNCNHETHIFGVDGAVSKAKSRGLGVLGNVPLDPQICSQSDKGVPVAVSGGVQAKYYDKIAEGVAEQLGV | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Required for the effective assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). Probably facilitates the assembly of Fe-S cofactors and subunits of complex I.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33167
Sequence Length: 312
Subcellular Location: Mitochondrion inner membrane
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A0A0D4BSN8 | MKLDDKRILIIGAGEVGTAVAEDLVNRSDPTEIIIHTSRQQTMDMRVGHLKEMAGPRTLLTGSWGDIFAPYELTHRSRSEINDRNVRLALAEFFLQPSGEAQLRRTTIYELISRHRPHIVIDAVNSASVCTYTEDPHQTCGELLDLARGTGGPRTAEAPAELPAVTPDIADVATDALLSLSTPILHRYVDSLRRAMADFQVERFIKVSTTGLGGMGYNCPYTHGSVTEFGLSDALVGKIGSAGVLHQLLWNLHHTAGCDVRLVIPAALIGWESVRHGAYTSRGRPVALQDCSRPLPLHLDRPLGEHAAASSVAEPAAEDEPSAEMVHVPAGDNSTYSRAEMSLSTALGQFESVTREEVAAAVLDTLLGSTRFDLFTAMDTASLQSSYLAAQMRTSTLTSMRQLEKAYDRPSIVSGNLGPTISKDLLELHVLCTAAGSLEQARTMSTTVLASSASALVREDVYLRQQALSIGLAVLLPDDQWLAGPRLSVPSRIDPEAKVTRADIDDWSRQGWVDLRPARILHWQENLRRIEQDASAGKTAFALDDTAYDVGEVLAYHYKLTGQARRIKGL | Function: Involved in the biosynthesis of the antibiotic indolmycin, an inhibitor of the bacterial tryptophan-tRNA synthetases. Catalyzes the NADH-dependent reduction of beta-methylindolepyruvate to yield indolmycenate.
Catalytic Activity: (2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate + NAD(+) = (R)-3-(indol-3-yl)-2-oxobutanoate + H(+) + NADH
Sequence Mass (Da): 62085
Sequence Length: 570
EC: 1.1.1.397
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A0A0D4BSP3 | MHTDWETSESAEDYSRNTAAAQWEPMGYPAVFRSLALATTDSDNAPPILDYGCGPGFVDRHVAEKYGRRVIAVDISSSMIDLARSQHSHPLVTYRHVPDSQLDFLGDKEIGGCMSCFVLMQMADSDTQVEICRRIRRTLAPGAMLAVLNTHPDSVGIQFATLRNGEPDRVYQPGDPMTTVLTTDKGVLRLQDYYWRVTDYVHALEAAGFHEVTVEHLPPPPADPTPHPQFLLVRGTA | Function: Involved in the biosynthesis of the antibiotic indolmycin, an inhibitor of the bacterial tryptophan-tRNA synthetases. Catalyzes the methylation of N-demethylindolmycin to yield indolmycin, with S-adenosylmethionine (AdoMet) acting as the methyl donor.
Catalytic Activity: N-demethylindolmycin + S-adenosyl-L-methionine = H(+) + indolmycin + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26296
Sequence Length: 237
EC: 2.1.1.328
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O49472 | MATVALLRSLRRRELHAAHISAYKFSSASAGGRTTELRLHGVKDIIAVASGKGGVGKSSTAVNLAVALANKCELKIGLLDADVYGPSVPIMMNINQKPQVNQDMKMIPVENYGVKCMSMGLLVEKDAPLVWRGPMVMSALAKMTKGVDWGDLDILVVDMPPGTGDAQISISQNLKLSGAVIVSTPQDVALADANRGISMFDKVRVPILGLVENMSCFVCPHCNEPSFIFGKEGARRTAAKKGLKLIGEIPLEMSIREGSDEGVPVVVSSPGSIVSKAYQDLAQNVVKGLKELRENPDNEIQMKLNVPHSSHSS | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Essential during early vegetative growth . Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) . Involved in mitochondrial translation activity . May deliver of one or more Fe-S clusters to complex I subunits (By similarity).
Sequence Mass (Da): 33426
Sequence Length: 313
Subcellular Location: Mitochondrion matrix
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Q9VVT2 | MATETTKMIYTPPPLDIKMEIEIGEQPQPPVKCSNFFANHWKGLVVFLVPLLCLPVMLLNEGAEFRCMYLLLVMAIFWVTEALPLYVTSMIPIVAFPIMGIMSSDQTCRLYFKDTLVMFMGGIMVALAVEYCNLHKRLALRVIQIVGCSPRRLHFGLIMVTMFLSMWISNAACTAMMCPIIQAVLEELQAQGVCKINHEPQYQIVGGNKKNNEDEPPYPTKITLCYYLGIAYASSLGGCGTIIGTATNLTFKGIYEARFKNSTEQMDFPTFMFYSVPSMLVYTLLTFVFLQWHFMGLWRPKSKEAQEVQRGREGADVAKKVIDQRYKDLGPMSIHEIQVMILFIFMVVMYFTRKPGIFLGWADLLNSKDIRNSMPTIFVVVMCFMLPANYAFLRYCTRRGGPVPTGPTPSLITWKFIQTKVPWGLVFLLGGGFALAEGSKQSGMAKLIGNALIGLKVLPNSVLLLVVILVAVFLTAFSSNVAIANIIIPVLAEMSLAIEIHPLYLILPAGLACSMAFHLPVSTPPNALVAGYANIRTKDMAIAGIGPTIITIITLFVFCQTWGLVVYPNLNSFPEWAQIYAAAALGNKTH | Function: Cation-independent electroneutral transporter (not associated with membrane depolarization) of a variety of tricarboxylic and dicarboxylic acid-cycle intermediates. There is also small, but detectable, transport of monocarboxylics. Transport is through the epithelium of the gut and across the plasma membranes of organs involved in intermediary metabolism and storage. Affinity for substrates is citrate > succinate > pyruvate. Fumarate, a-ketoglutarate, and glutarate are also transported, but not lactate. Transport mechanism that is not coupled to Na(+), K(+), or Cl(-). Function is shown in Xenopus oocytes and human retinal pigment epithelial (HRPE) cell lines.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65585
Sequence Length: 590
Subcellular Location: Basolateral cell membrane
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Q9VDQ0 | MAEPGEQRKFVLGRCCIFHWRGKASIIIPLITLPILIYGFQTDMAEFKCLWLIVTMALLWITETLPIYVTALFPLVFCPLLGLVNASIVCKQYFTDTIVVFLGGLIVALGIEYSNLHTRIALRVIRIVGGSPRRLFVGLMSVSTFMGLWISNSAGTAMMCPIVKALVNELDTNKIFPVYMTQEEEPVEEGEPPHPSKITVAFYAGIAYASSIGGLGTLIGTGTNLVFRGIYTERFPTSTVEITFANFMFYSIPLMVIVNVTLVIIAFLITHMGLFRPNSKTGKIIAEANTNRKLMEDVLRQRHIDLGPMSCHEIQMAIAFAFMIVLLITRKPGFVPGWSDLINRKVVGSASGLSFIVLLIFALPTQYTFFKYCCGKGPFTAQAIDAILSWEYVLRNIPWGLLFLLGGGFALAVASRETGLNIMISKAMQVLIGLPNIVVQSITFVLANFFSAFNANVVVANIVLPILCEMSLALELHPLILTLPACLGISMVYFLPVSTPPNAIVTQYAHIKTKYFACCGIVPTIIGISVALVNTNTWGLIIFPESKSFPDWAKEIKNQTKI | Function: Cation-independent electroneutral transporter (not associated with membrane depolarization) of a variety of tricarboxylic and dicarboxylic acid-cycle intermediates. There is also small, but detectable, transport of monocarboxylics. Transport is through the epithelium of the gut and across the plasma membranes of organs involved in intermediary metabolism and storage (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61935
Sequence Length: 562
Subcellular Location: Membrane
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Q9VR07 | MAENKDVSQVLNTTPDQVVINRAPPTGLAPLRHSQLSDSGAESCYEGDEQARLIRSSSSRAHKFIIIPATPGTPPGSGAVAGPLPFRQTSSTTSLAAMAAALHKQSPLRHTSVRTRPSSEVLQPGQVLANQPTAAVSTSTVTFTIDDCNEEGDAIPAAASVPAPVTMPAISPTPATLTCTTTTTMAGDSVAVSPLSMELKSRLGSHHSSMRSVVSGYLPGLSDSSGNLVGGVSMATSGLQAPNPLYMQPQASLSGSSYHFHELAGNQIYSDVTSVRSLASIGIGSTDGRKLVIRRVPTTANELFDMVNPQTPPPLGVDDDDSYLDMSDETAQLKPRQQHWANKMQFVLACIGYSVGLGNVWRFPYMCYKSGGGVFLVPYCIILFICSIPLLFMELSVGQYTGRGPIGALGQLCPLFKGAGLASVVVSFLMSTYYSVIIGYSIYYFFTSFKTEMPWIDCNNRWNTPDCWVPQRKGINASAPDTSRTPSEEFFENKVLQISGGLEYPGMMRWELFACLICAWLMVYFATWKSIKSSAKVRYFTATFPFVLIIILMVRAVTLDGAAEGLRFFFRPKWSELKNANVWINAASQNFNSLGITFGSMISFASYNKYNNNILRDTVAVSAVNMITSLLVGIFAFSTLGNLALEQNTNVRDVIGDGPGMIFVVYPQAMAKMPYAQLWAVMFFFMLLCLGLNSQFAIVEVVVTSIQDGFPRWIKRHLGYHEIVVLFVCVISCLFGMPNIIQGGIYYFQLMDHYAASVTIMFLAFCQMIAIAWFYGTGRLSKNVKQMTGKAPSFYLRSCWLVLGPCLLFAIWVLSLINYHEPTYHNGRYTYPDWAYGIGWMFASFSLICIPGYAVINFLRSSGDTFWERIRNTLRPNIYECKICGEHHCEHDYPEQEQFMLAQEMATVYKPTNPHLLNLGQKCGYNAMQASPSHAEAGGPCGQ | Function: Plays a role in neuronal membrane excitation, important for normal response properties of the photoreceptor. Able to control excitability from either neurons or glia cells. Ine negatively regulates neuronal sodium channels. Controls neurotransmitter-mediated signaling pathways associated with the structure of the larval peripheral nerve, ine and eag control perineurial glial growth through partially redundant pathways. Isoform A and isoform B are both functional, although isoform A functions with greater efficiency. Has a role in osmolyte transport within the Malpighian tubule and hindgut.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 103636
Sequence Length: 943
Subcellular Location: Membrane
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P42801 | MFIESFKVESPNVKYTENEIHSVYDYETTEVVHEKTVNGTYQWIVKPKTVKYDFKTDIRVPKLGVMLVGLGGNNGSTLTAGVIANKEGISWATKDKVQQANYFGSLTQASSIRVGSFNGEEIYAPFKSLLPMVNPDDVVFGGWDISDMNLADAMARARVLDIDLQKQLRPYMENIVPLPGIFDPDFIAANQGSRANHVIKGTKKEQVDHIIKDMREFKEKNKVDKVVVLWTANTERYSNVVVGMNDTMENLMESVDRDEAEISPSTLYAIACVLEGIPFINGSPQNTFVPGLIDMAIRNNVLIGGDDFKSGQTKMKSVLVDFLVGAGIKPTSIVSYNHLGNNDGMNLSAPQTFRSKEISKSNVVDDMVASNGILFEPGEHPDHVVVIKYVPYVADSKRAMDEYTSEIFMGGKNTIVMHNTCEDSLLAAPIILDLVLLAELSTRIQFKSEGEGKFHSFHPVATILSYLTKAPLVPPGTPVINALSKQRAMLENIMRACVGLAPENNMIMEFK | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner . Catalyzes the majority of myo-inositol synthesis required for plant growth and development . Acts as a repressor of programmed cell death and protects plant cells against cell death under high light intensity or long days . Controls its own transcription by inhibiting ATXR6 activity . Reduces the deposition of inhibitory histone marks on its own promoter .
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 56515
Sequence Length: 511
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
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Q8A7J8 | MKQEIKPATGRLGVLVVGVGGAVATTMIVGTLASRKGLAKPIGSITQLATMRMENNEEKLIKDVVPLTDLNDIVFGGWDIFPDNAYEAAMYAEVLKEKDLNGVKDELEAIKPMPAAFDHNWAKRLNGTHIKKAATRWEMVEQLRQDIRDFKAANNCERVVVLWAASTEIYIPLSDEHMSLAALEKAMKDNNTEVISPSMCYAYAAIAEDAPFVMGAPNLCVDTPAMWEFSKQKNVPISGKDFKSGQTLMKTVLAPMFKTRMLGVNGWFSTNILGNRDGEVLDDPDNFKTKEVSKLSVIDTIFEPEKYPDLYGDVYHKVRINYYPPRKDNKEAWDNIDIFGWMGYPMEIKVNFLCRDSILAAPIALDLVLFSDLAMRAGMCGIQTWLSFFCKSPMHDFEHQPEHDLFTQWRMVKQTLRNMIGEKEPDYLA | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3-phosphate in a NAD-dependent manner.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 48398
Sequence Length: 429
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Membrane
EC: 5.5.1.4
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Q2NL29 | MEAATEFVVESPDVVYSPETIEAQYEYRTTSVSREGGVLKVHPTSTRFTFRTARQVPRLGVMLVGWGGNNGSTLTAAVLANRLRLSWPTRTGRKEANYYGSLTQAGTVSLGLDAEGKEVFVPFSSLLPMVAPDDLVFDGWDISSLNLAEAMRRAQVLDWGLQEQLWPHMEAMRPRPSVYIPEFIAANQSARADNVIPGTRAQQLEQIRRDIRDFRFSAGLDKVIVLWTANTERFCEVIPGLNDTAENLLRTIQLGLEVSPSTLFAVASILEGCAFLNGSPQNTLVPGALELAWQRRVFVGGDDFKSGQTKVKSVLVDFLIGSGLKTMSIVSYNHLGNNDGQNLSAPPQFRSKEVSKSSVVDDMVHSNPVLYSPGEQPDHCVVIKYVPYVGDSKRALDEYTSELMLGGTNTLVLHNTCEDSLLAAPIMLDLALLTELCQRVSFCTDVDPDPQSFHPVLSLLGFLFKAPLAPPGSPVVNALFRQRSCIENILRACVGLPPQNHMLLEHKMERPGLKRVGPLATTSPVLCKKGSAPTAPNGCTGDANGHSQAEAPQMPTT | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner . Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 60761
Sequence Length: 557
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
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Q8NLE6 | MSTSTIRVAIAGVGNCATSLIQGVEYYRNADPSETVPGLMHVKFGDYHVGDIEFVAAFDVDAEKVGIDLADATEASQNCTIKIADVPQTGINVLRGPTLDGLGDHYRATIDESTAEPVDVVQALIDAKADVLVSYLPVGSEEADKFYAQAAIDAGCAFVNALPVFIASDPEWAKKFTDAGIPIVGDDIKSQIGATITHRVLARLFEERGVRVDRTMQLNVGGNMDFKNMLDRNRLESKKVSKTQAVTSNIPDGPLSGKVEDRNVHIGPSDHVQWLDDRKWAYVRLEGTAFGGVPLNLEYKLEVWDSPNSAGIIIDAVRAAKIALDRGIGGPIMPASSYLMKSPPEQLPDDVARERLEAFIIEA | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3-phosphate in a NAD-dependent manner . Plays a key role in oxidative stress resistance as its product is the precursor of the protective antioxidant mycothiol (MSH or AcCys-GlcN-Ins) .
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 39223
Sequence Length: 363
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
EC: 5.5.1.4
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J9VYL3 | MSPTALDACDHHDSFSLPAQDQSKVHPSARRTPEGGLIKVESDSTVYEADGIKAKFTDRGASVIKGSDGKLSVKKTEKNFEFFTKSTVGRVGLMLVGLGGNNGTTVLATNLANKYNISWHTKNGIQQPNYIGSVVRASTVRLGTDPETGKDVFVPISDMLPMVHPNDFVIGGWDISSLSMDKAMLRAKVLEWDLQRQLIPLMENVKPLPSIYYPDFIAANQADRADNLIPGDDKKVHLEHIRADIRRFKADNHLDSVVVLWTANTERYADIIPGVNDTADNLLKAVETSHEEVSPSTIFAMASILEGVPFINGSPQNTFVPGCIELAEKHKAFIGGDDFKSGQTKVKSVLAEFLVNAGIKPLSISSYNHLGNNDGKNLSSQRQFRSKEISKSSVVDDMVAANPILYKTAEDLSKATGEIVKKGEHPDHIVVIKHVPAVGDSKRAIDEYYSELLMGGRNVMNIFNECEDSLLATPLIFDLAILAELLTRVTYRENATGEWQPLYSVLSLLSYMLKAPLVKPGEDVVNSLNRQRNALEQFLKACLGLEHSNDLLLNTRVW | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner . Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 61383
Sequence Length: 558
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
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Q54N49 | MSAQMFESFKVNSPNVKYTDEHIISDYTYQTTKVQNVNGELIVEPVDQKYIFKTERKVPRMGVMIVGLCGNNGTTVVGGVIANREGLCWNTKQGLQTPNYFGSVVMSSTIRMGMDENGCDAYIPLKNLIPMVHPNDIVFGGWDINNANLADAMQRAQVFDYDLQVQLIPHMKNITPLPSIYFPDFIAANQKDRANNVLTGTKKEQMEQIRKDIRDFKESNKLDTVVVMWSANTERFSSLVPGVNDTIENLMAAIDRSEEEISPSTLFAVASILENTTYINGSPQNTFVPAVVDLAIQHNVSIGGDDFKTGQTKIKSVLTDYLVSAGIKPVSIVSYNHLGNNDGKNLSAPQQFRSKEITKSNVVDDMIASNNILYKQGEHPDHVIVIKYVPYVGDSKRAMDEYTSQIFMGGHNTIVLHNTCEDSLLAAPIILDLVILAEVTSRITMKKQDDDQFATFHPVLSLLSYLLKAPIVPKHATVVNALFKQRACIENIFKACVGIAPDNNMLLEQRL | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 56847
Sequence Length: 511
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
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O97477 | MKPTNNSTLEVISPKVQVDDEFITTDYDYQTSHVKRTADGQLQVHPQTTSLKIRTGRHVPKLGVMLVGWGGNNGSTLTAALEANRRQLKWRKRTGVQEANWYGSITQASTVFIGSDEDGGDVYVPMKELLPMVEPDNIIVDGWDISGLHLGDAMRRAEVLDVALQDQIYDQLAQLRPRPSIYDPDFIAANQSDRADNVIRGTRLEQYEQIRKDIRDFRERSGVDSVIVLWTANTERFADVQPGLNTTSQELIASLEANHSEVSPSTIFAMASIAEGCTYINGSPQNTFVPGLIQLAEEKNVFIAGDDFKSGQTKIKSVLVDFLVGAGIKPVSIASYNHLGNNDGKNLSAPQQFRSKEISKSNVVDDMVASNRLLYGPDEHPDHVVVIKYVPYVGDSKRAMDEYTSEIMMGGHNTLVIHNTCEDSLLATPLILDLVILGELSTRIQLRNAEKESAPWVPFKPVLSLLSYLCKAPLVPQGSQVVNSLFRQRAAIENILRGCIGLPPISHMTLEQRFDFSTITNEPPLKRVKILGQPCSVESVTNGKKLHANGHSNGSAKLATNGNGH | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner . Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 62249
Sequence Length: 565
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
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Q9NPH2 | MEAAAQFFVESPDVVYGPEAIEAQYEYRTTRVSREGGVLKVHPTSTRFTFRTARQVPRLGVMLVGWGGNNGSTLTAAVLANRLRLSWPTRSGRKEANYYGSLTQAGTVSLGLDAEGQEVFVPFSAVLPMVAPNDLVFDGWDISSLNLAEAMRRAKVLDWGLQEQLWPHMEALRPRPSVYIPEFIAANQSARADNLIPGSRAQQLEQIRRDIRDFRSSAGLDKVIVLWTANTERFCEVIPGLNDTAENLLRTIELGLEVSPSTLFAVASILEGCAFLNGSPQNTLVPGALELAWQHRVFVGGDDFKSGQTKVKSVLVDFLIGSGLKTMSIVSYNHLGNNDGENLSAPLQFRSKEVSKSNVVDDMVQSNPVLYTPGEEPDHCVVIKYVPYVGDSKRALDEYTSELMLGGTNTLVLHNTCEDSLLAAPIMLDLALLTELCQRVSFCTDMDPEPQTFHPVLSLLSFLFKAPLVPPGSPVVNALFRQRSCIENILRACVGLPPQNHMLLEHKMERPGPSLKRVGPVAATYPMLNKKGPVPAATNGCTGDANGHLQEEPPMPTT | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner . Rate-limiting enzyme in the synthesis of all inositol-containing compounds .
PTM: Phosphorylation at Ser-279 and Ser-357 may be associated with a decrease in activity.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 61068
Sequence Length: 558
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
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A0R7G6 | MSEHAGEIRVAIVGVGNCASSLVQGVQYYRNADENTTVPGLMHVKFGPYHVRDVNFVAAFDVDAKKVGFDLSEAIFASENNTIKIADVPPTDVIVQRGPTLDGIGKYYADTIEVSDAEPVDVVKVLKEAEVDVLVSYLPVGSEEADKFYAQCAIDAGVAFVNALPVFIASDPVWAKKFEDAGVPIVGDDIKSQVGATITHRVMAKLFEDRGVTLDRTYQLNVGGNMDFLNMLERSRLESKKVSKTQAVTSNLSGALAGKVEDKNVHIGPSDHVAWLDDRKWAYVRLEGRAFGDVPLNLEYKLEVWDSPNSAGVIIDAVRAAKIAKDRGIGGPIEAASAYLMKSPPKQLADDVARAELETFIEG | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3-phosphate in a NAD-dependent manner.
PTM: Pupylated at Lys-65 by the prokaryotic ubiquitin-like protein Pup, which leads to its degradation by the proteasome.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 39300
Sequence Length: 363
EC: 5.5.1.4
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P9WKI0 | MSEHQSLPAPEASTEVRVAIVGVGNCASSLVQGVEYYYNADDTSTVPGLMHVRFGPYHVRDVKFVAAFDVDAKKVGFDLSDAIFASENNTIKIADVAPTNVIVQRGPTLDGIGKYYADTIELSDAEPVDVVQALKEAKVDVLVSYLPVGSEEADKFYAQCAIDAGVAFVNALPVFIASDPVWAKKFTDAGVPIVGDDIKSQVGATITHRVLAKLFEDRGVQLDRTMQLNVGGNMDFLNMLERERLESKKISKTQAVTSNLKREFKTKDVHIGPSDHVGWLDDRKWAYVRLEGRAFGDVPLNLEYKLEVWDSPNSAGVIIDAVRAAKIAKDRGIGGPVIPASAYLMKSPPEQLPDDIARAQLEEFIIG | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3-phosphate in a NAD-dependent manner.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 39994
Sequence Length: 367
EC: 5.5.1.4
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P9WKI1 | MSEHQSLPAPEASTEVRVAIVGVGNCASSLVQGVEYYYNADDTSTVPGLMHVRFGPYHVRDVKFVAAFDVDAKKVGFDLSDAIFASENNTIKIADVAPTNVIVQRGPTLDGIGKYYADTIELSDAEPVDVVQALKEAKVDVLVSYLPVGSEEADKFYAQCAIDAGVAFVNALPVFIASDPVWAKKFTDARVPIVGDDIKSQVGATITHRVLAKLFEDRGVQLDRTMQLNVGGNMDFLNMLERERLESKKISKTQAVTSNLKREFKTKDVHIGPSDHVGWLDDRKWAYVRLEGRAFGDVPLNLEYKLEVWDSPNSAGVIIDAVRAAKIAKDRGIGGPVIPASAYLMKSPPEQLPDDIARAQLEEFIIG | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3-phosphate in a NAD-dependent manner.
PTM: Pupylated at Lys-73 by the prokaryotic ubiquitin-like protein Pup, which leads to its degradation by the proteasome.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 40094
Sequence Length: 367
EC: 5.5.1.4
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P28999 | MKFAYSLLLPLAGVSASVINYKRDGDSKAITNTTFSLNRPSVHFTPSHGWMNDPNGLWYDAKEEDWHLYYQYNPAATIWGTPLYWGHAVSKDLTSWTDYGASLGPGSDDAGAFSGSMVIDYNNTSGFFNSSVDPRQRAVAVWTLSKGPSQAQHISYSLDGGYTFEHYTDNAVLDINSSNFRDPKVFWHEGENGEDGRWIMAVAESQVFSVLFYSSPNLKNWTLESNFTHHGWTGTQYECPGLVKVPYDSVVDSSNSSDSKPDSAWVLFVSINPGGPLGGSVTQYFVGDFNGTHFTPIDGQTRFLDMGKDYYALQTFFNTPNEKDVYGIAWASNWQYAQQAPTDPWRSSMSLVRQFTLKDFSTNPNSADVVLNSQPVLNYDALRKNGTTYSITNYTVTSENGKKIKLDNPSGSLEFHLEYVFNGSPDIKSNVFADLSLYFKGNNDDNEYLRLGYETNGGAFFLDRGHTKIPFVKENLFFTHQLAVTNPVSNYTTNVFDVYGVIDKNIIELYFDNGNVVSTNTFFFSTNNVIGEIDIKSPYDKAYTINSFNVTQFNV | Function: Has both inulase and invertase activity.
Catalytic Activity: Endohydrolysis of (2->1)-beta-D-fructosidic linkages in inulin.
Sequence Mass (Da): 62214
Sequence Length: 555
Subcellular Location: Secreted
EC: 3.2.1.7
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O94220 | MLNPKVAYMVWMTCLGLTLPSQAQSNDYRPSYHFTPDQYWMNEPNGLIKIGSTWHLFFQHNPTANVWGNICWGHATSTDLMHWAHKPTAIADENGVEAFTGTAYYDPNNTSGLGDSANPPYLAWFTGYTTSSQTQDQRLAFSVDNGATWTKFQGNPIISTSQEAPHDITGGLESRDPKVFFHRQSGNWIMVLAHGGQDKLSFWTSADTINWTWQSDLKSTSINGLSSDITGWEVPDMFELPVEGTEETTWVVMMTPAEGSPAGGNGVLAITGSFDGKSFTADPVDASTMWLDNGRDFDGALSWVNVPASDGRRIIAAVMNSYGSNPPTTTWKGMLSFPRTLSLKKVGTQQHFVQQPITELDTISTSLQILANQTITPGQTLLSSIRGTALDVRVAFYPDAGSVLSLAVRKGASEQTVIKYTQSDATLSVDRTESGDISYDPAAGGVHTAKLEEDGTGLVSIRVLVDTCSVEVFGGQGEAVISDLIFPSDSSDGLALEVTGGNAVLQSVDVRSVSLE | Function: Endo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60.
Catalytic Activity: Endohydrolysis of (2->1)-beta-D-fructosidic linkages in inulin.
Sequence Mass (Da): 55793
Sequence Length: 516
Subcellular Location: Secreted
EC: 3.2.1.7
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Q96TU3 | MAPLSKALSVFMLMGITYAFNYDQPYRGQYHFSPQKNWMNDPNGLLYHNGTYHLFFQYNPGGIEWGNISWGHAISEDLTHWEEKPVALLARGFGSDVTEMYFSGSAVADVNNTSGFGKDGKTPLVAMYTSYYPVAQTLPSGQTVQEDQQSQSIAYSLDDGLTWTTYDAANPVIPNPPSPYEAEYQNFRDPFVFWHDESQKWVVVTSIAELHKLAIYTSDNLKDWKLVSEFGPYNAQGGVWECPGLVKLPLDSGNSTKWVITSGLNPGGPPGTVGSGTQYFVGEFDGTTFTPDADTVYPGNSTANWMDWGPDFYAAAGYNGLSLNDHVHIGWMNNWQYGANIPTYPWRSAMAIPRHMALKTIGSKATLVQQPQEAWSSISNKRPIYSRTFKTLSEGSTNTTTTGETFKVDLSFSAKSKASTFAIALRASANFTEQTLVGYDFAKQQIFLDRTHSGDVSFDETFASVYHGPLTPDSTGVVKLSIFVDRSSVEVFGGQGETTLTAQIFPSSDAVHARLASTGGTTEDVRADIYKIASTWN | Function: Exo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. Splits off terminal fructose units successively from the non-reducing end of the inulin molecule, and also hydrolyzes levan, stachyose and raffinose.
Catalytic Activity: Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.
Sequence Mass (Da): 59171
Sequence Length: 537
Subcellular Location: Secreted
EC: 3.2.1.80
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O05265 | MIRFAIIGTNWITDRFLESAADIEDFQLTAVYSRSAERAGEFAAKHNAAHAFSDLQEMAASDCFDAVYIASPNALHKEQAVLFMNHGKHVLCEKPFASNTKETEEMISAAKANGVVLMEAMKTTFLPNFKELKKHLHKIGTVRRFTASYCQYSSRYDAFRSGTVLNAFQPELSNGSLMDIGVYCIYPAVVLFGAPKDVKANGYALSSGVDGEGTVILSYDGFEAVLMHSKISTSYAPAEIQGEDGTIVIDTIHRPERVEIRYRDGRLENIAIPDPKPAMFYEAEEFVTLIKENKLESEENTFERSLTTAKIMEEARKQMGIVYPADQA | Function: Catalyzes the NADPH-dependent reduction of scyllo-inosose (SIS) to scyllo-inositol (SI) in vitro, but is unable to dehydrogenate scyllo-inositol and myo-inositol. Is less efficient than the functional paralog IolW. Under physiological conditions, may primarily function as an NADPH-dependent oxidoreductase that reduces carbonyl group(s) in its substrates. Cannot use NADH instead of NADPH.
Catalytic Activity: NADP(+) + scyllo-inositol = H(+) + NADPH + scyllo-inosose
Sequence Mass (Da): 36515
Sequence Length: 328
EC: 1.1.1.371
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O32223 | MITLLKGRRKVDTIKVGILGYGLSGSVFHGPLLDVLDEYQISKIMTSRTEEVKRDFPDAEVVHELEEITNDPAIELVIVTTPSGLHYEHTMACIQAGKHVVMEKPMTATAEEGETLKRAADEKGVLLSVYHNRRWDNDFLTIKKLISEGSLEDINTYQVSYNRYRPEVQARWREKEGTATGTLYDLGSHIIDQTLHLFGMPKAVTANVMAQRENAETVDYFHLTLDYGKLQAILYGGSIVPANGPRYQIHGKDSSFIKYGIDGQEDALRAGRKPEDDSWGADVPEFYGKLTTIRGSDKKTETIPSVNGSYLTYYRKIAESIREGAALPVTAEEGINVIRIIEAAMESSKEKRTIMLEH | Function: Catalyzes the reversible NADPH-dependent reduction of scyllo-inosose (SIS) to scyllo-inositol (SI). Cannot use NADH instead of NADPH. May be involved in reduction of not only SIS but also various oxidized compounds manifested upon stressful conditions.
Catalytic Activity: NADP(+) + scyllo-inositol = H(+) + NADPH + scyllo-inosose
Sequence Mass (Da): 40112
Sequence Length: 358
EC: 1.1.1.371
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P40332 | MEHQVRCAVLGLGRLGYYHAKNLVTSVPGAKLVCVGDPLKGRAEQVARELGIEKWSEDPYEVLEDPGIDAVIIVTPTSTHGDMIIKAAENGKQIFVEKPLTLSLEESKAASEKVKETGVICQVGFMRRFDPAYADAKRRIDAGEIGKPIYYKGFTRDQGAPPAEFIKHSGGIFIDCSIHDYDIARYLLGAEITSVSGHGRILNNPFMEQYGDVDQALTYIEFDSGAAGDVEASRTSPYGHDIRAEVIGTEGSIFIGTLRHQHVTILSAKGSSFDIIPDFQTRFHEAYCLELQHFAECVRNGKTPIVTDIDATINLEVGIAATNSFRNGMPVQLDVKRAYTGM | Function: Catalyzes the reversible NAD(+)-dependent oxidation of scyllo-inositol (SI) to 2,4,6/3,5-pentahydroxycyclohexanone (scyllo-inosose or SIS). Is required for SI catabolism that allows B.subtilis to utilize SI as the sole carbon source for growth. Cannot use NADP(+) instead of NAD(+).
Catalytic Activity: NAD(+) + scyllo-inositol = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 37484
Sequence Length: 342
Pathway: Polyol metabolism.
EC: 1.1.1.370
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O28783 | MLNDVVRDAEGEKVFLLGNEAIARGAIEAGIDVFAAYPGTPSSEIADTLSDACRLLRGKMDFYMEYSANEKVAFEVAVGASLAGKRAMATMKHVGVNVAADPLFSFAYVGARGGFVLVTADDPSMHSSQNEQDNRWYGKAAKLPVVEPSSVQEAKDYAKLCFDLSEKFGLPMILRSYTRLSHASGVVELGKIPEKEFSRVEWERHPETDVVLPAHARKLKPILLEKLEKIERYFNSSEMNWVDEGDGDVGIIACGLSYAYTKEALENLNLNLPVLKLSSMHPLPERLIENFVSQMKKVIVVEEVDPFVELHVRAMGLAEVYGKMNGYMPMNYEYNVGRVETGIAKALGIKPSRDYEGIVAESQKLAAKAPPRPPVLCPGCPHSASFYAIRRVVDELGDAALPSDIGCYTLGINKPLEGVDITICMGASVGVSNGLAHVLNNKIIATIGDSTFIHAGIPPLINAVYNHADFVLVILDNSTTGMTGHQPHPGTGFRGCGEAGKAVRIEDIVRGCGVEFVEVVNPYNVRKMVDVLRRALNHDGVAVVIARQPCAILWSRARRREGKIVTYKVTEDCTLCMECVNTFACPALIFDGEKVSIDQSLCVGCAVCAKICPNRAIKPAKSN | Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] = (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 67798
Sequence Length: 623
EC: 1.2.7.8
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Q51697 | MIEFILNGQPVRVTEVPEDAPLLWVVREHLKLSGTKFGCGLGLCGACTVHINGEAARSCITPLSVVARQSVTTIEGLDPQHAHPLQRAWIAEQVPQCGYCQSGQIMQAAALLKKVPKPSDAQIVEAMDGNLCRCGTYQRIKIAIHRAAKEAA | Function: Specific towards N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline.
Catalytic Activity: A + H2O + isoquinoline = AH2 + isoquinolin-1(2H)-one
Sequence Mass (Da): 16410
Sequence Length: 152
EC: 1.3.99.16
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P80910 | MELDDILDAGRGDRLFLLGNEAAVRAAIESGVGVASTYPGTPSSEIGNVLSKIAKRAGIYFEFSINEKVALEVAAAAAASGVRSFTFMKHVGLNVASDSFMSVAYTGVRAGMVVLSADDPSMFSSQNEQDNRHYARLAWVPLLEPSNPQEILEYMNHAFELSEEYRIPVLLRTTTRVSHMRGVVEAGERRAEPVKGFFRKNPEQFVPVPATARVMRRELVEKMKKLKRVADTSELNRVLNEDSESDLGIIASGGAFNYVYDALQTLGLDVPVLKLGFTYPFPAGLVAEFLSGLEGVLVVEEVDSVMEKEVLAVATSEGLDVGVHGKLDGTLPEIYEYSEDIVRRAISGLTGIKSHEKGIEAPELPERPPALCPGCPHRAMYYSVRRAASELGIEGEDLIFPTDIGCYTLGIEPPYSAADYLLSMGSSVGTACGFSAATSQRIVSFIGDSTFFHAGIPPLINAVHNRQRFVLVILDNRTTAMTGGQPHPGLPVDGMGEEAPAISIEDITRACGVEFVETVNPMNIRRSSETIRRALQHESVAVVISRYPCMLSEGAVRGRPVRVDEEKCDLCLECLNELACPAIVEEDGRVFIDPLYCRGCTICLQICPAGAIKPEGKR | Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] = (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 67098
Sequence Length: 618
EC: 1.2.7.8
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O07835 | MAKVTDIVLWDKPGERVLLLGNHAIARGALEANIAVFAAYPGTPSSELTDTMAAVAKKAGVYMEYSTNEKVAFETALAAAWSGLRAMTAMKHVGLNVAADSFLSSVGMGVEGGFVIMVADDPSMWSSQNEQDTRVYAKFANVPVLEPSSPHEAKEMTKYAFELSEKFKHFVILRTTTRSSHARGDVVLGELPEEIKTGKRKFGKFKKDPTRFVDVPAHARKFHPLILEKIEKIREELNNCPFNWIEGKEDAKVGIIAPGLSYAYVKEALAWLGVEDVKILKLGTPFPVPYGLLGKFFDGLEKVLIVEELEPVVEEQVKTWAYDKGLRIPIHGKDLVPRVYEMTTRRAVEAIAKFLGLETPINFAEIDEKYEKVSQIVPPRPPSLCPACPHRNSFFAIRKAAGPKAIYPSDIGCYTLGVLPPLRTVDTTVAMGASIGIGHGLSIAMNGSLAEEEHKEGKEKQIIVATIGDSTFYHTGLPALANAIYNRSNVLIVVLDNLVTAMTGDQPNPGTGQTPHGMGKRIPIEDVAKAMGADFVAVVDPYDIKATYETIKKALEVEGVSVVVSRQVCALYKIGQMRRRGMKWPIYHVVEDKCTGCKICINAYGCPAIYWDPETKKAKVDPTMCWGCGGCAQVCPFDAFEPMKEGE | Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] = (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 70900
Sequence Length: 647
EC: 1.2.7.8
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O28249 | MRLNIVVVGVGGQGALTTSGIIARAAMRAGLNVVTAETHGMAQRGGSVEVHVRIGDVRAPLIPEGGADVMIALEPAEALRYAKFLNKNTLVILNTRKIIPPSVTAGTAKYPELDEIIGELRKVTPRVIPVNASEIAEKAGSVLATNVVVVGMLFGYYSMPFGIEHVEEAIRETMKSKIVDLNLKALKMGYNQAISGRPSAV | Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] = (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 21328
Sequence Length: 201
EC: 1.2.7.8
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Q51698 | MKTVLPSVPETVRLSRRGFLVQAGTITCSVAFGSVPAAAGDTAESTPSIAAVSPNVWVRVHADGIVDIVCPAVELGQGAHTALPRFVAEELDADWDRVRVQQAGASDKVYGNPLAWGTQFTAASRTTVGYFDVLRVAGAQARFVLVQTAARRWSVPADQLETQKGVVLHRRSRRSATYGELVASVQVPESFPHFFARNEATQPADDYFGAAPPSVVAQAAGPASGAIALKHRSTYRLIGKDAPRKDIPPKVNGQACYGMDVQVPGMLYAMVETGPVAGMAPERVDDGAARQVPGIHHVLSLPHGVAVVGRDIFAVRAARARLLVNWKANPDKQSYDSGQVLDEFSDLCRNGIERNAVQAWKQGELSSIDAVFARPDVRIESFEMQSDLVYQAPMEPQSAVIQPHADGSAEAWVGTQWPTVEQGFAAGILGIAPDKLTMHLPLVGGGFGRRLEPGALVDAAHIVRAIGKTVKVIWSREDDLKRNPFRQALACRVEAAVLEKDQRILALRHTVAADSWLARLFPQYFNAYQQTDPGNWIGGMVAYDVPLQRIDALTPRRSVDVCYMRGIGVAQVKFAQESLVDQIARRLNADPVDFRLAHLNTSPRGAAVVRTVAEMSDWKRRSADAGGGMALGLAYTPYSNAHVALVSEVHFNRSENTLSVSRVWCAVDVGMVAQPDIVKAQMEGGIIQGLSVALMERVQVAKGVLQHSNFHDYPMLRMSQVPQIHVRLVETDQAMAGVAELGLLQIGPAINNAFARITGQHLRSLPMRPALAQMKRSGPTA | Function: Specific towards N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline.
Catalytic Activity: A + H2O + isoquinoline = AH2 + isoquinolin-1(2H)-one
Sequence Mass (Da): 84483
Sequence Length: 781
EC: 1.3.99.16
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O27881 | MNYNIYVCGVGGQGIIKTSVIIGEAAMKKDINVVMSEIHGMAQRGGSVSTEIRIGEVHGSIIPDGEADLVLAFEPLEAIRALPKMSEESEVILNTSVIPPFNLMRSPHPYPPLDEIMSTLEERAGSVRGFNAEEIALKAGHILSLNMVMLGAAAATPGFPLESESLISSMRDNLPSRLIDVNLRAFRDGFGAAAES | Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] = (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 20948
Sequence Length: 196
EC: 1.2.7.8
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P80911 | MSYNIYVCGVGGQGIIKTSVIIGEAAMNEGMNVVMSEIHGMAQRGGAVSTEIRFGDVRGSIIPQGEADLVIAFEPLEALRALPKMSEDACVIVNTSKIPPFNLIKSPHPYPPLEEIIKTLEENAGRVRSFNGEKIAVEAGHILSLNMVMLGAAAATTGFPLGEETLIESMKNNLPPKLMEVNLRAFHEGFETVNCD | Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] = (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 21068
Sequence Length: 196
EC: 1.2.7.8
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O07836 | MKEYNIVITGVGGQGILTAANLLGWAALRAGYKVRVGEVHGMSQRFGSVIAYVRFGEDVYGAMVPEGKADVILSFEPVEALRYINYLKKGGLVFTNARPIPPVQVSMGLATYPTLDEMKKIVEEDFGGKFMAFDAEKLAMEAGNIVTTNVVLIGALSQTPGFPLSEEQIKEVIRISVPPKTIDVNMRAFELGVKAAKEMLGL | Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] = (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 21886
Sequence Length: 202
EC: 1.2.7.8
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P23677 | MTLPGGPTGMARPGGARPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAKRRGGQVPNGLPRAPPAPVIPQLTVTAEEPDVPPTSPGPPERERDCLPAAGSSHLQQPRRLSTSSVSSTGSSSLLEDSEDDLLSDSESRSRGNVQLEAGEDVGQKNHWQKIRTMVNLPVISPFKKRYAWVQLAGHTGSFKAAGTSGLILKRCSEPERYCLARLMADALRGCVPAFHGVVERDGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAPTEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVLRVFEEFVQGDEEVLRRYLNRLQQIRDTLEVSEFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKTTPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER | Function: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis.
Catalytic Activity: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+)
Sequence Mass (Da): 51009
Sequence Length: 461
Subcellular Location: Cytoplasm
EC: 2.7.1.127
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P27987 | MAVYCYALNSLVIMNSANEMKSGGGPGPSGSETPPPPRRAVLSPGSVFSPGRGASFLFPPAESLSPEEPRSPGGWRSGRRRLNSSSGSGSGSSGSSVSSPSWAGRLRGDRQQVVAAGTLSPPGPEEAKRKLRILQRELQNVQVNQKVGMFEAHIQAQSSAIQAPRSPRLGRARSPSPCPFRSSSQPPGRVLVQGARSEERRTKSWGEQCPETSGTDSGRKGGPSLCSSQVKKGMPPLPGRAAPTGSEAQGPSAFVRMEKGIPASPRCGSPTAMEIDKRGSPTPGTRSCLAPSLGLFGASLTMATEVAARVTSTGPHRPQDLALTEPSGRARELEDLQPPEALVERQGQFLGSETSPAPERGGPRDGEPPGKMGKGYLPCGMPGSGEPEVGKRPEETTVSVQSAESSDSLSWSRLPRALASVGPEEARSGAPVGGGRWQLSDRVEGGSPTLGLLGGSPSAQPGTGNVEAGIPSGRMLEPLPCWDAAKDLKEPQCPPGDRVGVQPGNSRVWQGTMEKAGLAWTRGTGVQSEGTWESQRQDSDALPSPELLPQDPDKPFLRKACSPSNIPAVIITDMGTQEDGALEETQGSPRGNLPLRKLSSSSASSTGFSSSYEDSEEDISSDPERTLDPNSAFLHTLDQQKPRVSKSWRKIKNMVHWSPFVMSFKKKYPWIQLAGHAGSFKAAANGRILKKHCESEQRCLDRLMVDVLRPFVPAYHGDVVKDGERYNQMDDLLADFDSPCVMDCKMGIRTYLEEELTKARKKPSLRKDMYQKMIEVDPEAPTEEEKAQRAVTKPRYMQWRETISSTATLGFRIEGIKKEDGTVNRDFKKTKTREQVTEAFREFTKGNHNILIAYRDRLKAIRTTLEVSPFFKCHEVIGSSLLFIHDKKEQAKVWMIDFGKTTPLPEGQTLQHDVPWQEGNREDGYLSGLNNLVDILTEMSQDAPLA | Function: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis.
Catalytic Activity: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+)
Sequence Mass (Da): 102376
Sequence Length: 946
Subcellular Location: Cytoplasm
EC: 2.7.1.127
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Q96DU7 | MRRCPCRGSLNEAEAGALPAAARMGLEAPRGGRRRQPGQQRPGPGAGAPAGRPEGGGPWARTEGSSLHSEPERAGLGPAPGTESPQAEFWTDGQTEPAAAGLGVETERPKQKTEPDRSSLRTHLEWSWSELETTCLWTETGTDGLWTDPHRSDLQFQPEEASPWTQPGVHGPWTELETHGSQTQPERVKSWADNLWTHQNSSSLQTHPEGACPSKEPSADGSWKELYTDGSRTQQDIEGPWTEPYTDGSQKKQDTEAARKQPGTGGFQIQQDTDGSWTQPSTDGSQTAPGTDCLLGEPEDGPLEEPEPGELLTHLYSHLKCSPLCPVPRLIITPETPEPEAQPVGPPSRVEGGSGGFSSASSFDESEDDVVAGGGGASDPEDRSGSKPWKKLKTVLKYSPFVVSFRKHYPWVQLSGHAGNFQAGEDGRILKRFCQCEQRSLEQLMKDPLRPFVPAYYGMVLQDGQTFNQMEDLLADFEGPSIMDCKMGSRTYLEEELVKARERPRPRKDMYEKMVAVDPGAPTPEEHAQGAVTKPRYMQWRETMSSTSTLGFRIEGIKKADGTCNTNFKKTQALEQVTKVLEDFVDGDHVILQKYVACLEELREALEISPFFKTHEVVGSSLLFVHDHTGLAKVWMIDFGKTVALPDHQTLSHRLPWAEGNREDGYLWGLDNMICLLQGLAQS | Function: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis . Can phosphorylate inositol 2,4,5-triphosphate to inositol 2,4,5,6-tetraphosphate (By similarity).
Catalytic Activity: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+)
Sequence Mass (Da): 75207
Sequence Length: 683
Subcellular Location: Nucleus
EC: 2.7.1.127
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Q53932 | MPVLMPSADVPTIDISPQLFGTDPTPRRTSRGRSTRPARGSGFFYASHHGIDVRRLQTWSNESTTMTDQRSTTWRSTRYNENNSHVRNGYYMARPGRETVESWCYLNPSFGEDHPMMKAGTPMHEVNVWPDEERHPDFGSFGEQYHREVSASRRCCCGASRWRRQAGESSSNEVTEEDTLSAVSMIRYPYLDPYPEAAIKTGPDGTRLSFEDHLDVSMITVLSKTEVQNLQVETVDGWQSLPTSGENFLINCGTYLGYLTNDYFPAPNHRVKYVNAERLSLPFFLHAGQNSVMKPFTRRTGDRKLNPAVTYGEYLQEGFTR | Function: Removes, in the presence of oxygen, 4 hydrogen atoms from delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to form the azetidinone and thiazolidine rings of isopenicillin.
Catalytic Activity: N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = 2 H2O + isopenicillin N
Sequence Mass (Da): 36577
Sequence Length: 321
Pathway: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine: step 2/3.
EC: 1.21.3.1
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Q8TMI3 | MLDMTERQVESVLIEIPKGSRNKYEYDKEKKVIKFDRMLFSSMVYPCDYGFFPDTLALDGDPLDALVLTWEPTFPGCVIDVHPVALLDMKDDKGRDEKILCVPETDPLWNYIETLEQVPPHLLKEIVHFFETYKNLEGKHVIVIGWEGLDAAVDMLREAKSRYLEKNK | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 19525
Sequence Length: 168
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q8PWY5 | MTERQVECVLIEIPQGSRNKYEYDKERKVIRFDRMLFSSIVYPCDYGFFPDTLALDGDPLDAMVLMWEPTFPGCVIDVHPVAMLDMEDDKGRDEKILCVPQRDPLWNYIKTIEQVPPHLLKEITHFFETYKNLERKDVVVYGWRDLETARKVIQEAKDRYTEQKKLSNQ | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 20066
Sequence Length: 169
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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P47593 | MDKFLIDVIVEIPKNSKIKYEYDRQTGQIRVDRILFGSESYPQNYGFIKNTLDWDGDELDCFIFADQPFLPATVVPTRIVGALEMIDDGEIDTKLLGVIDCDPRYKEINQISDLPKHRIEEILIFLKTYKLLQKKTVIIKGLKDVCWAKKEYEICLQLMKDYGHLSKDQFIQKMQILHPEHYQK | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 21646
Sequence Length: 184
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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O69540 | MQFDVTIEIPKGQRNKYEVDHKTGRVRLDRYLYTPMAYPTDYGFIEDTLGEDGDPLDALVLLPEPLFPGVLVEARPVGMFRMVDEHGGDDKVLCVPVNDHRWDHIHGIIDVPTFELDAIKHFFVHYKDLEPGKFVKAADWVGRDEAEAEVQRSVERFKAGGH | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 18533
Sequence Length: 162
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q98Q96 | MSKIVVNIEIQKDSNIKYEYDRKRGKIVVDRILRGDFRYPANYGYLEDALDWDGDELDVLVYSQEKFLPGTSLNARIVGAMKMIDDGETDTKLIAVHDDDYRLENIKALEDLDSKWLEEIKYFFSNYKNWKRPGITKVSGFENTSWALKEYQECKDLMREYGHLPKKEFISKMMKMHPEKYEI | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 21715
Sequence Length: 183
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q74MY6 | MEVYAFIEVPKGSNVKYEYEDGKLKVDRILYGAMFYPYNYGFIPETLEEDGDPLDVLVITEEPLVPGSYIKVKPIGVLVTEDEKGVDRKIIAVPVKKVDPIYGEIEDISELKEGIKLKIKHFFERYKELEPGKFVKVKEFLGKEEAEKIIKQAQENYKKQ | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 18495
Sequence Length: 160
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q9JVG3 | MADFNQILTTGDVDGGIINVVNEIPAGSNHKIEWNRKLAAFQLDRVEPAIFAKPTNYGFIPQTLDEDGDELDVLLVTEQPLATGVFLEARVIGVMKFVDDGEVDDKIVCVPADDRNNGNAYKTLADLPQQLIKQIEFHFNHYKDLKKAGTTKVESWGDAEEAKKVIKESIERWNKQA | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 19799
Sequence Length: 177
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q9K0G4 | MADFNQILTPGDVDGGIINVVNEIPAGSNHKIEWNRKLAAFQLDRVEPAIFAKPTNYGFIPQTLDEDGDELDVLLVTEQPLATGVFLEARVIGVMKFVDDGEVDDKIVCVPADDRNNGNAYKTLSDLPQQLIKQIEFHFNHYKDLKKAGTTKVESWGDAEEAKKVIKESIERWNKQA | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 19811
Sequence Length: 177
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q6MVH7 | MASQYSVRKVGAPYTLEHRVYIEKDGVPVSPFHDIPLYANAEQTILNMVVEIPRWTNAKQEISKEELLNPIKQDTKKGKLRFVRNCFPHKGYLWNYGAFPQTWEDPNSIHPETKAKGDNDPLDVCEIGELVGYTGQVKQVKVLGVMALLDEEETDWKVIVIDVNDPLAPKLNDVEDVERHLPGLIRATNEWFRIYKIPDGKPENQFAFTGECKNKTYAMDVVRECNEAWERLITGKTAPGGVSTTNVTVQHSSSRVAPDQLPPLPPNENLPPAPIDSSIDKWFFISGASA | Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 32639
Sequence Length: 290
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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P80562 | MDLSRIPAQPKPGVINILIEIAGGSQNKYEFDKDLEAFALDRVLYSSVKYPYDYGFVPNTLADDGDPLDGMVIIDEPTFPGCVIAARPIGFLEMIDGGDRDEKILAVPDKDPRYAHVKSLNDVAPHRLDEIAEFFRSYKNLEKKVTQILGWQDVDQVKALVDQSIKAYK | Cofactor: In the presence of Zn(2+), Mn(2+), Cu(2+), Fe(2+) or Co(2+) ions, activity is very low. In the absence of metal ions, there is no activity.
Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 18961
Sequence Length: 169
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q6DN90 | MWCLHCNSERTQSLLELELDSGVEGEAPSSETGTSLDSPSAYPQGPLVPGSSLSPDHYEHTSVGAYGLYSGPPGQQQRTRRPKLQHSTSILRKQAEEEAIKRSRSLSESYELSSDLQDKQVEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSVTNDGSQLGALVSPECGDLSEPTTLKSPAPSSDFADAITELEDAFSRQVKSLAESIDDALNCRSLHTEEAPALDAARARDTEPQTALHGMDHRKLDEMTASYSDVTLYIDEEELSPPLPLSQAGDRPSSTESDLRLRAGGAAPDYWALAHKEDKADTDTSCRSTPSLERQEQRLRVEHLPLLTIEPPSDSSVDLSDRSERGSLKRQSAYERSLGGQQGSPKHGPHSGAPKSLPREEPELRPRPPRPLDSHLAINGSANRQSKSESDYSDGDNDSINSTSNSNDTINCSSESSSRDSLREQTLSKQTYHKEARNSWDSPAFSNDVIRKRHYRIGLNLFNKKPEKGVQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSTMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCICNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKMKLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKTNEDHVSQVQKVEKLIVGKKPIGSLHPGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGIRLTSSVPGADIKVLINFNAPNPQDRKKFTDDLRESIAEVQEMEKHRIESELEKQKGVVRPSMSQCSSLKKESGNGTLSRACLDDSYASGEGLKRSALSSSLRDLSEAGKRGRRSSAGSLESNVEFQPFEPLQPSVLCS | Function: Guanine nucleotide exchange factor for ARF1 and ARF6 . Guanine nucleotide exchange factor activity is enhanced by lipid binding . Accelerates GTP binding by ARFs of all three classes. Guanine nucleotide exchange protein for ARF6, mediating internalization of beta-1 integrin . Involved in neuronal development (Probable). In neurons, plays a role in the control of vesicle formation by endocytoc cargo. Upon long term depression, interacts with GRIA2 and mediates the activation of ARF6 to internalize synaptic AMPAR receptors (By similarity).
Sequence Mass (Da): 108314
Sequence Length: 963
Domain: The PH domain mediates interaction with lipid membranes that contain phosphatidylinositol-4,5-bisphosphate, but does not bind membranes that lack phosphatidylinositol-4,5-bisphosphate.
Subcellular Location: Cytoplasm
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Q8R0S2 | MWCLHCNSERTQSLLELELDSGVEGEAPSSETGTSLDSPSAYHQGPLVPGSSLSPDHYEHTSVGAYGLYAGPGPQQRTRRPRLQHSTSVLRKQAEEEAIKRSRSLSESYELSSDLQDKQVEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSVTNDGSQLGALVPSECGDLSDPALKSPAPSSDFADAITELEDAFSRQVKSLAESIDDALNCRSLHSEEVPASDTARARDTEPKPGLHGMDHRKLDEMTASYSDVTLYIDEEELSPPLPLSQAGDRPSSTESDLRLRSGGAAQDYWALAHKEDKADTDTSCRSTPSLERPEPRLRVEHLPLLTIEPPSDSSVELSDRSDRSSLKRQSAYERSLGGQQGSPKHGPHGGPPKGLPREEPELRPRPPRPLESHLAINGSANRQSKSESDYSDGDNDSINSTSNSNDTINCSSESSSRDSLREQTLSKQTYHKETRNSWDSPAFSNDVIRKRHYRIGLNLFNKKPEKGIQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSAMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCVCNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKMKLEDFVKNLRGVDDGEDIPRETLIGIYERIRKRELKTNEDHVSQVQKVEKLIVGKKPIGSLHHGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGIRLTSAVPGADIKVLINFNAPNPQDRKKFTDDLRESVAEVQEMEKHRIESELEKQKGVVRPSMSQCSSLKKESGNGTLSRACLDDSYASGEGLKRSALSSSLRDLSEAGKRGRRSSAGSLESNVEFQPFQPPQPPVLCS | Function: Guanine nucleotide exchange factor for ARF1 and ARF6. Guanine nucleotide exchange factor activity is enhanced by lipid binding. Accelerates GTP binding by ARFs of all three classes. Guanine nucleotide exchange protein for ARF6, mediating internalization of beta-1 integrin (By similarity). Involved in neuronal development . In neurons, plays a role in the control of vesicle formation by endocytoc cargo. Upon long term depression, interacts with GRIA2 and mediates the activation of ARF6 to internalize synaptic AMPAR receptors (By similarity).
Sequence Mass (Da): 108015
Sequence Length: 961
Domain: The PH domain mediates interaction with lipid membranes that contain phosphatidylinositol-4,5-bisphosphate, but does not bind membranes that lack phosphatidylinositol-4,5-bisphosphate.
Subcellular Location: Cytoplasm
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O25008 | MLQRIYLDNNATTRIDPKVKEIMDPFLRDHYGNPSSLHQFGTETHPAIAEALDKLYKGINARDIDDVIITSCATESNNWVLKGVYFDECLKKGKNHIVTTVAEHPAVRSTCNFLESLGVEVTYLPINEHGSITAEQVKEAITEKTALVSVMWANNETGLIFPIEEIGAICKEKGVLFHTDAVQAIGKIPVDVLKANADFLSFSAHKFHGPKGIGGLYIRSGVGLTPLFHGGEHMNGRRSGTLNVPYIVGMGEAMKLAVEHLDYEKEVVGKLRDKLEEALLKIPDVMVVGDRIHRVPNTTLVSVRGIEGEAMLWDLNRSNIAASTGSACASEDLEANPVMVAIGASKELAHTAIRLSLSRFNTEAEIDKTIEVFSQAAVRLRNISSSY | Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 42404
Sequence Length: 387
Pathway: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.7
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P57795 | MAIHNCEGENVSTENKAVYMDNSATTPVRKEVVEAMLPYMTENFGNPSSIYEIGKTSKHAINLARKKAADALGAEENEIYFTSGGTESDNWAIKGIAFANRDKGKHIITSSIEHHAVLHTCAWLEGQGFEVTYLPVDKYGMVSPDELRNAIRDDTILISIMFANNEIGTIQPIKEIGEIAKENQIYFHTDAVQAIGHVPIDVKKLNIDLLSLSGHEFEGPKGCGALYIRKGVKIDPLLHGGAQERKRRAGTENVPGIVGLGKATELATAEIEESNRTLLKLRDRLIEGLLKIPKTHLNGHPTQRLANNVNVTFEYIEGESLLLLLNAKGIYASTGSACNSSSLEPSHVLTACGVPHEIIHGSLRLSLGRMNTSEDVDRVLEVVPEIVQKLRNMSPLTPKEYRTL | Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 44336
Sequence Length: 404
Pathway: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.7
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Q6GHV3 | MRIIKYLTILVISVVILTSCQSSSSQESTKSGEFRIVPTTVALTMTLDKLDLPIVGKPTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMSEEVKKMFQKEFKQNDIWKHFKAVKNNHVYDLEEVPFGITANVDADKAMTQLYDLFYKDKK | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Involved in heme (porphyrin) scavenging. Binds Fe(2+) and Fe(3+) heme but the largest fraction is Fe(2+) heme. Functions as a high-affinity heme binding protein and probably has a role in relaying heme-iron from cell wall-anchored isd proteins receptors to the probable permease IsdF (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 33261
Sequence Length: 292
Subcellular Location: Cell membrane
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Q2FZE5 | MMIKNKKKLLFLCLLVILIATAYISFVTGTIKLSFNDLFTKFTTGSNEAVDSIIDLRLPRILIALMVGAMLAVSGALLQAALQNPLAEANIIGVSSGALIMRALCMLFIPQLYFYLPLLSFIGGLIPFLIIILLHSKFRFNAVSMILVGVALFVLLNGVLEILTQNPLMKIPQGLTMKIWSDVYILAVSALLGLILTLLLSPKLNLLNLDDIQARSIGFNIDRYRWLTGLLAVFLASATVAIVGQLAFLGIIVHVVRKLVGGNYRVLIPFSTVIGAWLLLVADLLGRVIQPPLEIPANAILMIVGGPMLIYLICQSQRNRI | Function: Part of the binding-protein-dependent transport system for heme-iron. Responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35078
Sequence Length: 321
Subcellular Location: Cell membrane
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Q9TXD8 | IVGGKTAKFGDYPWMVSIQQKNKKGTFDHICGGAIINVNWILTAAHCFDQPIVKSDYRAYVGLRSILHTKENTVQRLELSKIVLHPGYKPKKDPDDIALIKVAKPIVIGNYANGICVPKGVTNPEGNATVIGWGKISSGGKQVNTLQEVTIPIIPWKKCKEIYGDEFSEFEYSQITPYMICAGAEGKDSCQADSGGPLFQIDANGVATLIGTVANGADCGYKHYPGVYMKVSSYTNWMSKNMV | Function: Peptide isomerase that inverts the chirality at the Ser-81 of omega-Aga IVB. Acts cofactor-independently.
PTM: N-linked glycan at Asn-127 consists of Man3-GlcNAc2-Fuc.
Sequence Mass (Da): 26511
Sequence Length: 243
Subcellular Location: Secreted
EC: 5.-.-.-
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Q9RBP5 | MSTVLVVGADKGIAHSISRQLHDRGEDVIAACLFDGADLAAAGITVEPGVDVTSQESVEALAARLSEKGVKLDAVFHVAGVMWLDEVGSLDYDLIRRQIEINTLGPLRTIEAVRPLLNEGAKVGIVTSRVGSLGDNTSGGMYSYRISKAAANMVGLNFHHDLSKDGVSVLLLHPGMVATDLTKDFPGEHSYITPEQAAAGLIKNIDNLTPETSGRFQHSDGTFLQW | Function: Involved in isoprene degradation . Catalyzes the two-step NAD(+)-dependent oxidation of 2-glutathionyl-2-methylbut-3-en-1-ol (HGMB) to 2-glutathionyl-2-methylbut-3-enoate (GMBA) .
Catalytic Activity: 2-glutathionyl-2-methylbut-3-en-1-ol + H2O + 2 NAD(+) = 2-glutathionyl-2-methylbut-3-enoate + 3 H(+) + 2 NADH
Sequence Mass (Da): 24062
Sequence Length: 226
EC: 1.1.1.398
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Q9RBP4 | MITVYGYVPAWGIPDISPYVTKVVNYLSFTGIEFEYKTQDLATLDQDSPHGKLPYIVDSDGTKVGDSNTIIEYLKNKFGDKLDADLSKQQLAQALAFHRLIEEHLYWSGIIQARWQDDAGWETYIPFIVQGAEVTPEMRVGLDAFRARILDGFNGQGMGRRSEEVVAEFFRADIDALSDFLDDKPFILGDKVHSIDASLYSTLRHIADQPQQWLGSGYVQTKPNLVDYLERIRKQYDI | Function: Involved in isoprene degradation . Catalyzes the glutathione-dependent ring opening of various epoxides . The highest conversion rate is observed with the physiological substrate, 3,4-epoxy-3-methyl-1-butene, which is the primary oxidation product of isoprene . It can also use other epoxides, including epoxyethane, epoxypropane, epithiopropane, epichlorohydrin, epifluorohydrin, epibromohydrin, 1,2-epoxybutane, 1,2-epoxyhexane, cis-2,3-epoxybutane, cis-1,2-dichloroepoxyethane and trans-1,2-dichloroepoxyethane .
Catalytic Activity: 2-glutathionyl-2-methylbut-3-en-1-ol = (3R)-3,4-epoxy-3-methylbut-1-ene + glutathione
Sequence Mass (Da): 27094
Sequence Length: 238
EC: 4.4.1.34
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B1I0S9 | MADTLAIVVAAGRSSRMGEGPKKQYRLLAGRPVLGRTLEVFEHAPAVDGVVLVVAPGEEDWCREEIVTRFGFTKVVAVVPGGEVRRDSVWAGLQALPPCALVLVHDGVRPFVTARQIAAVAEAARECGAATLAVPPKDTVKLGGPPGAPVSTLPRENLWLVQTPQAFRFDVLIKAHHLARERGLAATDDTSLAEAAGYDVRMVPGAYTNIKITTPEDLAFAEALLGGGPVLVGFGYDVHRLVDDRKLILGGVEVPHDRGLLGHSDADVLVHAVMDALLGAAGAGDIGRWFPDDDPTYRGISSMDLLVRVAAFLRERGLETSNLDAVVVAEAPRLSPFISRMRDNLASVLGVSPAAVNVKATTTEGLGFTGSGAGIAAYAVAALRRIVLPGDRVL | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 41482
Sequence Length: 394
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q6ARN9 | MKNGAVIIPAAGSGTRMKLDYPKQYHAVAGTPIIVHTIRAFNKHPCIAKIILVVPQDHLEESKALLQKYQLENISIVTGGARRQDSVLRGLQEVPESIDIVLVHDGARPMVSAELISRCYKGAQQYGAVIAAVPVKDTLKRGAGRIVTGTVDREGLWQAQTPQAARKALLVKAFKENGMRNVTDESTLLEGVGIPVTLIEGSETNIKITRPEDLILAENFLREKKEPMQKIRIGHGFDAHQLVEKRRLILGGVEIPYHLGLAGHSDADVLVHALCDALLGAIGAGDIGRHFPDSSDAFKDIYSIRLLESVMQKVGELNYKIGNADISVICQAPKLAPYLKQMQEIIATSCACQISDINIKATTTEKMGYTGRGEGISCHAVVLLQQ | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 41971
Sequence Length: 386
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q72C30 | MRTWVLLLAAGSGTRLATAGLPDAKQFLPLHGAPLYWASARTMAHVAGIEGIVFVFPPHRVEEERARISALDDGSVLGLDWHVVGGGAARQDSVACGLAALPRSCEAVLVHDAARPFASPALVARVLSALHDGHAGVVPGIPLTDTVKETTDGFVANTPDRSRLVAVQTPQGFTLKALSTAHETARTAGWNVTDDAALLERCGIPVRIVAGEVVNAKITTPEDLAMLDANEPQVTVPCVGWGYDVHRYGEGRPMKLGGVLIPEGPEVVAHSDGDVLLHALADALLGCIGAGDIGLHFPDSDAAFDNANSAMLLDRVLHMTHEARLRLTHVDLTIVAQVPKLSPWRDKIRANVARLLDLPVTSVNFKATTEEGLGFTGEKRGIKAIAAVTGLRPMP | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 41726
Sequence Length: 395
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q5FQD6 | MRIAALLLAAGRGRRFDASSQSGENSSKQFRMLRGKPVIRRAAEALLPHVDVLLPVGDDPLLADSLEGLDILPPVSGGAERHDSVRNGLEALAKLPEPPDLVLVHDGARPCVPAEVVQNVINALKTHEGVIPAVAVIDTIKKAKDGIIVDTVPRDGLWRAQTPQGFRFGTLLELHRTHRDARTDDAALLEQAGHPVAIVEGSEDNIKLTVAEDLMRLEGVIDRNLLPRVGLGYDVHAFEEGRKLILCGIEVPHTKGLAGHSDADVGIHTLCDAIYGALAEGDIGRHFPPSDNKWKDMDSARFLVHAGERIRERGGFLVNADVTLICERPKIGPHAEAMRNRLADLLKVSVSRISVKATTSERLGFTGREEGIAATATVSIMVPDNGEA | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 41815
Sequence Length: 388
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q7VFU3 | MVLDNVSLIMMAAGDSTRFCASNAQTFRCKKQWLRVGEEPLWLVATRNLTHHFSFKQVILTASSKDYVYMQNISPYKVVQGGQTRCQSLRNALKYVDTPLVLVSDVARWDSSDSIIKTMLKALDESVACVVPFVGVADTSFYEGEYLKRESIKLIQTPQLSRVEDLQEALKDTSKDFSDESSALYALGKKIAFVQGSELMNKLTFSSDLKAHITRLSPPSKRVFIGNGIDVHQFEKNKQMWLGGVEIESPFGFKAHSDGDVVLHALSDAILGAIGGGDIGEWFPDTDETYKNADSKMMLSEIYTFAQSVGYELYNADISIIAQTPKIAPYKSAMRECIARILRVPNAHINIKATTTEGLGFVGREEGVCVEACVSMGFINWHTYIKDLH | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 43300
Sequence Length: 389
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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O25664 | MSLIRVNGEAFKLSLESLEEDPFETKETLETLIKQTSVVLLAAGESRRFSQTIKKQWLRSNHTPLWLSVYESFKEALDFKEIILVVSELDYIYIKRHYPEIKLVKGGASRQESVRNALKIIDSAYTLTSDVARGLANIEALKNLFLTLQQTSHYCIAPYLPCYDTAIYYNEALDREAIKLIQTPQLSHTKALQSALNQGDFKDESSAILQAFPDRVSYIEGSKDLHKLTTSGDLKHFTLFFNPAKDTFIGMGFDTHAFIKDKPMVLGGVVLDCEFGLKAHSDGDALLHAVIDAILGAIKGGDIGEWFPDNDPKYKNASSKELLKIVLDFSQSIGFELFEMGATIFSEIPKITPYKPAILENLSQLLGLEKSQISLKATTMEKMGFIGKQEGLLVQAHVSMRYKQKL | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 45529
Sequence Length: 406
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q0C0N0 | MTETVAIIVAGGRGQRAGAERPKQWQMLLGKRVIDWSIAAFVDHPQISQVVIVAGDELGDCSAEPKIIQAKPGNTRTQSVLSGLAAATISEDATVVIHDAARPGIDAATISSLIARLQDPSVSGAAPAMPVADALKTNSGQSWTNVDRTGLVRVQTPQAFRLGEIRAALSAAGPDLVDDLTAIEAAGGRVEIVSGSARLTKITYPEDFDMLARLLSPTGAPRIGKGYDVHEFEAGDHVTLCGVAIPHIAKLKGHSDADAAWHALTDAILGAVALGDIGDHFPPSDPQWKGADSGLFLKEAQRLAEAKGYVIANCDITVICEAPKVKPHREAMRARTAELLGLPLDAVSVKATTTEGLGFTGRREGIAAEAVALLMPKG | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 39494
Sequence Length: 378
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q28Q60 | MEKPAQRATAIIVAAGRGIRAGGGEPKQWRRIAGRSIVEWSVNRFAAHHAGFDVVLVIHPDDEWRLNGLDLPTTLRVVHGGDSRAASVKAGLAVCCDAGHVLIHDVARPCVSLAVIQSVLDATRAGGAAAPALPVTDALWRGDTHVSGTQNRDGLWRAQTPQGFDVSAIRAAHAAHDGTAADDVEVARLAGIDVAIVPGDEANLKITGPEDFARAEALLTGGDMDIRVGNGFDVHRFGPGDQVWLCGISVPHTRGLQGHSDADVGLHTLTDAIYGALAEGDIGTHFPPSDPQWKDAESHIFLTHAVELAANRGFSITNADLTLICEQPKIGPVASAMRARVADLLRIDVARVSVKATTSERLGFTGREEGIAALATITLVAR | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 40213
Sequence Length: 382
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q6ADI0 | MCTASRPRIAVIVVAAGSGTRLGAGSPKAFVTLGGRTLLERSLHAVRCMREPAQVVVVAPEERLAEAAALGEAGFGAAVDVVAGGETRQGSVAAGLGALREGVEIVLVHDAARALTPAAQFDAVVAAVDAGGAGVVPGLPVSDTIKRVGADGEVRETVDRSVLSAVQTPQGFPRDQLVAAYAAATTDETDDAELAAAAGHPVTVIPGDARAFKITTPWDLRRAEELLAGLAAPRIGFGTDTHAFDPSAELWLAGLRWEGEPGLAGHSDGDVVAHAIVDALLSAARLGDIGGVFGTGDPRFSGAHGEVFLTETRRLVEEEGFRIGNVSAQIVGNRPKFAPRRAEAETLLSRVLGAPVSVSATTTDGLGLTGRGEGVAVFATALLLAP | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 39296
Sequence Length: 386
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q472F2 | MSDRRFALIPCAGTGSRAGGSVPKQYQPVAGRPMIWYALAAFSACDAISATALVLAPDDMPLESRFGADIFAGLRFDTAFVGGDTRHASVLAGLHHLAQLGATDTDWVLVHDAARPGLTPAMIHNLVRAVESDNDDDPDAAIGGILAVPVPDTLKRADAGERIGTTVPRDGLWQAQTPQMFRVGVLRQALQDALAAGAVVTDEASAIERLGLHPRLVNGSLRNFKVTYPEDFALAEVLLGTGPARSADSGA | 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): 26331
Sequence Length: 251
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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Q6AAV8 | MPTMVDEHTPPVVAVVVAAGLGTRFGGPVPKQVTSLTGKAVVAVAVESLAAGGCDEAVVVVKEGMHNHLQLALAASPIPVHFVTGGNTRQESVRNGLRFIAQHHRLSDATTVLIHDAVRPLVPAYVVENVIAAVENGAVAVTPVVDVVDTIRQVDGDTSSVVDRSTLRAVQTPQGFKRDIITECHEQLSIEGGSVTDDISCCERYGHHATFVEGSRMSLKITEPVDLDVAEVFAKAAAGAGRHSGRRIGRMLHAVKPSTVARKLGRGSRR | 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): 28502
Sequence Length: 270
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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A0JPF9 | MGTVTIQLSCLRHIRKLCFSCPWEGRRLFKMLLQFHHETQRPLDPGCLLPQDAERSADQPGRAVVDFPVAAVLPAGGSGERMGLTTPKQFCSIFNRPLISYTIQAFERLPWIVMVVVVVAKDNHDLMLNIVRKFNHTKVKVVHGGTTRHRSIYNGLQAFSDSTDSSTPKPKVVIIHDAVRPFVEEDLLLKITLAAKEQGASGAIRPLVSTVIATTSESYLDHSLERAKYRASEMPQGFLYDIIFQAYQRCSEFDLEFGTECLHLALQYCGTNARLIEGPPTLWKVTYKRDLAAAEAIIKETLSVSACIIAEAEEEAVELAKTLQKNLNMMETDVIPCGKESNVQYLSKTRNFIHISASASSSLWVLEMVKCFEDIDHARLYPVVIVWVQLSMTKQSADSQETDEFMALASEVKQRNVLLYGIKIDHSKELEQWQRSLERLGQITLVLIRDRNMALTGQMLHV | Function: Cytidylyltransferase required for protein O-linked mannosylation . Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate (By similarity). 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 (By similarity). 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 (By similarity). Not involved in dolichol production (By similarity).
Catalytic Activity: CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol + diphosphate
Sequence Mass (Da): 52064
Sequence Length: 462
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cytoplasm
EC: 2.7.7.40
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Q47EL2 | MPRHYAIVPAAGSGSRFGAEKPKQYLDLLGRPLIFHTLAALTASPDIERVWVVLAPDDPWWPRYDWSELGSKLETVRCGGATRAESVSNGLRAAAMVAADDDWVLVHDAARPCLSAAMLDALFAELASDPVGGILAVPVADTLKRADAEQRVGATEPRDGLWQAQTPQMFRYGLLGEALEKCRDVTDEAGAIEAVGLKPKLVRGDSTNLKVTYPADLALAAMILRARK | 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): 24573
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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Q3ZAD7 | MFLNEKVGAVIVAAGQSRRMGGQDKIFARLSGKPVLAHTLSVFQQSPEIDDIALVVSEHNLKKAKELVKEYNFSKVIAICSGGELRQDSVSSGLTALCDCGWVLIHDGARPLLDPVSIPEGLEAAKLCGSAVAAVPLKDTVKEISPEGLVEKTLPREKLISVQTPQVFRADIIQKAYRRVGITATDDAQLVEKLKLPVKIFSGAYANIKITTPEDLLMAEILLKKGR | 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): 24556
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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Q9RR90 | MSAPHTSSPRTAALIPAAGSGTRLGLGPKAFVEVAGRSLLARSVAALAPFVDEVVVALPAGMDLPAGVPARAIVGGETRQGSVRRLLEATEAGTVLIHDAARPFVPPPVILALLDAIAATGAATVALPVADTLVRAEGQSWGQLVPREGLWAVQTPQGFRRELLLQAHARAEAEQYAATDDAGLLARLGVQVRLVPGDARLFKVTTPGDLALAEALTGHVDGGWLTVEGEKR | 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): 23895
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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A4J0Y3 | MGNIVAVIPAAGMGSRMGTEVKKQYLKLQDRPILAHTIDALEQVPDITGIVLVVSPGEETLCQELILKGNLFNKIMAVVPGGDHRQTSVYHGLCSLPGDTELVVIHDGARPLVQRAEISHIIKEARRVGAAALAVPVKDTVKLVNDQGYVIATPNREKLWAVQTPQVFNYELILKAHQDAREKGVYATDDCALVEALGQPVKLVQGSYENIKITTPEDMVMAQAFLKRRNCWCE | 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): 25658
Sequence Length: 234
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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B5YF77 | MEKIVGIVVAAGKSKRFGEDKLLINIKGMPIVYYSIRKLHDIKDIEKIILVVRNEMLEYYKEKIKDWKLEKVYKLVLGGEERQDSVYNALKSVDFHCDYVLIHDAARPFVSIKKIEELIKFCTENSLSAILGIPVKDTIKVVDNTTKRIMETLDRSKLWIIQTPQMFPFEIIKEAHKKAREENFVGTDDASLVERLGIPVYVIEGEPFNIKITTKDDLLWMEGILSKSELV | 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): 26688
Sequence Length: 231
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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Q8X7Y4 | MATTHLDVCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQLPLANHPQITVVDGGDERADSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSRTGGILAAPVRDTMKRAEPGKNAIAHTVDRNGLWHALTPQFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIHQENT | 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): 25733
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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Q3ALY8 | MHLLIAAAGSGRRMGADRNKLLLPLAGRPVIAWTIEAALRSERIEWIGIVGQEVDREAILAVLDEPSKPVHWIQGGSTRQESVLCGLAGLPEQARHVLIHDGARCLAEPKLFDRCAAVVEDGTALIAATPVSDTIKRVGSDGVIRDTPDRSELWAAQTPQGFAVDQLRRGHAEAVAQGWTVTDDASLYERLGWPVQVLDAGPANIKVTTPFDLTVAEAVLALRSAG | 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): 24200
Sequence Length: 226
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
|
P74323 | MHLLIPAAGSGKRMGSGHNKLLLNVLGQPLLSWTVQAALASQSIEWIGIMGQPYDFPAFEALLTPLHSPKPVQLIVGGDTRQQSVFNGIQALPPGAKFVLIHDGARCLATPDLFDRCTEALQHCQGLIAAMPVKDTIKIVNADGWITDTPDRQGLWGAQTPQGFDVALLKACHDKGKQEGWEVTDDAALLEKCGQPVKIVPGEDTNLKITTPVDLAIAEFILGQRSAKSA | 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): 24643
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
|
Q47LV0 | MSLDQPAHRRPRVAAAVLAGGVGSRMGSAHPKQLLRLAGQTILERSVAALCAAPEVDEVVVVMNAAHLAEAEKILAEGRYDKVSRIVPGGASRSESSLAALQAVDDYDDNDLLLLHDAARPLVSGRTITACVTELTEVGAVGVAVPSSDTVVQVTLDASGREVIAAVPDRAALRRMQTPQGFRLGVIRRAYARAFAEPGFTATDDCGVVLRYLPEEPVRIVTGEESNIKVTHPSDLAVAEALLRTGVAQ | 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): 26230
Sequence Length: 249
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
|
A6LPA6 | MNVAVILFGGKGERFSKDYPKQFVKFHGKTLMEHTVEKFLENFIHLIIIVVNGEYLEESKKILKKYKRKNIYVILGGKTREFSTLNAVKYLKDLISEDDNVIIHDGARPFVSKEVILRNIDFVNKYGAVVTAVPVENTIAFVENKIVKEIPPRRYLFTLQTPQTFKYSILYKSFRLIKDLEKFTDDSSVVLAAGYNVHVVYGEKTNIKITTKEDLYLIGVEKIEGNI | 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): 26161
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
|
Q9X1B3 | MNVAILLAAGKGERMSENVPKQFLEIEGRMLFEYPLSTFLKSEAIDGVVIVTRREWFEVVEKRVFHEKVLGIVEGGDTRSQSVRSALEFLEKFSPSYVLVHDSARPFLRKKHVSEVLRRARETGAATLALKNSDALVRVENDRIEYIPRKGVYRILTPQAFSYEILKKAHENGGEWADDTEPVQKLGVKIALVEGDPLCFKVTFKEDLELARIIAREWERIP | 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): 25370
Sequence Length: 222
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
|
Q72GN3 | MEVSVLIPAAGNGLRLGRGPKAFLQVGGRTLLEWTLAAFRDAAEVLVALPPGAEPPKGLGAVFLEGGATRQASVARLLEAASLPLVLVHDVARPFVSRGLVARVLEAAQRSGAAVPVLPVPDTLMAPEGEAYGRVVPREAFRLVQTPQGFFTALLREAHAYARRKGLEASDDAQLVQALGYPVALVEGEATAFKITHPQDLVLAEALARVWSA | 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): 22423
Sequence Length: 213
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
|
Q3SK38 | MKFYALIPAAGSGSRMGGAIEKQYMDVNSVPMIAHAMMVLAREPRIARIFVVLSPTDKRWNNYEWQGWEERIEVLRCGGGTRAETVLNALDAIAEVCDPADWVLVHDAARPCLPDEMLGKLLDEVADDPVGGLLAVPVADTLKRAAGDTSSGTRVEATVPRAGLWQAQTPQMFRHGTLTEALRAAGSDMTDEASAIEKLGLQPQLVESDSRNLKVTYPQDLELASLILGKMNA | 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): 25286
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
|
A5CW51 | MSNDYYLIIPAGGIGTRMHSEKDNINRKIKIAKQYLKLDNGLTILDQTLKILLNIDQIKGCIIALANKDYLFTKSKFNNHSKLITTVIGGKKRMNSVFNGLKALTNLAKDDDWILVHDSVRPCVKASEIINLMNQLKHHETGGLLATKVVDTIKQASNNIVNTTIDRSNLWQAQTPQMYRFGVLLKALNTVINDGMNITDEASAIEYLRLKSVLVKSSKSNIKITNSEDLELANFYLTQYKE | 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): 27242
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
|
Q181G8 | MDFIRLKSRAKINLSIDVLGKRQDGYHFVEMIMQTIDLYDIVKIKELDEDEIKVKSTSLDIPLDEDNIVYKAAKILKNKFYIKKGVEIFIEKNIPVAAGMAGGSSNAAAVLVGLNHLWELRLSEDELKEIGLNLGADVPFCISGRPALAQGIGEKLTNIKGLPCDTNILICKPDLFVSTKEVYQGLDLNNIKKRPNNKYLIECLKSEDIKAVSESMVNILENVTIGKHKEISDIKQVMMKNNALGSMMSGSGPTVFGLFKNKEDALIGKKELLKKYKQVYVVNSSQKGVEICGEFN | 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): 32943
Sequence Length: 296
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
|
Q8XIA9 | MKMKAYAKINIALDAIGKREDNYHLLRMIMQTVDLYDVIDIEKSNDSNISISCNKHYVSTDERNLAYKAAVLFRDEFNIKDGVKINIKKNIPVAAGMAGGSTNAAAVLVIMNKLFNVNASLEVLKEIGLKIGADVPYCIEGGTALCEGIGEIITPLKPFENKILVVLKPNFGVSTKEVYTNLDINKIRKHVNIEGLIQAMENDDLDYVSKNMKNVLENVTLKKHTILKNIKEDMRKSGALGAMMSGSGPTVFAFFDDMLTAQRAFEFLKGKYKYSDVYITRTINSNNL | 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): 32086
Sequence Length: 288
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
|
Q8FQZ4 | MRITARAWGKINLHLGVGPAREDGYHELVTVFQTIDLAETITLTTLEDELVEEGSVVRQLTVTGPRGVPTTPDNLAWRAVDALVGRRREHDRTPLPAVELHIDKGIPVAGGMAGGSADAAAALRAVDAWIGPFGEETLLEVAAELGSDVPFCLLGGTKLGTGRGEQLVDMLSRGTYHWALVVSPKGLSTPEVFAKFDEMSLPSSMDVTPMSQALLDGSAGALAEVLENDLAPAALSLRPDLRKTQLAGLRAGALATMVSGSGPTIALLCDDAQSARDVADALMDEGVGLSVHPATSPVPGPAKNRGAHIVSIESE | 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): 32871
Sequence Length: 315
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
|
Q8NRY0 | MKITAKAWAKTNLHLGVGPAHDDGFHELMTVFQTIDLFDTVTLTTLDEELVEEGSVVKQLSVTGARGVPEDASNLAWRAVDALVKRRAEKTPLSAVSLHISKGIPVAGGMAGGSADAAATLRAVDAWIGPFGEDTLLEVAAELGSDVPFCLLGGTMRGTGRGEQLVDMLTRGKLHWVVAAMAHGLSTPEVFKKHDELNPESHMDISDLSAALLTGNTAEVGQWLHNDLTSAALSLRPELRSVLQEGIRSGAHAGIVSGSGPTTVFLCESEHKAQDVKEALIDAGQVYAAYTATGPAASTADQRGAHILTVS | 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): 32630
Sequence Length: 311
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
|
Q4JU24 | MSISHIFGPQQPQYSSVTASAHGKVNLHLGVGPAREDGYHELDTIFQAVSLKEEVTVALRDARGAQDAEAVQVAEAAQEAADAAPCTWSVSGFDSHLVPQDSSNLAWKAVAAIQKLARQAHVPWADAPVHIHIDKGIPVAGGMAGGSADAAAALVAATELYFPDSRASRRPDGAQLSDIAAELGADVPFCLLGGTARGTGKGENLMPVIATGTYHWAIATDKRGLSTPEVFKQLDQQRAAASAASPKAARAGSPEGLIAALRTGNPEEVGKLLVNDLQAPAISLLPSLRETLKAAEEAGAIAAIVSGSGPTVAMLCASADDAVEVATAVSVAGKASSTMTTSSPAAAAGVIKREEVLE | 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): 36500
Sequence Length: 358
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
|
Q2YBH5 | MNGILSTTEVDSQAELSCPAPAKLNLFLHVVGRREDGYHLLQTVFRLVDFADQLHFGLRADGVIKLHTPTPGVPEEQDLCVRAAKLLQRESGTPWGANIFLEKRIPMGGGLGGGSSDAATTLLALNRLWKLGWRRNQLLKLAPELGADVPVFVFSENAFAEGIGEKLLPIALPPAWYLILTPPVHVSTAKVFSSKELTRNTIPIKIPPFSTEQGHNDLEPVVCASYPEVARHLEWLRQLEGARMAAMTGSGACVFAEFATESGARSALGKIPYGMKGFVAQGLDRHPLHDFAEQ | 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): 32008
Sequence Length: 294
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
|
A1SNG8 | MRAPAKVNLHLGVGAPREDGFHPLVTVYQAVGLYDDVTARAAPDWSVGVGLPDWMDDDAVPLNGANIVDRAADLLAAHHGVERTGELHIAKAIPVAGGMAGGSADAAAALVALDRLWGLDTSDDDLLALAARLGSDVPFALLGGTALGTGRGEVVTPVQDRGTWWWVVVPSDTGLSTPEVYRHFDRMFPDAPSQPVPADALLGAIAAGDTWALADALHNDLEAAAIDLRPELGRLIERGEEAGALRGLVSGSGPTCVFLCGSADHARSLAADLSGAGHPVVLAANGPVAGAHLVSYA | 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): 30448
Sequence Length: 297
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
|
Q30ZH4 | MLTVPQQTIRSGCKINLFLEITGVRPDGYHELVTLFYPLSEPFDLMEISPATHGVTVLSERADLCGDKNIICKAWHTFAAAGGTPPPMQVRLAKGVPDGAGLGGGSANAAAVLKLLNTAGGAPRFSDTALAKIAAQVGADVPFFLHNTPCLATGIGEKLVPAPLDLSGWHLVLVCPGVQVSTPWAYNRWDTLYRSGLHHPCGQLPAAHAPAACAQLQTTGPDRPVRAETGCAGRKKNTCRSLTTERQADSKPVSRALWLFNSFETVVFSAYSELRQHKNTLLAHGASAALMSGSGSSLFGLFRDKAQAEAAMLHFCQRSIAVYVHRL | 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): 34850
Sequence Length: 327
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
|
A1AZ43 | MPLHRREAAPAKLNLTLHVTGRRVDGYHLLDSLVVFLDLGDVVTIAPGPLSLSLTGPFAPGLAAEPDNLCLRAARLAGREARITLEKNLPVASGIGGGSADAAAVLRALDASPRRPEALGADVPVCLASRPVRMRGVGEILAPLPALPELNVLLVNPGRGLSTPAVFKALARHDNPPMPEPLPDFPDAQALIGFLHECRNDLEAPAIALMPGIADCLAALRSAGAQLARMSGSGATCFGLFASAAEAQAARARIAGTNPGWWVAASGLAPAKH | 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): 28146
Sequence Length: 273
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
|
Q7U7D2 | MGTITVTAPAKVNLHLEVLGIRSDGFHELAMVMQSIDLADRLSFQTTADAALTLSCDDPSLSLGEDNLVIRAAQLLRSRSGFNELGAAIHLEKRIPIGAGLAGGSSDGAAALVGLNALWGLGHSRSDLQRFAAELGSDMPFCVAGGSQLCFGRGELLEPLPAVQESLAVLLVKDPRVSVSTPWAYRRCRELQGDRYLSGEDAFEQRRQVLRDMAWTQPIRAAEPPPLQNDLQEVVEPETPAVQAALRLLSTLEGTLAVAMSGSGPSCFALFADPTSCAAAQATLEQQLAAEGLQSWCCNLRPDGVRIEA | 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): 32875
Sequence Length: 309
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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