ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P07562 | MKWATWILALGLLVVRTVVAREAPRELCYGHPVHDDRRPVGPATDAQPVNPLAPANATGTDYSRGCEMRLLDPPLDVSSRSSDPVNVTVAWFFDGGHCKVPLVHREYYGCPGDAMPSVETCTGGYSYTRTRIDTLMEYALVNASLVLQPGLYDAGLYIVVLVFGDDAYLGTVSLSVEANLDYPCGMKHGLTITRPGATLPPIAPTAGDHQRWRGCFPSTDEGAWENVTAAEKGLSDDYADYYDVHIFRSESDDEVVHGDAPEAPEGEEVTEEEAELTSSDLDNIEIEVVGSPAAPAEGPATEEGRGAEEDEELTSSDLDN... | Function: Chemokine-binding protein that inhibits neutrophils' chemotaxis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 53722
Sequence Length: 498
Subcellular Location: Virion membrane
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A4Q8F7 | MGALIPSSTLFNIFDFNPKKVRIAFIAVGLRGQTHVENMARRDDVEIVAFADPDPYMVGRAQEILKKNGKKPAKVFGNGNDDYKNMLKDKNIDAVFVSSPWEWHHEHGVAAMKAGKIVGMEVSGAITLEECWDYVKVSEQTGVPLMALENVCYRRDVMAILNMVRKGMFGELVHGTGGYQHDLRPVLFNSGINGKNGDGVEFGEKAFSEAKWRTNHYKNRNGELYPTHGVGPLHTMMDINRGNRLLRLSSFASKARGLHKYIVDKGGESHPNAKVEWKQGDIVTTQIQCHNGETIVLTHDTSLQRPYNLGFKVQGTEGLW... | Cofactor: Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
Function: Glycosidase that has specific alpha-N-acetylgalactosaminidase activity.
Catalytic Activity: Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood gr... |
Q02643 | MDRRMWGAHVFCVLSPLPTVLGHMHPECDFITQLREDESACLQAAEEMPNTTLGCPATWDGLLCWPTAGSGEWVTLPCPDFFSHFSSESGAVKRDCTITGWSEPFPPYPVACPVPLELLAEEESYFSTVKIIYTVGHSISIVALFVAITILVALRRLHCPRNYVHTQLFTTFILKAGAVFLKDAALFHSDDTDHCSFSTVLCKVSVAASHFATMTNFSWLLAEAVYLNCLLASTSPSSRRAFWWLVLAGWGLPVLFTGTWVSCKLAFEDIACWDLDDTSPYWWIIKGPIVLSVGVNFGLFLNIIRILVRKLEPAQGSLHT... | Function: Receptor for GRF, coupled to G proteins which activate adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone gene transcription and growth hormone secretion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47402
Sequence Length: 423
Subcellular Location: Cell membrane
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P32082 | MDGLMWATRILCLLSLCGVTLGHLHLECDFITQLRDDELACLQAAEGTNNTSLGCPGTWDGLLCWPPTGSGQWVSLPCPEFFSHFGSDTGFVKRDCTITGWSNPFPPYPVACPVPLELLTKEKSYFSTVKIIYTTGHSISIVALCVAIAILVALRRLHCPRNYIHTQLFATFILKASAVFLKDAAIFQGDSTDHCSMSTVLCKVSVAISHLATMTNFSWLLAEAVYLSCLLASTSPRSKPAFWWLVLAGWGLPVLCTGTWVGCKLAFEDTECWDLDNSSPCWWIIKGPIVLSVGVNFGLFLNIICILLRKLEPAQGGLHT... | Function: Receptor for GRF, coupled to G proteins which activate adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone gene transcription and growth hormone secretion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47004
Sequence Length: 423
Subcellular Location: Cell membrane
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Q8JFY4 | MRQMKRTAYIILLVCVLALWMDSVQAGSSFLSPSQRPQGKDKKPPRVGRRDSDGILDLFMRPPLQDEDIRHITFNTPFEIGITMTEELFQQYGEVMQKIMQDLLMDTPAKE | Function: Ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
PTM: O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylati... |
Q9BDJ6 | MPAPWTICSLLLLSVLCMDLAMAGSSFLSPEHQKLQRKEAKKPSGRLKPRTLEGQFDPEVGSQAEGAEDELEIRFNAPFNIGIKLAGAQSLQHGQTLGKFLQDILWEEAEETLANE | Function: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity).
PTM: O-octanoylated by GOAT/MBOAT4... |
Q8AUU1 | MPLRRRASHMFVLLCALSLCVESVKGGTSFLSPAQKPQGRRPPRMGRRDVAEPEIPVIKEDDQFMMSAPFELSVSLSEAEYEKYGPVLQKVLVNLLGDSPLEF | Function: Ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity). Has an appetite-stimulating effect.
PTM: O-octanoylated by GOAT/MBOAT4 (By similarity... |
Q90W22 | MNFGKAAIFGVVLFCLLWTEGAQAGLTFLSPADMQKIAERQSQNKLRHGNMNRRGVEDDLAGEEIGVTFPLDMKMTQEQFQKQRAAVQDFLYSSLLSLGSVQDTEDKNENPQSQ | Function: Ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
PTM: O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylati... |
Q76IQ4 | MPLKRNTGLMILMLCTLALWAKSVSAGSSFLSPSQKPQVRQGKGKPPRVGRRDIESFAELFEGPLHQEDKHNTIKAPFEMGITMSEEEFQEYGAVLQKILQDVLGDTATAE | Function: Ligand for growth hormone secretagogue receptor type 1 (GHSR). Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity). Induces the release of growth hormone from the pituitary.
PTM: O-octanoylated by GOAT/MBOAT4 (By similarity... |
A0MLS4 | MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRAQQRKESKKPPAKLQPRALGGWLRPEDGDQAEGAEDELEIQFNAPFDVGIKLSGVQYQQHSQALGKFLQDILWEEAKEAPADK | Function: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity).
PTM: O-octanoylated by GOAT/MBOAT4... |
Q9QYH7 | MVSSATICSLLLLSMLWMDMAMAGSSFLSPEHQKAQQRKESKKPPAKLQPRALEGWLHPEDRGQAEEAEEELEIRFNAPFDVGIKLSGAQYQQHGRALGKFLQDILWEEVKEAPANK | Function: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
PTM: O-octanoylated by GOAT/MBOAT4 (By similarity)... |
Q9Z254 | MPLGLGRRKKAPPLVENEEAEPSRSGLGVGEPGPLGGSGAGESQMGLPPPPASLRPRLVFHTQLAHGSPTGRIEGFTNVKELYGKIAEAFRLPAAEVMFCTLNTHKVDMDKLLGGQIGLEDFIFAHVKGQRKEVEVFKSEDALGLTITDNGAGYAFIKRIKEGSVIDHIQLISVGDMIEAINGQSLLGCRHYEVARLLKELPRGRTFTLKLTEPRKAFDMISQRSSGGHPGSGPQLGTGRGTLRLRSRGPATVEDLPSAFEEKAIEKVDDLLESYMGIRDTELAATMVELGKDKRNPDELAEALDERLGDFAFPDEFVFD... | Function: May be involved in G protein-linked signaling.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36133
Sequence Length: 333
Subcellular Location: Cytoplasm
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P48546 | MTTSPILQLLLRLSLCGLLLQRAETGSKGQTAGELYQRWERYRRECQETLAAAEPPSGLACNGSFDMYVCWDYAAPNATARASCPWYLPWHHHVAAGFVLRQCGSDGQWGLWRDHTQCENPEKNEAFLDQRLILERLQVMYTVGYSLSLATLLLALLILSLFRRLHCTRNYIHINLFTSFMLRAAAILSRDRLLPRPGPYLGDQALALWNQALAACRTAQIVTQYCVGANYTWLLVEGVYLHSLLVLVGGSEEGHFRYYLLLGWGAPALFVIPWVIVRYLYENTQCWERNEVKAIWWIIRTPILMTILINFLIFIRILGI... | Function: This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
PTM: N-glycosylation is required for cell surface expression and lengthens receptor half-life by preventing degradation in the ER.
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
P43218 | MPLRPRLLLLCLWGLLLQQAETDSEGQTTGELYQRWERYARECEETLTAADPPSGMVCNGSFDMYVCWDYTAANTTAQASCPWYLPWYRHVAAGYVFRQCGSDGQWGPWRDHTQCENPEKNGAFQDQRLILERLQVVYTVGYSLSLGTLLLALLILSLFRRLHCTRNYIHMNVFLSFMLRAVAILTRDRLLPTLGPYPGDRTLTLRNQALAACRTAQIVTQYCVGANYTWLLVEGVYLHHLLVIVGGSEKGHFRCYLLLGWGAPALFVIPWVIVRYLLENTQCWERNEVKAIWWIIRTPILITILINFFIFIRILGILVS... | Function: This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
PTM: N-glycosylation is required for cell surface expression and lengthens receptor half-life by preventing degradation in the ER.
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q88IU0 | MNAFTQIDELVMPLPLEPQGYTIAPSKQSPRLLELTFARETVEAFVQAVAQWPVQALEYKSFLRFRVGEILDELCQGTLRPVLLNTILDRATGGMLITPIGLDDVSQAEDMVKFTTACAHLIGRSNYDAMSGQFYARFVVVNSDNSDSYLRQPHRVMELHNDGTFVNQITDYVLMLKIDEKNMEGGNSLLLHLDDWEQCEAFFRHPLARREMRWTAPPSKKVAEDVFHSVFDTDAEGRPTMRYIDQFVQPENYEEGIWLNALSESLEGSGKKVSVPVGVGSFLLINNLFWLHGRDRFTPHEGLRRELMRQRGYVAFPKPL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Acts as an alpha-ketoglutarate-dependent dioxygenase catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate (L2HG) . Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (By similarity). Is extremely ... |
Q97UY8 | MVRIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGEINELEGKVTNEGVVIGSLRFPVSVSSDRAIIGIRPEDVKLSKDVIKDDSWILVGKGKVKVIGYQGGLFRITITPLDS... | Function: Part of the ABC transporter complex GlcSTUV involved in glucose uptake (Probable). Responsible for energy coupling to the transport system . In vitro, as a free subunit, exhibits a constitutive ATPase activity .
Catalytic Activity: ATP + D-glucose(out) + H2O = ADP + D-glucose(in) + H(+) + phosphate
Location T... |
O80816 | MGSSYQESPPLLLEDLKVTIKESTLIFPSEETSERKSMFLSNVDQILNFDVQTVHFFRPNKEFPPEMVSEKLRKALVKLMDAYEFLAGRLRVDPSSGRLDVDCNGAGAGFVTAASDYTLEELGDLVYPNPAFAQLVTSQLQSLPKDDQPLFVFQITSFKCGGFAMGISTNHTTFDGLSFKTFLENLASLLHEKPLSTPPCNDRTLLKARDPPSVAFPHHELVKFQDCETTTVFEATSEHLDFKIFKLSSEQIKKLKERASETSNGNVRVTGFNVVTALVWRCKALSVAAEEGEETNLERESTILYAVDIRGRLNPELPPS... | Function: Required for double fertilization of the egg cell and the central cell by two sperm cells, resulting in the formation of the embryo and the endosperm . Involved in the regulation of embryonic expression of PHE1 . Essential in maternal tissues to ensure the paternal embryonic expression of several genes, inclu... |
Q17339 | MPSCTTPTYGVSTQLESQSSESPSRSSVMTPTSLDGDNSPRKRFPIIDNVPADRWPSTRRDGWSSVRAPPPARLTLSTNNRHIMSPISSAYSQTPNSLLSPAMFNPKSRSIFSPTLPATPMSYGKSSMDKSLFSPTATEPIEVEATVEYLADLVKEKKHLTLFPHMFSNVERLLDDEIGRVRVALFQTEFPRVELPEPAGDMISITEKIYVPKNEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMVRGKGSMRDKSKESAHRGKANWEHLEDDLHVLVQCEDTENRVHIKLQAALEQVKKLLIPAPEGTDELKRKQLMEL... | Function: RNA-binding protein which recognizes the 5'-UACUCAU-3' RNA consensus sequence . Binds sequences in both the 5'coding and the 3'-UTR region of rme-2 mRNA . Binds sequences in the 3'-UTR region of cye-1 mRNA. Binds to cyb-2.1, cyb-2.2 and cyb-3 mRNA . Binds sequences in the 3'-UTR region of tra-2 mRNA . Binds t... |
Q0GYU5 | MSSGRTVTLNTGYKIPQIGYGTWQAAPGEVGAGVFEALKVGYRHLDLAKVYGNQKEVGEGIKKALAEVPGLKREDIFITSKLWNNSHKPEDVEPALDDTLAELGLDYLDLYLIHWPVAFAPGADLFPKSEDGSEVQLNQNVSIVQTWKAMTELPKSKVRSVGVSNFTIEHLDAVIEATGVVPAVNQIERHPRLPNQPLIDYCAKKGIIITAYSAFGNNTKGLPLLVSSDEVKAVADNLSKKQGKTVTPAQVILAWSQIGGHTVIPKSVTKARIAENFQEVELDDEAIAALNKLGEKPQRFNIPYTYKPRWNINLFNTEEE... | Function: Mediates the conversion of L-glyceraldehyde to glycerol in D-galacturonate catabolic process. Also able to reduce D-glyceraldehyde.
Catalytic Activity: glycerol + NADP(+) = H(+) + L-glyceraldehyde + NADPH
Sequence Mass (Da): 36291
Sequence Length: 331
Pathway: Carbohydrate acid metabolism.
EC: 1.1.1.372
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O13702 | MIGPRLCAATPRFPLVSLAHRNSKVFALASSNAVAQRWGKRFYAPIETETPHKVGVEFEESKDRIFTSPQKYVQGRHAFTRSYMYVKKWATKSAVVLADQNVWNICANKIVDSLSQNGMTVTKLVFGGEASLVELDKLRKQCPDDTQVIIGVGGGKTMDSAKYIAHSMNLPSIICPTTASSDAATSSLSVIYTPDGQFQKYSFYPLNPNLIFIDTDVIVRAPVRFLISGIGDALSTWVETESVIRSNSTSFAGGVASIAGRYIARACKDTLEKYALSAILSNTRGVCTEAFENVVEANTLMSGLGFENGGLAAAHAIHNG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Glycerol dehydrogenase involved in the assimilation of glycerol.
Catalytic Activity: glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH
Sequence Mass (Da): 49433
Sequence Length: 450
Pathway: Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (o... |
Q06104 | MDNFESTAEGNLSIGNKRVYELRKRNFQRNLVNNLSFLGYVLISLEYIKYDRTVWTLITRAIVQSLISSPFPSDAKLRRLATLGADNNTTGVATLPGGRSIRFPGMFGTEMLYNSSSEAEQQDHDDTAIVSMKKQIRKFLFHGCLSLNMLFIILTILFPIDFFEPLSGSEPVDDGPKNTPSPFSNSDGLLLGERRGGLFLQMIGERLPKSNFSGNLGLVMFEFSILIVQFTLFSLTCVVLADLDFEEPERLEPVNSDGYDGSVIVARIPLNKTMNAILNDGNINDNNENASNSV | Function: Component of the Golgi/endosome-localized DSC E3 ubiquitin ligase complex involved in the targeting of the DSC complex to the Golgi apparatus and endosome membranes via the AP3 pathway to ubiquinate Golgi/endosome membrane proteins . Competes with VLD1 to determine the subcellular localizations of the DSC com... |
Q9FN15 | MLRLIVNYPLIPKISHRVCSNSSSKLGSYYDSSSIIKYGGISDVVGKKQELFLSVSVKAVEDKGNNGGGSMSFSGQSWDPSSEIEVPSDQRPVNEYSSLKEGMLYSWGELGPSEFFIRLGGLWLVTFTVLGVPVAAASFNPSREPLRFILAAGTGTLFLVSLIVLRIYLGWSYVGDRLLSAVIPYEESGWYDGQMWVKPPEVLARDRLLGSYKVKPVIKMLKQTLIGTGALLVSAFVLFVFATPVEDFFKTTLGSTENQPEVSISRTSNKFNIRKEQLLRLPVDVVTDDDLAAAAAEAADGRPVYCRDRYYRALAGGQYC... | Function: Required for growth in low iron conditions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36114
Sequence Length: 327
Subcellular Location: Membrane
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Q6DFA8 | MYPNSPSLGRIPLPLPCARQQQTSAYLSKVPVSVAPDLLSPEQFFQASLNIHKNANLPRLLMNGNVLTVPPLSSPPWSYLNHSPLISPGSPPSSFQNRKRRSDEGNSPYDVKRQRFQSPQEQTVNHQAVPLRGDIRCSYPGSPAFPLLQSPSPPVLKGHSSNSGDCWLYDHIDTTLPVAKDKLSKQILDLFQALQQQVCDLKKKDICRAELQREIQQIFPQSRLYLVGSSLNGFGIRSSDADLCLVLKEEPMNQNTEARHILSLLHKHFYTRLSYIERPQFIRAKVPIVKFRDKVSGAEFDLNVNNVVGIRNTFLLRTYA... | Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs during oocyte maturation. Plays a central role during oocyte maturation b... |
Q503I9 | MLPRPYIFSHNDGPSSHLFQHVLPHNVSQQQRIEAHLNSTNNFIGPPMNAPRFIPTYQWTPVELSDVACSPNGPMGNNRKRRIQDNSDINLKRQRFSCPSPHNQSARNSNFTSQPVTRPVTGREVTCPTCSSATFIPGGCVPSLGETCHQNAFSPSSVKDKLSQQILNLFFACEQQSDDLEKKESCRAALQTDIQKIFPCAKVFLGGSSLNGFGSRSSDADLCLVIEEGPVNHRKDAVYVLSLVRKLLYKLSYIEKPQLIRAKVPIVKFRDRISGVEFDLNFNNTVGIRNTFLLRTYAFVEKRVRPLVLVIKKWANHHCI... | Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. May not play a role in replication-dependent histone mRNA degradation (B... |
Q6PIY7 | MFPNSILGRPPFTPNHQQHNNFFTLSPTVYSHQQLIDAQFNFQNADLSRAVSLQQLTYGNVSPIQTSASPLFRGRKRLSDEKNLPLDGKRQRFHSPHQEPTVVNQIVPLSGERRYSMPPLFHTHYVPDIVRCVPPFREIAFLEPREITLPEAKDKLSQQILELFETCQQQISDLKKKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKEEPCFFQVNQKTEARHILTLVHKHFCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHQI... | Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs . Does not play a role in replication-dependent histone mRNA degradation ... |
Q0GYU4 | MASKTYTLNTGAKIPAVGFGTFANEGAKGETYAAVTKALDVGYRHLDCAWFYHNEDEVGDAVRDFLARRPDVKREDLFICTKVWNHLHEPEDVKWSAKNSCENLKVDYIDLFLVHWPIAAEKNSDRSVKLGPDGKYVINQALTENPEPTWRAMEELVESGLVKAIGVSNWTIPGLKKLLQIAKIKPAVNQIEIHPFLPNEELVAFCFENGILPEAYSPLGSQNQVPSTGERVRDNPTLKAVAERSGYSLAQILLAWGLKRGYVVLPKSSTPSRIESNFNIPELSDEDFEAIQQVAKGRHTRFVNMKDTFGYNVWPEEE | Function: Glycerol oxidoreductase probably involved in glycerol synthesis.
Catalytic Activity: glycerol + NADP(+) = dihydroxyacetone + H(+) + NADPH
Sequence Mass (Da): 35721
Sequence Length: 318
EC: 1.1.1.156
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Q91YI6 | MFPNSILGRPPFTPTHQQHNNFFALSPTLYSHQQLIDAQFNFQNVDLSRAVSLQPLTYGTVSPIQTSTSPLFRGRKRISDEKAFPLDGKRQRFHSPHQEPTIINQLVPLSGDRRYSMPPLFHTHYIPDIVRCVPPLREIPLLEPREITLPEAKDKLSQQILELFETCQQQASDLKKKELCRAQLQREIQLLFPQSRLFLVGSSLNGFGARSSDGDLCLVVKEEPCFFQVNQKTEARHILTLVHKHFCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNTVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHDI... | Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation (... |
Q8CWX0 | MKILFVAAEGAPFAKTGGLGDVIGALPKSLVKNNNEVSVILPYYDVVDAKFGDQIEDLFYFFTNVGWRREYVGIKHIFRDGVDFYFIDNKHYFYRGQIYGEFDDGERFAYFQLAALEAMEKIQFIPDILHVHDYHTAMIPYLLKEKYHWINAYHGIKTVFTIHNIEFQGQFNPSMLGELFGVGDERYRDGTLRWNDCLNWMKAAVLYADRVTTVSPSYAKEIMTPEFGKGLDQIMRMESGKLSGVVNGIDTDLFDPETDPHLAVHFSKDDLSGKAKNKAALQERVGLPVREDVPLVGIVSRLTDQKGFQLVVDQLNTMMQ... | Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Mass (Da): 54312
Sequence Length: 476
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.21
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Q3BYI0 | MSERQGGQEQRTEADGMTTEGISETSQTLQALANGLPADAFAVLGPKPLAEGRRQVRVLAPGAEAMGLIDPRGKLLARMQASAIDGVFEGILAADGPYRLRIVWPDRVQEVEDPYAFAATLDESLLLQIAAGDGQAVRRALGAQHVHCGDVPGVRFAVWAPHAQRVAVVGDFNGWDVRRHPMRQRIGGFWELFLPRVEAGARYKYAVTAADGRVLLKADPVARQTELPPATASVVPSAAAFAWTDAAWMANRDPGAVPAPLSIYEVHAASWRRDGHNQPLDWPTLAEQLIPYVQQLGFTHIELLPITEHPFGGSWGYQPL... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
D2WL32 | MVSLSNQTRFSFHPNNLVVSEKRRLGISGVNFPRKIKLKITCFAAERPRQEKQKKKSQSQSTSDAEAGVDPVGFLTRLGIADRIFAQFLRERHKALKDLKDEIFKRHFDFRDFASGFELLGMHRHMEHRVDFMDWGPGSRYGAIIGDFNGWSPTENAAREGLFGHDDYGYWFIILEDKLREGEEPDELYFQQYNYVDDYDKGDSGVSAEEIFQKANDEYWEPGEDRFIKNRFEVPAKLYEQMFGPNSPQTLEELGDIPDAETRYKQWKEEHKDDPPSNLPPCDIIDKGQGKPYDIFNVVTSPEWTKKFYEKEPPIPYWLE... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. Essential during embryogenesis.
Catalytic Activity: Transfers a segment ... |
A6VP15 | MTTFVTQDTINAFFDGRHADPFAVLGMHETDNGIEIRALLPDAGRVVVIDKETQDEVCELSRIDERGFFAGIMPQRNSFFNYQLQVSWGNEVLRIEDPYRFHPMIQELDNWLLAEGSHLRPYEVLGAHFMECDHVSGVNFRLWAPNAKRVSVVGDFNYWDGRRHPMRFHQASGVWELFIPKVALGDLYKFELLDNNNRLRLKSDPYAFAAQLRPDTASQISVLPEIQEMTAARRKANQLDQPISIYEVHLGSWRRNLANNFWLNYDEIADELIPYVKEMGFTHIELLPISEFPFDGSWGYQPIGLYAPTSRFGSPEGFKR... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q8U8L4 | MKKPLNSAEEKKTGDITKAEIEAIKSGLHSNPFALLGVHETPEGFSARCFIPGAEEVSVLTLDGNFVGELKQIDPDGFFEGRIDLSKRQPVRYRACRDDAEWAVTDPYSFGPVLGPMDDYFVREGSHLRLFDRMGAHPLKLEGVEGFHFAVWAPNARRVSVVGDFNNWDGRRHVMRFRKDTGIWEIFAPDVYAGCAYKFEILGANGELLPLKADPYARRGELRPKNASVTAPELTQKWEDQAHREHWAQVDQRRQPISIYEVHAGSWQRREDGTFLSWDELAAQLIPYCTDMGFTHIEFLPITEHPYDPSWGYQTTGLYA... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q21WG7 | MKSDHDIYLFREGTHAKLYNKLGCHLQSNGGANFAVWAPNAESVSVVGDWNYWSGNVDRLDLRDDGSGIWQGFVENAVRGQGYKYRIQSSHGSYGVDKADPFAFYAEPPPATASRVWSLEHDWKDDQWMSSRGPKNALDAPMSIYEIHLGSWRRQDGHFLDYRELAHSLADYVIEMGFTHVELMPVTEHPFYGSWGYQTTGYFAPTSRFGTPQDFMHFVDHLHQRGIGVLLDWVPSHFPTDEHGLGYFDGTHLFEHSDPRQGFHPEWNSSIFNYGRNEVRSFLISSGLFWLDKYHLDGLRVDGVASMLYLDYARKEDEWI... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q0AA26 | MRVYDPHAEAVAFEDGTKLPRRPGSDFFEGPLPAGLSAPYRLRRTSQDGAAHTAHDPYAFGPALPDYDLHLFGEGRHYHAQRFLGAHPLEHEGVPGVRFAVWAPNAERVSVVGDFNRWDGRCHPMRVRGGSGVWELFIPGLPDGSLYKFELRNRDSGAVLVKTDPYGRRYQLRPDSAAVVEPPADYAWNDREWMAARREDQWQSIPISIYEVHLGSWQRAGDGSFLDYRTLAHRLVDHVLATGFTHIELLPITEHPFDGSWGYQTTGYFAPTTRFGAPDDFRYFVDHCHRHGIGVILDWVPAHFPRDDWALANFDGTPLY... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
O66936 | MKKFSLISDYDVYLFKEGTHTRLYDKLGSHVIELNGKRYTFFAVWAPHADYVSLIGDFNEWDKGSTPMVKREDGSGIWEVLLEGDLTGSKYKYFIKNGNYEVDKSDPFAFFCEQPPGNASVVWKLNYRWNDSEYMKKRKRVNSHDSPISIYEVHVGSWRRVPEEGNRFLSYRELAEYLPYYVKEMGFTHVEFLPVMEHPFYGSWGYQITGYFAPTSRYGTPQDFMYLIDKLHQEGIGVILDWVPSHFPTDAHGLAYFDGTHLYEYEDWRKRWHPDWNSFVFDYGKPEVRSFLLSSAHFWLDKYHADGLRVDAVASMLYLD... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q96VA4 | MGTSQAVDSSPPDGTGVIQLDPWLEPFRDALKQRFSFIEGWVKAINETEGGLETFSKGYERFGLNVQSNGDIIYREWAPNAVQAQLVGEFNNWDVTAHPMTKNGFGVWEVTVPAVNGAPAIPHDSKIKISMVIPSGERIYRIPAWIKRVVQDLSVSPTYEAVFWNPPTEKQYKFQYSRPKRPESLRIYEAHVGISSPETKVATYKEFTSNMLPRIKYLGYNAIQLMAIMEHAYYASFGYQVNNFFAASSRYGTPEDLKELVDKAHSMGLVVLLDVVHSHASKNVLDGLNMFDGTDHLYFHGGGKGRHELWDSRLFNYGHH... | Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 78751
Sequence Length: 689
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q15VD0 | MQLEKQLQHAQCTFPFSHLGLLKTDNAFTITAWVPNATGIKVIDLATDKAIGSLKRQAQSDLFTAEFTKGNPPAVYAFEVKNAQGSYRIIDPYQFQDQAFHAVHFVDHLPKNVYQQLGAQLIDLDVGLKTPIAATRFAVFAPNASAVSVIGDFNYWDGSCLPMQKTDFGYWVLVVPGVKAGDKYKYQIKDAHGNELPHKADPVGFYAEQYPSHASVVFDHEQYQWQDTKWQQQVKGDKYTQAMSIYEVHLGSWKRPDSQSGKTYLSYHELVDELIPYVKDMGYTHLELLPISEFPFDGSWGYQPVGLFAPTSRFGGPDDF... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q9I1W2 | MSEPMSERERWQLELDKLQRGLQGDPFAFLGPQRDPGGEGGVLRAYLPGAQRVELLDEDGATLAELEQSDPGSGLFQRHLERLPPRYRLRVHWPDGVQESEDPYAFGPLLGELDLYLFAEGNHRQLASCLGAQLTRHEGVEGVRFAVWAPNAVRVSVVGDFNGWDGRRHPMRRRYPSGVWELFVPRLGEGELYKYELQGHDGLLPLKADPLALACETPPGTASKTCAALRHEWRDQDWLARRAERQGYAAPLSIYEVHAGSWRHRDGRPPHWSELAEELIPYVRQLGFTHIELMPVMEHPFGGSWGYQPLGLFAPTARYG... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q88FN1 | MNVTTRENGGLRQRDLDALARAEHADPFAVLGPHGDGAGGQVVRAFLPNALKVRIQARDDGRVLAEMEQGSLPGLFSAHLDKAQPYQLHIVWAGGEQVTEDPYSFGPQLGDMDLHLFAEGNHRDLSGRFGAQPTQVDGIDGVCFSVWAPNARRVSVVGDFNNWDGRRHPMRLRHGAGVWELFIPRLGVGETYKFEVLGKDGILPLKADPLARATELPPSTASKVAGELSHAWQDHDWMAQRAQRHAYNAPLSIYELHPGSWRCELDEAGEIGRFYNWRELAERLVPYVQELGFTHIELLPIMEHPFGGSWGYQPLSMFAP... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q8XT76 | MTSVHDFATATRPATPSAAAQEPAPALPPGLDRNTLDALTHGRLGDPFAVLGPHRLETAEGERPHRVVRAFHPGARRVQAIDPRGQVMAELAPVGRTGLFHGRLPDDAPDADGHPGAYRLRVVWPAGAGHEAVQEAEDPYAFGLLLGDLDLHLIAEGRHWELARCLGAQAMRQDDVAGVRFAVWAPNARRVSVVGDFNQWDGRRHPMRLRHGTGVWELFVPAGLGAGPGSRYKFELVGADGHLLVKADPVARRTEAPPATASVVADPLPFRWSDAAWMETRAARQRPDAPIAIYEVHAGSWLRDVEDGGRSLDWDALGER... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q7UVH1 | MNSQLSLSTIQSLVDGSVANPGSLLGRHPVNYRGREATSVRVLEPNAESVWLIDSASGLRRPMRRLHPGGFFEAICDEPITKPSTSRLQMIDKTGKEIKTTSPYTVPSIFSDLDRYLIGEGRHNQLYERLGAQLREVDGVKGVNFAVWAPNARSVQVVGDFNGWDGRGHVAQPVESTGIWELFLPGATVGQKYKFRIQTQHGHWMDKCDPMAFAAELPPLTANIITDINTYSWNDSDWLQQRAEMDPMHTPMNVYEVHLGSWQKGPGRTHGWLDYRDLAKRLVDYCHRMNFTHVELMPISEHPFTGSWGYQSVGYYAPTS... | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan cha... |
Q9CHN1 | MAIEMLGLILAGGQGTRLGKLTKDVAKPAVPFGGRYRIIDFALSNCANSNVKNVGVITQYQPLTLNAHIGNGAPWGLNGINSGVTILQPYSSQEGSKWFEGTSHAVYQNISYIDQQNPEYVLILSGDHIYKMDYEAMLESHKEREASLTVSVMEVPLEEASRFGIMNTDDNDRIIEFEEKPKEPKSNLASMGIYIFNWKRLREVLVNGYSKGNPMEDFGGDVIPAYIEAGENVFAYRFKGYWKDVGTIDSLHQSSMEFLDLNNELNITDKSWRIYSHNDISAPQFITEKSNVKNALVGDGCYVDGTVLHSILSQNVHVQE... | Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glu... |
P55233 | MDASAAAINVNAHLTEVGKKRFLGERISQSLKGKDLRALFSRTESKGRNVNKPGVAFSVLTSDFNQSVKESLKYEPALFESPKADPKNVAAIVLGGGAGTRLFPLTSRRAKPAVPIGGCYRLIDVPMSNCINSGIRKIFILTQFNSFSLNRHLARTYNFGDGVNFGDGFVEVFAATQTPGESGKKWFQGTADAVRQFFWAFEDSKSKDVEHIVILSGDHLYRMDYMSFWQKHIDTNADITVSCIPMDDSRASDYGLMKIDHTGRIVHFAEKPKGSDLTAMQVDTTVLGLSDLEAMSNPYIASMGVYVFRTDVLMELLNRK... | Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Mass (Da): 57717
Sequence Length: 522
Pathway: Glycan biosyn... |
Q00081 | NKIKPGVAYSVITTENDTQTVFVDMPRLERRRANPKDVAAVILGGGEGTKLFPLTSRTATPAVPVGGCYRLIDIPMSNCINSAINKIFVLTQYNSAPLNRHIARTYFGNGVSFGDGFVEVLAATQTPGEAGKKWFQGTADAVRKFIWVFEDAKNKNIENIVVLSGDHLYRMDYMELVQNHIDRNADITLSCAPAEDSRASDFGLVKIDSRGRVVQFAEKPKGFDLKAMQVDTTLVGLSPQDAKKSPYIASMGVYVFKTDVLLKLLKWSYPTSNDFGSEIIPAAIDDYNVQAYIFKDYWEDIGTIKSFYNASLALTQEFPE... | Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Mass (Da): 52253
Sequence Length: 470
Pathway: Glycan biosyn... |
P55236 | SVTADNASETKVREIGQEKSS | Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Mass (Da): 2236
Sequence Length: 21
Pathway: Glycan biosynth... |
P12298 | GVLILSGDHLYRMDYMDFVQSHRQRDAGISICCLPIDGSRASDFGLMKIDDTGRVISFSEKPRGADLKEMEEAEKKPYIASMGVYIFKKEILLNLLRWRFPTANDFGSEIIPAAAREINVKAYLFNDYWEDIGTIKSFFEANLALAEQPSKFSFYDASKPMYTSRRNLPPSMISGSKITDSIISHGCFLDKCRVEHSVVGIRSRIGSNVHLKDTVMLGADFYETDMERGDQLAEGKVPIGIGENTSIQNCIIDKNARIGKNVTIANAEGVQEADRASEGFHIRSGITVVLKNSVIADGLVI | Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Mass (Da): 33430
Sequence Length: 301
Pathway: Glycan biosyn... |
P55230 | MESCFPAMKLNQCTFGLNNEIVSERVSAFWGTQVVKPNHLRTTKLRSAPQKKIQTNLIRSVLTPFVDQESHEPLLRTQNADPKNVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNGVNFGDGFVEVLAATQTSGDAGKKWFQGTADAVRQFIWVFEDAKTKNVEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPMDESRASDFGLLKIDQSGKIIQFSEKPKGDDLKAMQVDTSILGLPPKEAAESPYIASMGVYVFRKEVLLKLLRSSYPTS... | Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Mass (Da): 57470
Sequence Length: 518
Pathway: Glycan biosyn... |
P55239 | KYPYIAGMGVYIFKKEILLNLLRWRFPTANDFGSEIIPAAAREINVKAYLFNDYWEDIGTIKSFFEANLALAEQPSKFSFYDASKPMYTSRRNLPPSMISGSKITDSIISHGCFLDKCRVEHSVVGIRSRIGSNVHLKDTVMLGADFYETDAERGDQLAEGKVPIGIGENTSIQNCIIDMN | Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Mass (Da): 20329
Sequence Length: 181
Pathway: Glycan biosyn... |
Q7G065 | MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHHTYLGGGINFTDGSVQVLAATQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHL... | Function: Involved in synthesis of starch. Catalyzes the synthesis of ADP-glucose, a molecule that serves as an activated glycosyl donor for alpha-1,4-glucan synthesis. Essential for starch synthesis in seed endosperm . Is essential for both catalytic and allosteric regulatory properties of the cytosolic heterotetramer... |
P12299 | MSSMQFSSVLPLEGKACISPVRREGSASERLKVGDSSSIRHERASRRMCNGGRGPAATGAQCVLTSDASPADTLVLRTSFRRNYADPNEVAAVILGGGTGTQLFPLTSTRATPAVPIGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHRTYLGGGINFTDGSVEVLAATQMPGEAAGWFRGTADAVRKFIWVLEDYYKNKSIEHILILSGDQLYRMDYMELVQKHVDDNADITLSCAPVGESRASEYGLVKFDSSGRVVQFSEKPKGDDLEAMKVDTSFLNFAIDDPAKYPYIASMGVYVFKRDVLLNLLKSR... | Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Mass (Da): 57809
Sequence Length: 522
Pathway: Glycan biosyn... |
P12300 | RASPPSESRAPLRAPQRSATRQHQARQGPRRMCNGGRGPPYWTAGVTSAPARQTPLFSGRPSGGLSDPNEVAAVILGGGTGTQLFPLTSTRATPAVPIGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHRTYLGGGINFTDGSVEVLAATQMPGEAAGWFRGTADAWRKIIWVLEDYYKNKSIEHILILSGDQLYRMDYMELVQKHVDDNADITLSCAPVGESRASEYGLVKFDSSGRVVQFSEQPKGDDLEAMKVDTSFLNFAIDDPAKYPYIASMGVYVFKRDVLLNLLKSRYAELHDFGSEILPRALHDH... | Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Mass (Da): 55560
Sequence Length: 500
Pathway: Glycan biosyn... |
Q0D7I3 | MATCSWAATTAAAAPPRPPARCRSRVAALRRTAAASAAAASCVLAEAPKGLKVEQADAVEPAAAAAARRDVGPDTVASIILGGGAGTRLFPLTRTRAKPAVPVGGCYRLIDIPMSNCINSKINKIYVLTQFNSQSLNRHIARTYNIGEGVGFGDGFVEVLAATQTTGESGKRWFQGTADAVRQFLWLFEDARLKRIENILILSGDHLYRMDYMDFVQKHVDKGADISVACVPVDESRASDFGLMKTDKNGRITDFLEKPKDESLKSMQLDMGTFGLRPEVADTCKYMASMGIYVFRTDILLRLLRGHYPTANDFGSEVIP... | Function: Involved in synthesis of starch. Catalyzes the synthesis of ADP-glucose, a molecule that serves as an activated glycosyl donor for alpha-1,4-glucan synthesis. Essential for starch synthesis in leaf chloroplasts.
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
S... |
A0R2E2 | MRVAMMTREYPPEVYGGAGVHVTELVAQLRKLCDVDVHCMGAPRDGAYVAHPDPTLRGANAALTMLSADLNMVNNAEAATVVHSHTWYTGLAGHLASLLYGVPHVLTAHSLEPLRPWKAEQLGGGYQVSSWVERTAVEAADAVIAVSSGMRDDVLRTYPALDPDRVHVVRNGIDTTVWYPAEPGPDESVLAELGVDLNRPIVAFVGRITRQKGVAHLVAAAHRFAPDVQLVLCAGAPDTPQIAEEVSSAVQQLAQARTGVFWVREMLPTHKIREILSAATVFVCPSVYEPLGIVNLEAMACATAVVASDVGGIPEVVADG... | Function: Involved in the biosynthesis of the maltose-1-phosphate (M1P) building block required for alpha-glucan production by the key enzyme GlgE. Catalyzes the formation of an alpha-1,4 linkage between glucose from ADP-glucose and glucose 1-phosphate (G1P) to yield maltose-1-phosphate (M1P).
Catalytic Activity: ADP-a... |
P35409 | MEDRGICPRVLQVLFLVVLILISPVYAAKNDACTKCSCNPKGMVSCFELQEFPPLATFPRNTTTLHVSFSGEISIPSDILQHLEKLKYLTLNNNKIKNIAKFRVKNGYSSLITLSYTHNIIETIENGAFDDLQQLTQLDLSNNRLKEFPIFNKTSSVTKLYLRGNPGITKLPRQSLGNLPSLENLFMERTGIQEIPAGIFRQNTRLINLYFNKTKALERINEDAFDEDSSLKTLVLDETSVTSLPSRGLKNLHFLSLKDVPNFWQLPELDSIREVYLSPYNGFLCCEFESGEKYGKDCTMQKPSTEENNGQTTASSPTKE... | Function: Probable receptor for a glycoprotein hormone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100060
Sequence Length: 925
Subcellular Location: Cell membrane
|
A0JZ25 | MSRLFGTDGVRGLANGLLTAELAMQLAQAAAVVLGHERSTNGARPRAVVARDPRASGEFISAAVSAGLSSSGIDVYDAGVLPTPAAAYLVADLHADFGVMISASHNPAPDNGIKFFAKGGQKLPDEVEDAIEAQMAKDPVRPTGSDVGRIQTFSDAEDRYIVHLLGTLPHRLDGLKVVLDCAHGAASGCSPQLFNDAGAEIVVIGAEPDGLNINDGVGSTHLGALQRAVVEHGADLGIAHDGDADRCLAIDHEGNEVDGDQIMAILALALKESGKLKDNVLVATVMSNLGLKIALRNAGISIRETAVGDRYVLEEMRDGG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 46803
Sequence Length: 452
EC: 5.4.2.10
|
B0TWU1 | MAKYFGTDGIRGEVGKSVIKAEFMQKLGNAVGTLINDNGYPGFVIIGQDTRSSGKFLKFALVSGLNAAGIDVIDLGVVPTPIVAFMTVKYKAAAGFVITASHNKFTDNGVKLFSSSGFKLDDALEEEVEAKIDSDFIYQTECKFGNYKVAENFIDEYIENLFERFGSLVNYKGKVVIDCANGAASNHFEALLDRFCIDYISVASNPDGLNINVDCGATCTSNIKKAVIEHNADLGISLDGDADRIIIVDENAQEIDGDGILNIIAQYSNICGGTTGIVGTQMTNMSYENHYKSNNIPFIRSKVGDRYVLEDLVKHGYKIG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 47951
Sequence Length: 443
EC: 5.4.2.10
|
Q8R6A7 | MGRYFGTDGIRGEANRELTVDKALRLGYALGYYLKNNNPNEEKIKVIMGSDTRISGYMLRSALTAGLTSMGIYIDFVGVIPTPGVAYITKQKKAKAGIMISASHNPAKDNGIKIFNLEGYKLSDEIENQIEDYMDNLDKILANPLAGDKVGKFKYAEDEYFQYKNYLTQCVKGNFKDIKIVLDTANGAAYRAAKDVFLDLRAELVVINDAPNGRNINVKCGSTHPDILSKVVVGYEADLGLAYDGDADRLIAVDKFGNVIDGDKIIGILALGMKNKGTLKNNKVVTTVMSNIGFEKYLKENSIELLRANVGDRYVLEKML... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 50068
Sequence Length: 452
EC: 5.4.2.10
|
Q74C70 | MKKLFGTDGVRGVANVYPMTTEMAMQIGRAAAYLFKDGNRRHRIVIGKDTRLSGYMLENALVAGICSMGVDVLVVGPLPTPGIANITSSMRADAGVVISASHNPFQDNGIKFFSRDGFKLPDEMELKIEDLIFSGKIDSLRPVATEVGKAYRIDDAVGRYVVFLKNSFPKDLDLAGMKIVLDCANGAAYKVAPAVLEELGAEVIPYGVKPNGTNINAGCGSLYPQVISEAVKEHRADLGIALDGDADRVIFVDEFGNEVDGDHIMAICATQMLKQKKLRKNTLVATVMSNMGLDIAVKRAGGKVVKTAVGDRYVVEEMIK... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 48786
Sequence Length: 451
EC: 5.4.2.10
|
Q8EHM0 | MSERKFFGTDGIRGKVGSGQMTPELALKLGWAAGRVLSRSGTKKVIIGKDTRISGYMFESALEAGLSAAGLNVMLMGPMPTPAVAYLTRTFRAEAGVVISASHNPYYDNGIKFFSTDGSKLDDNLELEIEAELEKPLVCVESHLLGKVSRIEDARGRYIEYCKGNFPADQTLTGLKIVVDCAHGATYHIAPAVFRELGAEVIAIGDKPNGVNINDKVGATSMAKICETVLAETADLGIALDGDGDRIMMVNSKGEVIDGDQILYILACDAKARGVLRGGVVGTLMSNLGLDLALQALDIPFARSKVGDRYVMELLKELDW... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
PTM: Activated by phosphorylation.
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Mass (Da): 47584
Sequence Length: 445
EC: 5.4.2.10
|
O84823 | MCGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAVSSDIHSQAAIGHTRWATHGEPSRFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETRDLIQSFSWTLKRLQGSFACALMHQDHPEVLLCAAHESPLILGLGEDEVFISSDIHAFLKYSGCTQTLASGELAVLRIGKSIETYNFELARIQKEVRCIDHTEDSLDKKGFDYYMLKELYEQPEVFERILHLTCEENGFTESFLKGFSLDEIQSLHIVACGSSYHAGYLAKYVIESIASIP... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 67400
Sequence Length: 606
Subcellular Location: Cytoplasm
... |
Q97MN6 | MCGIVGYSGKKEASSILVEGLSKLEYRGYDSAGVAILNDGKINVSKCKGRLVNLENKLEENPIAGNIGIGHTRWATHGEPSDLNAHPHSNKDNTISVVHNGIIENYMQLRTWLKSKGYEFKSETDTEVIPNLVDYFYEGNLLDAVIKAISKVEGSYALGIVSSKEPDKVVAVRKDSPLIVGISEDGNFIASDVPAILNHTRDIYYIKDKEFVVLTSEGVEFYSNEGEKIEKELNHIEWDANAAEKGGYEHFMLKEIYEQPKAIRDTMTSRIIAGQPIKLDDISITKEQIENIDKIYIVACGTAYHAGVVGKYVIEKFARI... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 66949
Sequence Length: 608
Subcellular Location: Cytoplasm
... |
Q8XHZ7 | MCGIVGYVGQKKATDILVEGLSKLEYRGYDSAGVAVLEDNKIKAEKHKGRLANLEGMLNENPIEGGIGIGHTRWATHGEPSDVNSHPHLNNKETIAVVHNGIIENYNELRNWLMEKGYEFKSETDTEVIPNLVDFYYKGDLLDAVMEATKHMEGSYAIGVICNDEPEKLVAVRKDSPLIVGLGEKEYFIASDIPAVLNHTREVYLLEDKEFVVLTNDGVTLFDEEKNPVEKEVYHITWNVDAAEKGGYEDFMLKEINEQPKAIKDTMTSRIMEEKEVTLDDISITKEYLDNVDRVYIVACGTAYHAGVIGKYAIEKLVRI... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 67804
Sequence Length: 610
Subcellular Location: Cytoplasm
... |
Q8NND3 | MCGIVGYIGQAGDSRDYFALDVVVEGLRRLEYRGYDSAGIAIHANGEISYRKKAGKVAALDAEIAKAPLPDSILGIGHTRWATHGGPTDVNAHPHVVSNGKLAVVHNGIIENFAELRSELSAKGYNFVSDTDTEVAASLLAEIYNTQANGDLTLAMQLTGQRLEGAFTLLAIHADHDDRIVAARRNSPLVIGVGEGENFLGSDVSGFIDYTRKAVELANDQVVTITADDYAITNFDGSEAVGKPFDVEWDAAAAEKGGFGSFMEKEIHDQPAAVRDTLMGRLDEDGKLVLDELRIDEAILRSVDKIVIVACGTAAYAGQV... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 67215
Sequence Length: 623
Subcellular Location: Cytoplasm
... |
O19908 | MCGIIGYVGEGSCRDVLINGLDKLSYRGYDSAGIAFIKNSKINVVRSKGRIEKLKEKINDNFQKFEIGNIGIGHTRWATHGEPTEINAHPHLDAEGQFAVVQNGVIENYVQLKNYLTVNGTYFLSDTDAEVIPHLIAYKQKHLKLQIVEAILCALSELKGNFSTVIIARDMPDSIFVYQNKTALTLGKGSNFYSVSSDPIALIPYTKNFIQLHDRELGIISISQLAIYNKGKFTYPSRRFKANLNDLITNKASFDSYTLKEIHDQKKVLRNLIISTLQSEKSIDESGQLHLEYKKIKNFQIIACGSSFNAALVGKVILEK... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 69302
Sequence Length: 621
Subcellular Location: Plastid
EC... |
P17169 | MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESLAG... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 66894
Sequence Length: 609
Subcellular Location: Cytoplasm
... |
Q5NHQ9 | MCGIVGANSTRNVTNILIEGLKKLEYRGYDSAGLAIIDDKNNIDICKEVGKVIELEKSVHNLANFKGDIGIAHTRWATHGKPSKNNSHPHASESFCIVHNGVIENFAELKKVLINDGYKFKSDTDTEVIAHLLQKEWRDNFSIVDNIKYIMAMLKGAYAVAIISQKFSDKIVAVRSGSPLVIGVGIDENFISSDALSLLPVTNKFSYLDEGDIAIISKDNVEVFDNNGAAKNLEVEEYNYSSSSASKDGYKHYMLKEIYEQPEAVSNTILASLADGEISLDSFDKRAKELFEKTKHICIVACGTSYNAGMTAKYWIEKYA... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 67444
Sequence Length: 612
Subcellular Location: Cytoplasm
... |
Q8RG65 | MCGIIGYSGSKANAVEVLLEGLEKVEYRGYDSAGIAFVTDSGIQIEKKEGKLENLKNHMKNFEVLSCTGIGHTRWATHGIPTDRNAHPHYSESKDVALIHNGIIENYVEIKKELLEQGVKFSSDTDTEVVAQLFSKLYDGDLYSTLKKVLKRIRGTYAFAIIHKDFPDKMICCRNHSPLIVGLGEHQNFIASDVSAILKYTRDIIYLEDGDVVLVTKDNVTVYDKDEKEVKREVKKVEWNFEQASKGGYAHFMIKEIEEQPEIIEKTLNVYTDKEKNVKFDEQLEGINFHDIDRIYIVACGTAYYAGLQGQYFMKKLLGI... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 67899
Sequence Length: 607
Subcellular Location: Cytoplasm
... |
Q5L3P0 | MCGIVGYIGYQDVKEILLRGLEKLEYRGYDSAGIAVLNESGVHVFKEKGRIADLRRIVDPNVNATVGIGHTRWATHGAPSRVNAHPHQSASGRFTLVHNGVIENYEMVKRDYLADVAFQSDTDTEVIVQLVEKFVRDGLTTEEAFRKTLSLLKGSYAIAMIDAQDENTIYAAKNKSPLLVGLGDGFNVVASDAMAMLQVTNQFVELMDGELVIVTSENVTIQTLNGETVKRKPFTAELDASDIEKGTYPHYMLKEIDEQPFVIRRIIQKYQDDNGELAIDKAIINEVLNADRLYIVACGTSYHAGLVGKQLIESWAKIPV... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 65643
Sequence Length: 600
Subcellular Location: Cytoplasm
... |
Q74GH6 | MCGIVGYIGAQEATPIILDGLKRLEYRGYDSAGICTLLEGKADKRRSEGKLINLERLIQSTPLAGRIGIGHTRWATHGPPSERNAHPHQAGSIIVVHNGIIENYLELKQRLVTSGRVFNSDTDTEVIAHLIDDKFAGTGDFERAVREALAEVRGAYALCILCEREPGVLIAAKQGSPMVVGLGEGEFFVASDIPAILSHTREMVFMEDGEIVVFRDGHPTFSTVAGAPLDKKSRHIDWSPLMAEKGGYKHFMLKEIFEQPRAVQDTITGRLLEEQGDVRLEEMKLADEQLRGIGRICIVACGTSWHSALVGKFLMEEHCR... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 66459
Sequence Length: 609
Subcellular Location: Cytoplasm
... |
Q7NIG8 | MCGIVGYIGGRTALPFLVDGLKRLEYRGYDSAGIATVGESGLELVRAKGKLHNLEEKLNGVAQSTGTVGIGHTRWATHGKPEEHNAHPHTDASGRLAVIQNGIIENYAELRLGLKERGCLFKSETDTEVIPHLIACRLAGHSLLEAVLAAVVELKGAFAIAVVSADFPDELIVVRQQAPLVIGFGEGENYFASDVPAIVSHTTRVLTLQDGECARLTRDEVQIHDFSGARLRRTPRSLNWNPSLVEKRGFRHFMLKEIHEQPGVIRDTLEDRIGDATGPIRLGLSSDLFADLERIYIIACGTSWHASLVGKYLIEELAGI... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 66042
Sequence Length: 609
Subcellular Location: Cytoplasm
... |
P44708 | MCGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINKQNELQRIRCLGKVKALDEAVSEKPLIGGTGIAHTRWATHGEPSETNAHPHSSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRTTDSLLDAVKKAVKQLTGAYGMVVMDSRHPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRTVDIYDTHGNKAKREIHESNLENDAAEKGKFRHFMQKEIYEQPTALINTMEGRINHENVIVDSIGNGAKGILEKVEHIQIVACGTSYNAGMVARYWFESLAG... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 66832
Sequence Length: 610
Subcellular Location: Cytoplasm
... |
Q3AFM0 | MEGIILAAGKGTRMKSDLPKVVHEVAEKPMVLRVYEALVGAGVKRVVAVVGYRKEKVEEILRGRAVIAVQEEQLGTGHAALVAMPYVEDENVIIVPGDTPLLKASTLQALIKKHLETGAYATVLTCFLSNPYGYGRIVRDGYGKIIKIVEEKDATLEEKQIAEVNTGIYCFNTKILKEILPLLKAENAQKEYYLTDVIPLLLERGKVVETITIQDETEVYGVNDRVQLARLTKGVYRRKAEALMQEGVTIIDPETVYIGEEVVVGSDTVIYPNTYLEGKTVIGSGCRLGPNTRITDSVIGNNTEITFSVIIQARVGDEVN... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q3J3H0 | MDRATVSLIVLAAGQGTRMNSDLPKVLHPLGAAPMLHHALRAGQSLEPERVVVVAGHGAEAVAKAARAFDESIEVVVQAEQLGTAHAVAQAAPLLADAPGEAVVLYGDTPFIRPETLERMLDLRSRHAVVVLGFEATDPGRYGRLVTRGEELDRIVEWKDATDEERTISLCNSGVICAEAGLLLALVSEVGNANAAGEYYLTDVVALARVRGLSAGVAICDEAETLGVNTRAQLAEAEAEFQKRARAAALEDGVTLTAPDTVFFALDTFLGRDAIVGPNVVFGPGVTVESGAEIRAFCHLEGCHISRGATVGPFARLRPG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q1QSD2 | MTLDVVILAAGQGTRMRSAKPKVLHALAGKPLVSHVLDTAEQLGATRTHVVIGHGAEQVETELDGRDVRFALQAEQKGTGHAVAQTLDELGDGKVLILYGDVPLIRAETLTALLDEVDERRLGLLTVTLDDPGGYGRIVRDAEGRVTRIVEHKDASEAERGITECNTGIVAATGTQLKRWLPQLSAENAQGEYYLTDIFAMAAAEGIEVATASPASALEVEGVNNRSQMAALERAYQRDRAERLLTEGVALADPARFDVRGRLQCGHDVFIDVGCVFEGDVTLGDGVSVGPYTLIRDSHVAAGTVIEAHSIIEGAEVAEQ... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q8RHM3 | MKSIIMAAGKGTRMKSDLPKVVHLAHGKPMIVRIIDALNTLDVEENILILGHKREKVLEVLGNDVSYVVQEEQLGTGHAVKQAIPKIKDYDGDVLIINGDIPLIRKQTLIDFYNLYKNENADGIILSAIFENPFSYGRVIKDGNKVLRIVEEKEANEEQKKVKEINAGVYIFKAQALVKALEKINNNNEKGEYYITDVIEILSNDKKVISYSLEDSMEIQGVNSKVELALVSKVLRERKNTALMEDGVILIDPATTYIDDEVKIGRDTTIYPNVTLQGNTEIGENSEILSGTRIIDSKIYDNVRIESSVIEESIVENGVT... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q74GH5 | MDNLAAIILAAGKGTRMKSGIVKVMHPLAGAPMVAWPVAVARQAGAGRIVAVVGHQAERLREHFSNDADITLAVQEEQLGTGHAVACAAGDLSGFSGKVLILCGDVPLIRTETLRAMVTAHEATGAVLTVLTARQENPHGYGRIIRGFDGRVIRIVEEKDATPDERSRTEVNAGIYCAEASFLFDAVKRIGNDNAQGEYYLTDIITMANDRGLRCTAHPVADPVEVMGINDRVQLAEAARHARRRIAEEHMLNGVTLVDPAATYIDQGVVIGADTTIQPGVQIAGGCRVGEGCTIEAGAIIKGSELGDRCVVESRAVIRG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q5FUY6 | MTDSTHRTTAIILAAGLGTRMKSRLPKALHRLGNQPMINHLITTARQVFDDVVVVTGPDMPELEKAVRPFKTVTQVERLGTAHAANTARDLFGTGDVAILYADNPLITAETMRRLLAARREGASLALLGMRPAEPGRYGRIVEDHGRVVKIVEFKDATEDERRITLCNAGVMCAGVDDFRTWLANVGNDNAQGEYYLTDVVEMAAKAGPVVCVEAPEAELAGVNSRSELARAEATLQTRLRNAAMDAGVTLVAPETVFFSTDTVIEADVTIEPNVFFGPGVKVRSGALIRAFSHLEGCEVGENAMIGPYARLRPGTLCAA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q92PS3 | MERTCLAIILAAGESTRMKSAMSKVLHPVAGRPMIAHVVDALASASISDVALVVGRDADAVSAAAATDEVAVTSFLQKERLGTAHAVLAAREAIAKGYDDVLVVFGDTPLITAAPLKAARDGLAAGNDVVVIGFQATDPTGYGRLIVKDGALVAIREHRDASDEERRITYCNGGLMAIDGRKALDLLNRIGNANAKGEYYLTDLVEIARSLDGRAIAVEAPEEELTGCNTRAELAYIERLWQQRRRHELMLAGVSMIAPETVFLSWDTALAQDVLLEPNVVFGPGVRVESGAVIHAFSHLEGAHVRAGATVGPFARLRPG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q0S4N3 | MPVQTAVVVLAAGAGTRMRSKTPKVLHTLGGRTMLAHSLYAAAEVDPTHLVTVVGHDKERVGVAVSALEAELGRPIAIAVQDEQNGTGHAVECGLSALPADFRGTVLVTAADVPLLDGRTLHALVDEHHSEPTPSAVTVLTFTAPEPRGYGRIVRLPHDGEIAEIVEEADATEEQAAITEVNAGVYAFDAEFLRSALGQLNANNAQGELYLTDVVKIAREAGAPVFAAHLADSAKVAGANDRVQLSRLAAELNRRTVENWMRAGVTVVDPSTTWIDVGVTLARDVTIHPGVQLLGTTAVGEDAVIGPDTTLTDVTVGEGA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
A7INP6 | MSDRSLLVVVLAAGEGTRMASRLPKVLHKVAGRTMLHHVLAATRAAGATRTAVVVGPGREDVAAEVRKIVPDAEVFEQTERLGTAHAVLAARAALENGADDVLVLYADTPLVRPETLGLLRAPLKAGAAVAALGFEPADPTGYGRLVTAGDELVAIREEKDASAAEKAIRFCNAGLMALAGAHALSILERIGNANAKGEYYLTDAVEIARADGLSAVAARADADEVAGVNSRVQLAEAEAILQRRLRLAAMAGGATLVAPETVFLSADTVLGRDVIVEPHVVFGPGVSVGDDVVIHSFCHLEGARLESGVTIGPYARLRP... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylgluco... |
Q56WN1 | MSLVSDLINLNLSDSTDKIIAEYIWVGGSGMDMRSKARTLPGPVTDPSQLPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRRGNNILVMCDAYTPAGEPIPTNKRHAAAKVFSNPDVAAEVPWYGIEQEYTLLQKDVKWPVGWPIGGYPGPQGPYYCGIGADKSFGRDVVDSHYKACLYAGINISGINGEVMPGQWEFQVGPAVGISAADEIWVARYILERITEIAGVVVSFDPKPIPGDWNGAGAHCNYSTKSMREEGGYEIIKKAIDKLGLRHKEHIAAYGEGNERRLTGHHETADINTFLWGVANRGASIRVGRD... | Function: High-affinity glutamine synthetase which catalyzes the synthesis of glutamine from ammonium and glutamate . May contribute to the homeostatic control of glutamine synthesis in roots.
PTM: Phosphorylated by CRK3.
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Mas... |
Q470D5 | MPTNLPALPMDTTPELLLAARVRDQLKADKQALFADFDLSSHVGTLVTRLRRAVDAALAEAWRGLDMPADAALVAVGGYGRGELFPYSDVDVLLLLRAEPDADTVSRLERFIGMCWDLGLEIGSSVRTVEDCIREARADITIQTSLLEARLLTGNRKLFEALRTQHQADLDPAAFFQAKLLEMRQRHAKYQDTPYALEPNCKESPGGLRDLQVILWMTKAAGLGDSWKELFERGLLTQREAQELSRNERLLKTIRARLHLVAGRRQDVLVFDLQTALAESFGYRQNANKRASEQLMRRYFWAAKAVTQLNSVLLLNIEAL... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
Q04RQ6 | MEVFRIYTNSPLRNFTYILRNSETSETLSIDPYDSEQIEKFLDSKGWTLDFLLNTHEHEDHTSGNTGLVQRYGCTVYSHPEGIGKIPHATHPLKKGDFLLRSSKEYLEILDTPGHTFCHVCLLLVENQKPKAIFTGDTIFNAGVGNCHHGGDPEVLAKTILEQFYPLEEEILLYPGHDYLETNLKFTLSLDPSNQDAIRTLEECSRLSKNVEFLTTDLRKERKINTFFQCDKPSLELRKNVSKKIPFKQLLDNDPTSFFISLRSLRDQW | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 31016
Sequence Length: 269
Pathw... |
A6VVZ9 | MTIFPLPAFNDNYIWIIQDKDSSGIWAVDPGKADVVLNFCHEYQKTLTGILITHHHKDHTGGVAELKQHSNCPVYGPEHLTELVTHPVDDGDRILVFSKVFTVIATPGHTLDHLCYFSEQETPILLSGDTLFKGGCGRIMEGTHEQMLAAMIKISGLPNDTLIYGTHEYTLANYRFALSLEPNNKDLIESNITCQKLRTEEKPTLPTKLSIEKKTNPFLRSHIEALKIQAAQQLNEIPAENPIGAFSQVRRAKDSFS | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28763
Sequence Length: 257
Pathw... |
A1U0V1 | MRIHPVPAFSDNYIWCLTNLESGKTLIVDPGQAKPVLDYLSDSGFSADTILITHHHPDHTGGVKELQQQYPDLRIVGPTDSPFKGATNTVHAGDEVVWEGITFNVLAVPGHTLDHIAYYSDTQVNDKPVLFCGDTLFVCGCGRLFEGTPEQMHTSLQTLRDLPDNTAVYCAHEYTLANLRFARHWLPEDKALAEFENACKDLRERGKPTVPTTIGQEKQLNPFLRWDDAMVIEAAENYSTTHRLATGSDCAVFAAVRHGKDNF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 29267
Sequence Length: 263
Pathw... |
Q60BX0 | MLEILQIPVLEDNYVYLLHEPGSGATAAVDPAVAGPVLEALDARGWRLGHVLNTHHHGDHVGGNLELKAATGCTVVGAAGDRHRIPGIDVALKDGEEFRLGSASARMLDVPGHTSGHVAFWFEDDAALFCGDTLFALGCGRLFEGSAEQMWRSLERLRALPAETKVFCAHEYTQANARFAVTIEPGNAALRERVERVEALRREGAATVPSILSEELATNPFLRPESPEIRARLGLPGVPEVEVFAEIRRRKDVFRG | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 27829
Sequence Length: 256
Pathw... |
Q1H188 | MFEIIPILAFEDNYIWLLHQHGHALVVDPGDAHPVLEILDARGLQLRAILVTHHHQDHTGGVEELIQATSAQVFAPAKEQFSFPHHPVTAGDRLDIPGIALSLSVLDVPGHTVGHVAYYGDGMLFSGDTLFGAGCGRLFEGTPGQMYSSLQQLAQLPVNTRVYCGHEYTERNLAFALSLEPHHEALLSRREATAALRAQGLPSLPSSMALELATNPFLRCHEPGIIAASKSAATDPVSVFAAIREMRNHF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 27188
Sequence Length: 250
Pathw... |
B8ICA2 | MPEIRTFLCRSDNIGVLLHDPVTSACAAIDVPEAGAVLRALKETGWRLTDILVTHRHFDHVEGIPEVKARTGARVTAPAKAGDAVPEVDATVREGDVVKVGSLVGTVWETPGHCADHVTYWFERERLAFAGDTLFTLGCGRVMESPPEVLWRSLSRFLALPDETAIYSGHDYVLSNARFALAADPDNSNLKARAELAERVKRDGRFLIPTTLGEEKATNPFLRAGEPALARSVDMAPGSDPAAVFAALREWKNRF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 27842
Sequence Length: 255
Pathw... |
Q5F7J0 | MKITPVKALTDNYIWMIQHGNHAVCVDPSEPSPVLEFLVRNRLMLAQTWVTHPHPDHEGGAAALWRGYMESPVYGESDIEAATHTVTAGTRFTFGNGQVTVWATPGHTDRHTSYLLETSDGIHVFCGDTLFSAGCGRVFTGTVEQLYDNFQRFNQLPEGTLFYPAHEYTAANLRFAAHIEPDNADIQTALKAAEHTPTLPVTLAHERRVNPFLRTEIPAVRQRAEALVGKTLNSGLEVFAALRELKNAYR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 27810
Sequence Length: 250
Pathw... |
S3DB78 | MVFTSPSWCQDILMPIPNNELVGEFVMRRGHGLNDVSEDSPSSVCAYTGKSYSIRDIRHNVKSLSKSLSQILGWDFNHGNPEDKVVAVCSLNSIDYVPLTWAIHRLGGICLLLHPTSSASELETLMRKANCKAVFTCKPLMAQCQAAFTAINGDPSNIFLVELPLPEEQPVKISNTTISQLIADGEGLPDLQPLDLQDFDSKERLAYFCPTSGTSGFLKIAKVSHANVMANILQCTTMDSYTTASQTDVTLGILPLSHAYGLLVQHFVTFRGDCIILHPKFDMQIALKSVQQYRIVRLYLVPTIIGALATNPILFKLFDL... | Function: Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyk... |
S3E7Q2 | MDYIKQAESTQLSSLSLSRLEGNNAEESKRLLEACAQDGFFYLDLRDHKQLLVDYEALLEIIKQYFNEPLDQKMKDDRKSDTIGYEPVATSAGVLDGLPDYYESFKVSWNQLRDHVQELPTVVETNIEVFDRFAKYVHSILLMILSRLSQTMGRNNDNRFESYHRDSIATRTNLTFLKYPKQDTTEHGVGHNKHTDVGTLTFLLSGQRGLQRLTPEGWCHVEPRSGFAVVNVGDSLRFLSDCVLSSVIHRVLPVGAHQTEDRYTLAYFLRPEDDAVFKDINGNLVSARSWHDRKFDHFRASHNQQKNDTILMGGMEENQK... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-di... |
S3D784 | MAIQTLDYRDFQYGGQEQHRTFCHNLCETLSTWGFIKIQNTSIPDAVIDELFSYNKKFFALPEHIKQKARHPAAPNPHRGWSAVGQEQLSRIAGFEKDEETDGFVPEYRESFDQGAADDELFPNRWIDEDDLPGFRKFMENYYEMCYNFHTQLLRAISTGLSLPEDLLLSRHQTDTSELRMNHYPAIACENLKFGMRIGEHSDFGTLTLLLQDSTGGLQVEDQKKLGTFIPVESDSRYEVIVNVGDCLQRWTNRRLRSANHRVHLPEGKNFKSDEVLADRYSVAYFGKPDRNVLVDSFPEFCRGGESKYNDHMNALEYNQ... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-di... |
S3DQP8 | MTENFPLPPLLGVDWDHLGFEPLEVNGHVECTFSTTTSCWTEPVFVTNPYLPVHGLAPGLNYGQQIFEGMKAFRNPSGDVQLFRPDQNALRFARSALRVAIPPVPTDLFLRAVNTAVGMNTDFVPPHGTGASLYIRPMAFASSPTVGLFLASQFKFCVYVLPVSPLHGKATQEGASVLVIEDFDRAAPLGTGNVKVGGNYGPVLGLIDEAKKQGFNLTLHLDSLSHSLIDEFSTSGFIGVLNDGEVPTIVVSDSQQVVSSITVDSICELARAFDWHVQKRPISFLEVARFSEVYAAGTAAVLVPVESILRRSTGEHVVYS... | Function: Branched-chain amino acid aminotransferase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthe... |
S3E7P8 | MPKPTISYSLNGLPAAAVDSIGSLLEILARIRGIVLTEQSNDETASIIISAPDVHRLVVGSDDSHYDSTTLYIEDFLNRLCEALDAVGKKAEAGAFRHALQLYHTDRELGALKHGESVTNRQLKNDSFEDLEFLVEAWLVALNSEESARKLPAPLPVKSPDTRAMTLAEKILAHHAFSLPSSGGLKSGELGMKHGMVSIGELPSVWRNDRFWLAGDHTVEPRTYDQPRVRELLNGLNDAKQEFKMTENQGSNYTILHTEFVRERAEPGMLALGSDSHTCSAGAVSCLAIGLGAADVMTALATGETWIKVPESIRIDFTGE... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: 3-isopropylmalate dehydratase large subunit; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase .... |
Q7VNZ0 | MAAIFTEISPTTAWQLVKHENAFLADIRALAHYLDDHPSGAFHLTNDSYAEFLDLVSDEQAVIVVCYHGISSRSVAQFLVEQGFETVYSVTGGFEAWQKLALPVTKGCDQ | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 12151
Sequence Length: 110
Subcellular Location: Cytoplasm
EC: 2.8.1.1
|
C4ZGB4 | MAKYIMALDAGTTSNRCILFNEKGEMCSVAQKEFTQFFPKPGWVEHDAEEIWATQLEVAKEAMANIQATAADICAIGITNQRETTIVWDKNTGEPVYHAIVWQCRRTAEYADSLKEKGLTETFRKKTGLVIDAYFSATKLKWLLDNVPGARERAERGELLFGTVETWLIWKLTQGQVHVTDYSNASRTMMFNINTLKWDDEILKELDIPKSMLPKPMPSSCVYGEVNPVYFGGPIPIAGAAGDQQAALFGQTCFRAGEAKNTYGTGCFLLMNTGEMPVSSKNGLVTTIAWGIDGKVVYALEGSIFVAGASIQWLRDEMKF... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 55214
Sequence Length: 498
Pathway: Polyol metabolism; glycerol degradation ... |
Q0VRN6 | MPYILSIDQGTTSSRAIVFDANGHACGQAQKEFRQYFPEDGWVEHDAMEIWNDTLAMCQQALRNARVEAQQLVAIGITNQRETTVLWDRETGDPLARAIVWQDRRTASTCEALRDQGHENQVRSKTGLLLDPYFSATKLAWLLDNVPNARQRAEAGELAFGTIDSWLLWQLTRGKVHATDATNASRTLLFNIHEQCWDEELLTLFNVPASVLPDVRDSAADFGTTCPELLGAAVPVTGIAGDQQAALVGQACFAPGMVKSTYGTGCFMVMNTGEAVESHNRLLTTVGYRLNGKTTYALEGSIFVAGAAIQWLRDGLHLIR... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 54056
Sequence Length: 497
Pathway: Polyol metabolism; glycerol degradation ... |
Q8EVD0 | MDNTKKYIVSLDSGTTSCRTIIFDQNGNMVSSAQTEFTQYFPQSGWVEHDAIEIWTTQLGTLQSAKSRANIKSHNMAAIGITNQRETVVLWDKETGLPVYNAIVWQDRRTSEYCDELIKQGKANIISSKTGLIINPYFSGTKIRWILKNVPEAAQKLQEHKLLAGTIDTWLIWKLTDGKVHATDVTNASRTMLYNINTLEWDQEILDLLEIPREILPVVKSSSELYGTINPKYLSQRATAAVPIMGVAGDQQSSLFGQLCTEPGMVKNTYGTGCFTLINTGERAIFSKNKLVTTIAWKLGNQKPIYALEGSVFIAGSGIK... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 56414
Sequence Length: 507
Pathway: Polyol metabolism; glycerol degradation ... |
B1ZGW7 | MPDAVGAIDQGTTSTRFIVFDRRGTIRAQAQREHEQIFPRPGWVEHDPREIWRNTHAVMREGLARAGLVPGDLAAIGLTNQRETALLWDRRTGEPLHNALVWQDTRTDRTVAALARDGGRDRFRAVTGLPLASYFSASKLAWLLDHVEGARAKAEDGTALFGTIDSWLVWNLTGGPDGGLHVTDVTNASRTQLMSLATLDWDEAMLGVFRIPRAVLPEIVSSSAVLGETRDPFPGVPVGGILGDQQAALFGQTCFAPGEAKNTYGTGCFALMNTGPEPVASTAGLVTTVAYRLDGRPPAYALEGSIAITGALVQWLRDNL... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 54440
Sequence Length: 501
Pathway: Polyol metabolism; glycerol degradation ... |
P47284 | MDLKKQYIIALDEGTSSCRSIVFDHNLNQIAIAQNEFNTFFPNSGWVEQDPLEIWSAQLATMQSAKNKAQIKSHEVIAVGITNQRETIVLWNKENGLPVYNAIVWQDQRTAALCQKFNEDKLIQTKVKQKTGLPINPYFSATKIAWILKNVPLAKKLMEQKKLLFGTIDSWLIWKLTNGKMHVTDVSNASRTLLFDIVKMEWSKELCDLFEVPVSILPKVLSSNAYFGDIETNHWSSNAKGIVPIRAVLGDQQAALFGQLCTEPGMVKNTYGTGCFVLMNIGDKPTLSKHNLLTTVAWQLENHPPVYALEGSVFVAGAAI... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 56902
Sequence Length: 508
Pathway: Polyol metabolism; glycerol degradation ... |
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