ids
stringlengths 6
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stringlengths 11
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stringlengths 108
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P07562 | MKWATWILALGLLVVRTVVAREAPRELCYGHPVHDDRRPVGPATDAQPVNPLAPANATGTDYSRGCEMRLLDPPLDVSSRSSDPVNVTVAWFFDGGHCKVPLVHREYYGCPGDAMPSVETCTGGYSYTRTRIDTLMEYALVNASLVLQPGLYDAGLYIVVLVFGDDAYLGTVSLSVEANLDYPCGMKHGLTITRPGATLPPIAPTAGDHQRWRGCFPSTDEGAWENVTAAEKGLSDDYADYYDVHIFRSESDDEVVHGDAPEAPEGEEVTEEEAELTSSDLDNIEIEVVGSPAAPAEGPATEEGRGAEEDEELTSSDLDNIEIEVVGSPRPPASSPPPPPPRPHPRGRDHDHDHGHHRADDRGPQRHHRLPPEPTFVSPSDIFVTPTGSPALLLGFLGSALASRPLHLTAGETAQHVREAQQKSRHIRSLGGLQLSVETETTNTTTTQTGLSGDIRTSIYICVALAGLVVVGIVIMCLHMAIIRARARNDGYRHVASA | 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 | MGALIPSSTLFNIFDFNPKKVRIAFIAVGLRGQTHVENMARRDDVEIVAFADPDPYMVGRAQEILKKNGKKPAKVFGNGNDDYKNMLKDKNIDAVFVSSPWEWHHEHGVAAMKAGKIVGMEVSGAITLEECWDYVKVSEQTGVPLMALENVCYRRDVMAILNMVRKGMFGELVHGTGGYQHDLRPVLFNSGINGKNGDGVEFGEKAFSEAKWRTNHYKNRNGELYPTHGVGPLHTMMDINRGNRLLRLSSFASKARGLHKYIVDKGGESHPNAKVEWKQGDIVTTQIQCHNGETIVLTHDTSLQRPYNLGFKVQGTEGLWEDFGWGEAAQGFIYFEKIMNHSHRWDSSEKWIKEYDHPMWKKHEQKAVGAGHGGMDYFLDNTFVECIKRNEAFPLDVYDLATWYSITPLSEKSIAENGAVQEIPDFTNGKWKNAKNTFAINDDY | 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 group A lacto series glycolipids.
Sequence Mass (Da): 50211
Sequence Length: 444
EC: 3.2.1.49
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Q02643 | MDRRMWGAHVFCVLSPLPTVLGHMHPECDFITQLREDESACLQAAEEMPNTTLGCPATWDGLLCWPTAGSGEWVTLPCPDFFSHFSSESGAVKRDCTITGWSEPFPPYPVACPVPLELLAEEESYFSTVKIIYTVGHSISIVALFVAITILVALRRLHCPRNYVHTQLFTTFILKAGAVFLKDAALFHSDDTDHCSFSTVLCKVSVAASHFATMTNFSWLLAEAVYLNCLLASTSPSSRRAFWWLVLAGWGLPVLFTGTWVSCKLAFEDIACWDLDDTSPYWWIIKGPIVLSVGVNFGLFLNIIRILVRKLEPAQGSLHTQSQYWRLSKSTLFLIPLFGIHYIIFNFLPDNAGLGIRLPLELGLGSFQGFIVAILYCFLNQEVRTEISRKWHGHDPELLPAWRTRAKWTTPSRSAAKVLTSMC | 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 | MDGLMWATRILCLLSLCGVTLGHLHLECDFITQLRDDELACLQAAEGTNNTSLGCPGTWDGLLCWPPTGSGQWVSLPCPEFFSHFGSDTGFVKRDCTITGWSNPFPPYPVACPVPLELLTKEKSYFSTVKIIYTTGHSISIVALCVAIAILVALRRLHCPRNYIHTQLFATFILKASAVFLKDAAIFQGDSTDHCSMSTVLCKVSVAISHLATMTNFSWLLAEAVYLSCLLASTSPRSKPAFWWLVLAGWGLPVLCTGTWVGCKLAFEDTECWDLDNSSPCWWIIKGPIVLSVGVNFGLFLNIICILLRKLEPAQGGLHTRAQYWRLSKSTLLLIPLFGIHYIIFNFLPDSAGLDIRVPLELGLGSFQGFIVAVLYCFLNQEVRTEISRKWYGHDPELLPARRTCTEWTTPPRSRLKVLTSEC | 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-octanoylation or O-decanoylation is essential for activity. The O-decanoylated form ghrelin-21-C10 differs in the length of the carbon backbone of the carboxylic acid forming an ester bond with Ser-29. 44% of eel ghrelin is O-decanoylated .
Sequence Mass (Da): 12831
Sequence Length: 111
Subcellular Location: Secreted
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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 (By similarity). O-octanoylation is essential for ghrelin activity.
Sequence Mass (Da): 12793
Sequence Length: 116
Subcellular Location: Secreted
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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). O-octanoylation or O-decanoylation is essential for activity. The O-decanoylated form differs in the length of the carbon backbone of the carboxylic acid forming an ester bond with Ser-29 (By similarity).
Sequence Mass (Da): 11520
Sequence Length: 103
Subcellular Location: Secreted
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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-octanoylation or O-decanoylation is essential for activity. The O-decanoylated form ghrelin-27-C10 differs in the length of the carbon backbone of the carboxylic acid bound to Thr-27. 33% of frog ghrelin is O-decanoylated .
Sequence Mass (Da): 12756
Sequence Length: 114
Subcellular Location: Secreted
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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). O-octanoylation or O-decanoylation is essential for activity. The O-decanoylated forms differ in the length of the carbon backbone of the carboxylic acid forming an ester bond with Ser-29 (By similarity). The majority of trout ghrelin is Ghrelin-20 modified with unsaturated decanoic acid .
Sequence Mass (Da): 12304
Sequence Length: 111
Subcellular Location: Secreted
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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 (By similarity). O-octanoylation is essential for ghrelin activity.
Sequence Mass (Da): 12913
Sequence Length: 117
Subcellular Location: Secreted
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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). O-octanoylation is essential for ghrelin activity. The replacement of Ser-26 by aromatic tryptophan preserves ghrelin activity .
Sequence Mass (Da): 13176
Sequence Length: 117
Subcellular Location: Secreted
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Q9Z254 | MPLGLGRRKKAPPLVENEEAEPSRSGLGVGEPGPLGGSGAGESQMGLPPPPASLRPRLVFHTQLAHGSPTGRIEGFTNVKELYGKIAEAFRLPAAEVMFCTLNTHKVDMDKLLGGQIGLEDFIFAHVKGQRKEVEVFKSEDALGLTITDNGAGYAFIKRIKEGSVIDHIQLISVGDMIEAINGQSLLGCRHYEVARLLKELPRGRTFTLKLTEPRKAFDMISQRSSGGHPGSGPQLGTGRGTLRLRSRGPATVEDLPSAFEEKAIEKVDDLLESYMGIRDTELAATMVELGKDKRNPDELAEALDERLGDFAFPDEFVFDVWGAIGDAKVGRY | 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 | MTTSPILQLLLRLSLCGLLLQRAETGSKGQTAGELYQRWERYRRECQETLAAAEPPSGLACNGSFDMYVCWDYAAPNATARASCPWYLPWHHHVAAGFVLRQCGSDGQWGLWRDHTQCENPEKNEAFLDQRLILERLQVMYTVGYSLSLATLLLALLILSLFRRLHCTRNYIHINLFTSFMLRAAAILSRDRLLPRPGPYLGDQALALWNQALAACRTAQIVTQYCVGANYTWLLVEGVYLHSLLVLVGGSEEGHFRYYLLLGWGAPALFVIPWVIVRYLYENTQCWERNEVKAIWWIIRTPILMTILINFLIFIRILGILLSKLRTRQMRCRDYRLRLARSTLTLVPLLGVHEVVFAPVTEEQARGALRFAKLGFEIFLSSFQGFLVSVLYCFINKEVQSEIRRGWHHCRLRRSLGEEQRQLPERAFRALPSGSGPGEVPTSRGLSSGTLPGPGNEASRELESYC | 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 (Da): 53157
Sequence Length: 466
Subcellular Location: Cell membrane
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P43218 | MPLRPRLLLLCLWGLLLQQAETDSEGQTTGELYQRWERYARECEETLTAADPPSGMVCNGSFDMYVCWDYTAANTTAQASCPWYLPWYRHVAAGYVFRQCGSDGQWGPWRDHTQCENPEKNGAFQDQRLILERLQVVYTVGYSLSLGTLLLALLILSLFRRLHCTRNYIHMNVFLSFMLRAVAILTRDRLLPTLGPYPGDRTLTLRNQALAACRTAQIVTQYCVGANYTWLLVEGVYLHHLLVIVGGSEKGHFRCYLLLGWGAPALFVIPWVIVRYLLENTQCWERNEVKAIWWIIRTPILITILINFFIFIRILGILVSKLRTRQMRCPDYRLRLARSTLTLVPLLGVHEVVFAPVTEEQAEGTLRFAKLAFEIFLSSFQGFLVSVLYCFINKEVQSEIRRSWRHRVLHLSLRDERPCPHAELGPQALPSRSAPREVPITGSTLPSGPLHGPGEEVLESYC | 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 (Da): 52919
Sequence Length: 462
Subcellular Location: Cell membrane
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Q88IU0 | MNAFTQIDELVMPLPLEPQGYTIAPSKQSPRLLELTFARETVEAFVQAVAQWPVQALEYKSFLRFRVGEILDELCQGTLRPVLLNTILDRATGGMLITPIGLDDVSQAEDMVKFTTACAHLIGRSNYDAMSGQFYARFVVVNSDNSDSYLRQPHRVMELHNDGTFVNQITDYVLMLKIDEKNMEGGNSLLLHLDDWEQCEAFFRHPLARREMRWTAPPSKKVAEDVFHSVFDTDAEGRPTMRYIDQFVQPENYEEGIWLNALSESLEGSGKKVSVPVGVGSFLLINNLFWLHGRDRFTPHEGLRRELMRQRGYVAFPKPLYQRGQ | 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 specific for glutarate, but it can use both 2-oxoglutarate and 2-oxoadipate (2OA) as a cosubstrate for L2HG formation .
Catalytic Activity: 2-oxoglutarate + glutarate + O2 = (S)-2-hydroxyglutarate + CO2 + succinate
Sequence Mass (Da): 37177
Sequence Length: 325
Pathway: Amino-acid degradation.
EC: 1.14.11.64
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Q97UY8 | MVRIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGEINELEGKVTNEGVVIGSLRFPVSVSSDRAIIGIRPEDVKLSKDVIKDDSWILVGKGKVKVIGYQGGLFRITITPLDSEEEIFTYSDHPIHSGEEVLVYVRKDKIKVFEKN | 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 Topology: Peripheral membrane protein
Sequence Mass (Da): 39113
Sequence Length: 353
Domain: Consists of a typical ABC-ATPase domain, comprising two subdomains, connected by a linker region to a C-terminal domain of unknown function.
Subcellular Location: Cell membrane
EC: 7.5.2.-
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O80816 | MGSSYQESPPLLLEDLKVTIKESTLIFPSEETSERKSMFLSNVDQILNFDVQTVHFFRPNKEFPPEMVSEKLRKALVKLMDAYEFLAGRLRVDPSSGRLDVDCNGAGAGFVTAASDYTLEELGDLVYPNPAFAQLVTSQLQSLPKDDQPLFVFQITSFKCGGFAMGISTNHTTFDGLSFKTFLENLASLLHEKPLSTPPCNDRTLLKARDPPSVAFPHHELVKFQDCETTTVFEATSEHLDFKIFKLSSEQIKKLKERASETSNGNVRVTGFNVVTALVWRCKALSVAAEEGEETNLERESTILYAVDIRGRLNPELPPSYTGNAVLTAYAKEKCKALLEEPFGRIVEMVGEGSKRITDEYARSAIDWGELYKGFPHGEVLVSSWWKLGFAEVEYPWGKPKYSCPVVYHRKDIVLLFPDIDGDSKGVYVLAALPSKEMSKFQHWFEDTLC | 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, including RPS5a and FAC1, both of which being essential for early embryo and endosperm development in fertilized seeds .
Sequence Mass (Da): 50506
Sequence Length: 450
Subcellular Location: Cytoplasm
EC: 2.3.1.-
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Q17339 | MPSCTTPTYGVSTQLESQSSESPSRSSVMTPTSLDGDNSPRKRFPIIDNVPADRWPSTRRDGWSSVRAPPPARLTLSTNNRHIMSPISSAYSQTPNSLLSPAMFNPKSRSIFSPTLPATPMSYGKSSMDKSLFSPTATEPIEVEATVEYLADLVKEKKHLTLFPHMFSNVERLLDDEIGRVRVALFQTEFPRVELPEPAGDMISITEKIYVPKNEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMVRGKGSMRDKSKESAHRGKANWEHLEDDLHVLVQCEDTENRVHIKLQAALEQVKKLLIPAPEGTDELKRKQLMELAIINGTYRPMKSPNPARVMTAVPLLSPTPLRSSGPVLMSPTPGSGLPSTTFGGSILSPTLTASNLLGSNVFDYSLLSPSMFDSFSSLQLASDLTFPKYPTTTSFVNSFPGLFTSASSFANQTNTNVSPSGASPSASSVNNTSF | 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 to the 3' UTR of Notch receptor homolog glp-1, thereby repressing glp-1 translation in the embryo . Binding to the glp-1 3' UTR is inhibited by pos-1 binding to an overlapping binding site in the glp-1 3' UTR . Germ line-specific tumor suppressor essential for oogenesis . Controls the spatial pattern of translation of multiple oogenesis specific mRNAs (e.g. yolk receptor rme-2) by repression of translation during early meiotic prophase (leptotene to pachytene) and then derepression of translation during diplotene/ diakinesis, following its degradation. Also functions to promote the male sexual fate in the hermaphrodite germline but not the male germline . Represses translation of the vacuolar ATPase component vha-13 in the distal gonad . Functions redundantly with gld-2 to promote the initiation of meiotic development and/or inhibit stem cell proliferation . By regulating cye-1 expression, prevents entry into mitosis in meiotic germline cells .
PTM: Phosphorylated by cdk-2 which may negatively regulate its expression in distal mitotic germline cells.
Sequence Mass (Da): 50586
Sequence Length: 463
Domain: The KH domain and the Qua2 region are involved in RNA binding.
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Q0GYU5 | MSSGRTVTLNTGYKIPQIGYGTWQAAPGEVGAGVFEALKVGYRHLDLAKVYGNQKEVGEGIKKALAEVPGLKREDIFITSKLWNNSHKPEDVEPALDDTLAELGLDYLDLYLIHWPVAFAPGADLFPKSEDGSEVQLNQNVSIVQTWKAMTELPKSKVRSVGVSNFTIEHLDAVIEATGVVPAVNQIERHPRLPNQPLIDYCAKKGIIITAYSAFGNNTKGLPLLVSSDEVKAVADNLSKKQGKTVTPAQVILAWSQIGGHTVIPKSVTKARIAENFQEVELDDEAIAALNKLGEKPQRFNIPYTYKPRWNINLFNTEEEKAAAHTAVIKL | 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 | MIGPRLCAATPRFPLVSLAHRNSKVFALASSNAVAQRWGKRFYAPIETETPHKVGVEFEESKDRIFTSPQKYVQGRHAFTRSYMYVKKWATKSAVVLADQNVWNICANKIVDSLSQNGMTVTKLVFGGEASLVELDKLRKQCPDDTQVIIGVGGGKTMDSAKYIAHSMNLPSIICPTTASSDAATSSLSVIYTPDGQFQKYSFYPLNPNLIFIDTDVIVRAPVRFLISGIGDALSTWVETESVIRSNSTSFAGGVASIAGRYIARACKDTLEKYALSAILSNTRGVCTEAFENVVEANTLMSGLGFENGGLAAAHAIHNGMTAIHGPVHRLMHGEKVAYGTLVQVVLEDWPLEDFNNLASFMAKCHLPITLEELGIPNVTDEELLMVGRATLRPDESIHNMSKKFNPSQIADAIKAVDSYSQKWQEQTGWTERFRLPPSRHSPHLTDIHP | 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 (oxidative route): step 1/2.
Subcellular Location: Mitochondrion
EC: 1.1.1.6
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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 complex . May be required for cell cycle progression .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32710
Sequence Length: 294
Subcellular Location: Golgi apparatus membrane
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Q9FN15 | MLRLIVNYPLIPKISHRVCSNSSSKLGSYYDSSSIIKYGGISDVVGKKQELFLSVSVKAVEDKGNNGGGSMSFSGQSWDPSSEIEVPSDQRPVNEYSSLKEGMLYSWGELGPSEFFIRLGGLWLVTFTVLGVPVAAASFNPSREPLRFILAAGTGTLFLVSLIVLRIYLGWSYVGDRLLSAVIPYEESGWYDGQMWVKPPEVLARDRLLGSYKVKPVIKMLKQTLIGTGALLVSAFVLFVFATPVEDFFKTTLGSTENQPEVSISRTSNKFNIRKEQLLRLPVDVVTDDDLAAAAAEAADGRPVYCRDRYYRALAGGQYCKWEDLVK | 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 | MYPNSPSLGRIPLPLPCARQQQTSAYLSKVPVSVAPDLLSPEQFFQASLNIHKNANLPRLLMNGNVLTVPPLSSPPWSYLNHSPLISPGSPPSSFQNRKRRSDEGNSPYDVKRQRFQSPQEQTVNHQAVPLRGDIRCSYPGSPAFPLLQSPSPPVLKGHSSNSGDCWLYDHIDTTLPVAKDKLSKQILDLFQALQQQVCDLKKKDICRAELQREIQQIFPQSRLYLVGSSLNGFGIRSSDADLCLVLKEEPMNQNTEARHILSLLHKHFYTRLSYIERPQFIRAKVPIVKFRDKVSGAEFDLNVNNVVGIRNTFLLRTYAYLDKRVRPLVLVIKKWANHHGINDASRGTLSSYTIVLMVLHYLQTLPEPILPSLQKKYPECFDRTMQLHLVHQAPRNIPQFLSKNETPLGDLLLGFLKYFAVEFDWSKDIISLREAKALPRTDDYEWRNKYICVEEPFDGSNTARAVYEKQKFDLIRAEFLKAWVALRDNRDLYSLLPVKGIMKKMHSL | 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 by mediating polyadenylation of dormant mRNAs, which contain 5'AAUAAA-3' sequence in their 3'-UTR. In immature oocytes, polyadenylation of poly(A) tails is counteracted by the ribonuclease parn. During maturation parn is excluded from the ribonucleoprotein complex, allowing poly(A) elongation and activation of mRNAs. May not play a role in replication-dependent histone mRNA degradation (By similarity).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 58235
Sequence Length: 509
Subcellular Location: Cytoplasm
EC: 2.7.7.19
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Q503I9 | MLPRPYIFSHNDGPSSHLFQHVLPHNVSQQQRIEAHLNSTNNFIGPPMNAPRFIPTYQWTPVELSDVACSPNGPMGNNRKRRIQDNSDINLKRQRFSCPSPHNQSARNSNFTSQPVTRPVTGREVTCPTCSSATFIPGGCVPSLGETCHQNAFSPSSVKDKLSQQILNLFFACEQQSDDLEKKESCRAALQTDIQKIFPCAKVFLGGSSLNGFGSRSSDADLCLVIEEGPVNHRKDAVYVLSLVRKLLYKLSYIEKPQLIRAKVPIVKFRDRISGVEFDLNFNNTVGIRNTFLLRTYAFVEKRVRPLVLVIKKWANHHCINDASRGTLSSYTLVLMVLHYLQTLPEPVIPCLQRDYPTCFDPKMDIHLVPSGPSDIPAFVSRNQSSLGDLFLGFLRYYATVFKWDKQVISVRMARTLPKSNCKEWKDKFICVEEPFNRTNTARAVHERMKFEAIKAAFIESHRLLQLRKDLNFILPKSKQMARPQTAPR | 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 (By similarity).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 55562
Sequence Length: 489
Subcellular Location: Cytoplasm
EC: 2.7.7.19
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Q6PIY7 | MFPNSILGRPPFTPNHQQHNNFFTLSPTVYSHQQLIDAQFNFQNADLSRAVSLQQLTYGNVSPIQTSASPLFRGRKRLSDEKNLPLDGKRQRFHSPHQEPTVVNQIVPLSGERRYSMPPLFHTHYVPDIVRCVPPFREIAFLEPREITLPEAKDKLSQQILELFETCQQQISDLKKKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKEEPCFFQVNQKTEARHILTLVHKHFCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHQINDASRGTLSSYSLVLMVLHYLQTLPEPILPSLQKIYPESFSPAIQLHLVHQAPCNVPPYLSKNESNLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPDGIEWRNKYICVEEPFDGTNTARAVHEKQKFDMIKDQFLKSWHRLKNKRDLNSILPVRAAVLKR | 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 . Adds a single nucleotide to the 3' end of specific miRNAs, monoadenylation stabilizes and prolongs the activity of some but not all miRNAs .
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 56028
Sequence Length: 484
Subcellular Location: Cytoplasm
EC: 2.7.7.19
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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 | MFPNSILGRPPFTPTHQQHNNFFALSPTLYSHQQLIDAQFNFQNVDLSRAVSLQPLTYGTVSPIQTSTSPLFRGRKRISDEKAFPLDGKRQRFHSPHQEPTIINQLVPLSGDRRYSMPPLFHTHYIPDIVRCVPPLREIPLLEPREITLPEAKDKLSQQILELFETCQQQASDLKKKELCRAQLQREIQLLFPQSRLFLVGSSLNGFGARSSDGDLCLVVKEEPCFFQVNQKTEARHILTLVHKHFCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNTVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHDINDASRGTLSSYSLVLMVLHYLQTLPEPILPSLQKIYPESFSTSVQLHLVHHAPCNVPPYLSKNESSLGDLLLGFLKYYATEFDWNTQMISVREAKAIPRPDDMEWRNKYICVEEPFDGTNTARAVHEKQKFDMIKDQFLKSWQRLKNKRDLNSVLPLRAATLKR | 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 (By similarity).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 55934
Sequence Length: 484
Subcellular Location: Cytoplasm
EC: 2.7.7.19
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Q8CWX0 | MKILFVAAEGAPFAKTGGLGDVIGALPKSLVKNNNEVSVILPYYDVVDAKFGDQIEDLFYFFTNVGWRREYVGIKHIFRDGVDFYFIDNKHYFYRGQIYGEFDDGERFAYFQLAALEAMEKIQFIPDILHVHDYHTAMIPYLLKEKYHWINAYHGIKTVFTIHNIEFQGQFNPSMLGELFGVGDERYRDGTLRWNDCLNWMKAAVLYADRVTTVSPSYAKEIMTPEFGKGLDQIMRMESGKLSGVVNGIDTDLFDPETDPHLAVHFSKDDLSGKAKNKAALQERVGLPVREDVPLVGIVSRLTDQKGFQLVVDQLNTMMQLDLQIVLLGTGYADFENAFAWFGHAYPDKMSANITFDLELAQQIYAASDIFLMPSAFEPCGLSQMMAMRYGTLPLVHEVGGLRDTVIPYNEFEKTGTGFGFQDFSGYWLTKTLEAALDVYYNRKEDWKILQKNAMTTDFSWDTASQSYEHLYKELA | 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 | MSERQGGQEQRTEADGMTTEGISETSQTLQALANGLPADAFAVLGPKPLAEGRRQVRVLAPGAEAMGLIDPRGKLLARMQASAIDGVFEGILAADGPYRLRIVWPDRVQEVEDPYAFAATLDESLLLQIAAGDGQAVRRALGAQHVHCGDVPGVRFAVWAPHAQRVAVVGDFNGWDVRRHPMRQRIGGFWELFLPRVEAGARYKYAVTAADGRVLLKADPVARQTELPPATASVVPSAAAFAWTDAAWMANRDPGAVPAPLSIYEVHAASWRRDGHNQPLDWPTLAEQLIPYVQQLGFTHIELLPITEHPFGGSWGYQPLGLYAPTARHGSPDGFAQFVDACHRAGIGVILDWVSAHFPDDAHGLAQFDGAALYEHADPREGMHRDWNTLIYNYGRPEVTAYLLGSALEWIEHYHLDGLRVDAVASMLYRDYGRAEGEWVPNAHGGRENLEAVAFLRQLNREIATQFPGVLTIAEESTAWPGVTAAISDGGLGFTHKWNMGWMHDTLGYMQRDPAERAQHHSQLTFGLVYAFDERFVLPLSHDEVVHGTGGLLGQMPGDDWRRFANLRAYLALMWAHPGDKLLFMGAEFGQWADWNHDQSLDWHLLDGARHRGMQQLVGDLNAALRRTPALYRGSHRADGFDWSVADDARNSVLAFVRHDPAGGAPLLAVSNLTPQPHHDYHVGVPRAGLWREILNTDSAHYGGSNLGNSGRLATEPVGMHGHAQRLRLTLPPLATIYLQAEK | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 81692
Sequence Length: 743
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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D2WL32 | MVSLSNQTRFSFHPNNLVVSEKRRLGISGVNFPRKIKLKITCFAAERPRQEKQKKKSQSQSTSDAEAGVDPVGFLTRLGIADRIFAQFLRERHKALKDLKDEIFKRHFDFRDFASGFELLGMHRHMEHRVDFMDWGPGSRYGAIIGDFNGWSPTENAAREGLFGHDDYGYWFIILEDKLREGEEPDELYFQQYNYVDDYDKGDSGVSAEEIFQKANDEYWEPGEDRFIKNRFEVPAKLYEQMFGPNSPQTLEELGDIPDAETRYKQWKEEHKDDPPSNLPPCDIIDKGQGKPYDIFNVVTSPEWTKKFYEKEPPIPYWLETRKGRKAWLQKYIPAVPHGSKYRLYFNTPDGPLERVPAWATYVQPEDEGKQAYAIHWEPSPEAAYKWKYSKPKVPESLRIYECHVGISGSEPKVSTFEEFTKKVLPHVKRAGYNAIQLIGVPEHKDYFTVGYRVTNFFAASSRYGTPDDFKRLVDEAHGLGLLVFLDIVHSYAAADQMVGLSLFDGSNDCYFHYGKRGHHKHWGTRMFKYGDLDVLHFLISNLNWWITEYQVDGYQFHSLASMIYTHNGFASFNNDLDDYCNQYVDRDALMYLILANEILHVQHPNIITIAEDATYYPGLCEPVSQGGLGFDYYVNLSASEMWVSLLDNVPDNEWSMSKIVSTLVANKEYADKMLSYAENHNQSISGGRSFAEILFGGVDNGSPGGKELLDRGISLHKMIRLITFTSGGRAYLNFMGNEFGHPERVEFPTQSNNFSFSLANRRWDLLESGVHHHLFSFDKELMDLDKSKGILSRGLPSIHHVNDANMVISFSRGPFLFIFNFHPSNSYEKYDVGVEEAGEYTMILNSDEVKYGGQGIVTEDHYLQRSISKRIDGQRNCLEVFLPSRTAQVYKLTRILRI | 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 of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 103525
Sequence Length: 899
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.4.1.18
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A6VP15 | MTTFVTQDTINAFFDGRHADPFAVLGMHETDNGIEIRALLPDAGRVVVIDKETQDEVCELSRIDERGFFAGIMPQRNSFFNYQLQVSWGNEVLRIEDPYRFHPMIQELDNWLLAEGSHLRPYEVLGAHFMECDHVSGVNFRLWAPNAKRVSVVGDFNYWDGRRHPMRFHQASGVWELFIPKVALGDLYKFELLDNNNRLRLKSDPYAFAAQLRPDTASQISVLPEIQEMTAARRKANQLDQPISIYEVHLGSWRRNLANNFWLNYDEIADELIPYVKEMGFTHIELLPISEFPFDGSWGYQPIGLYAPTSRFGSPEGFKRFVDKAHAAGINVILDWVPGHFPSDTHGLATFDGTALYEHADPKEGYHQDWNTLIYNYGRHEVKNYLSGNALYWVERFGLDGIRVDAVASMIYRDYSRRDGEWIPNQYGGRENLEAIEFLKHTNYILGTEHPGVMCVAEESTAFAGVTLPPENGGLGFNFKWNMGWMNDTLSYMKLDPIYRQYNHSKLTFGMLYQYSENFVLPLSHDEVVHGKCSLLDKMPGDTWQKFANLRAYYGYMWAYPGKKLLFMGNEFAQGREWNYQESLDWYLLDEFHGGGWHSGVQRLVKDLNKTYQKQSALYQLDTKPEGFEWLVVDDAQNSVFVFERRNAKGEPLIVVSNFTPVPRENYRFGVNVAGSYEEILNTDADIYKGSGLNNGGVIDSEEIESHGKTQSISITVPPLATVYFKLKSARKVASPRKVTKKKTTADGAEATAKNASASKATKVSTKKTVKSSEAKPVKAATKSSVTKVATKKSTDKPTAKATRTKKATVTKTAKASAKTTAKKTKDNA | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 94021
Sequence Length: 829
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q8U8L4 | MKKPLNSAEEKKTGDITKAEIEAIKSGLHSNPFALLGVHETPEGFSARCFIPGAEEVSVLTLDGNFVGELKQIDPDGFFEGRIDLSKRQPVRYRACRDDAEWAVTDPYSFGPVLGPMDDYFVREGSHLRLFDRMGAHPLKLEGVEGFHFAVWAPNARRVSVVGDFNNWDGRRHVMRFRKDTGIWEIFAPDVYAGCAYKFEILGANGELLPLKADPYARRGELRPKNASVTAPELTQKWEDQAHREHWAQVDQRRQPISIYEVHAGSWQRREDGTFLSWDELAAQLIPYCTDMGFTHIEFLPITEHPYDPSWGYQTTGLYAPTARFGDPEGFARFVNGAHKVGIGVLLDWVPAHFPTDEHGLRWFDGTALYEHADPRQGFHPDWNTAIYNFGRIEVMSYLINNALYWAEKFHLDGLRVDAVASMLYLDYSRKEGEWIPNEYGGRENLESVRFLQKMNSLVYGTHPGVMTIAEESTSWPKVSQPVHEGGLGFGFKWNMGFMHDTLSYFSREPVHRKFHHQELTFGLLYAFTENFVLPLSHDEVVHGKGSLIAKMSGDDWQKFANLRSYYGFMWGYPGKKLLFMGQEFAQWSEWSEKGSLDWNLRQYPMHEGMRRLVRDLNLTYRSKAALHARDCEPDGFRWLVVDDHENSVFAWLRTAPGEKPVAVICNLTPVYRENYYVPLPVAGRWREILNTDAEIYGGSGKGNGGRVQAVDAGGEIGAMLVLPPLATIMLEPEN | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 83761
Sequence Length: 735
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q21WG7 | MKSDHDIYLFREGTHAKLYNKLGCHLQSNGGANFAVWAPNAESVSVVGDWNYWSGNVDRLDLRDDGSGIWQGFVENAVRGQGYKYRIQSSHGSYGVDKADPFAFYAEPPPATASRVWSLEHDWKDDQWMSSRGPKNALDAPMSIYEIHLGSWRRQDGHFLDYRELAHSLADYVIEMGFTHVELMPVTEHPFYGSWGYQTTGYFAPTSRFGTPQDFMHFVDHLHQRGIGVLLDWVPSHFPTDEHGLGYFDGTHLFEHSDPRQGFHPEWNSSIFNYGRNEVRSFLISSGLFWLDKYHLDGLRVDGVASMLYLDYARKEDEWIPNRHGGRENLEAVDFLQTLNKAVYREYPDTLTIAEESTAWPRVSRPTDMDGLGFGMKWNMGWMHDSLAYMQQEPVHRKYHHHKLTFSLVYAFNENFVLPLSHDEVVHGKGSLLGKMPGDAWQQFANLRALFGYMWAHPGKKLLFMGGEFGQRREWTHDGELEWWVTKLEGHAGLQRYVAQLNRVYRSLPALYQLDFSPAGFEWVEADAADTSVFAFLRKPREHGAPVLIVSNMTPVPRTNYMLGVPLAGFWREVINSDASEFGGSGWGNLGGVEASPVRFHGRPHSVCLTLPPLSTLIFEHVPHA | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 71407
Sequence Length: 625
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q0AA26 | MRVYDPHAEAVAFEDGTKLPRRPGSDFFEGPLPAGLSAPYRLRRTSQDGAAHTAHDPYAFGPALPDYDLHLFGEGRHYHAQRFLGAHPLEHEGVPGVRFAVWAPNAERVSVVGDFNRWDGRCHPMRVRGGSGVWELFIPGLPDGSLYKFELRNRDSGAVLVKTDPYGRRYQLRPDSAAVVEPPADYAWNDREWMAARREDQWQSIPISIYEVHLGSWQRAGDGSFLDYRTLAHRLVDHVLATGFTHIELLPITEHPFDGSWGYQTTGYFAPTTRFGAPDDFRYFVDHCHRHGIGVILDWVPAHFPRDDWALANFDGTPLYEHADPRRGEHRDWGTLIFNFGRNEVRNFLTASALYWLEEFHIDGLRVDAVASMLYLDYSRDEGDWVPNIHGGNENLEAIDFLQELNRITHGEQPGTMIMAEESTSWPQVTRPTWLGGLGFTMKWNMGWMHDTLTYMGEDPIHRRYHHDQLTFGMLYAFTENFVLPFSHDEVVHGKRSLLWRMPGDEWQRFANLRLLYAYQFTYPGKKLLFMGCEFGQGNEWNAEAALDWYVLDYPLHQGVLRLVGDLNALYREVPALHRHDFDEHGFAWIDCHDTEQSAISYLRRDGGHDGEATPPAATVLNFTPVPRHDYRLGVPAPGYWRERLNTDSTHYGGTNLGNGGGVWAEAVPWMGHPWSVVLTLPPLAGVVLSPEAGP | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 79236
Sequence Length: 695
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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O66936 | MKKFSLISDYDVYLFKEGTHTRLYDKLGSHVIELNGKRYTFFAVWAPHADYVSLIGDFNEWDKGSTPMVKREDGSGIWEVLLEGDLTGSKYKYFIKNGNYEVDKSDPFAFFCEQPPGNASVVWKLNYRWNDSEYMKKRKRVNSHDSPISIYEVHVGSWRRVPEEGNRFLSYRELAEYLPYYVKEMGFTHVEFLPVMEHPFYGSWGYQITGYFAPTSRYGTPQDFMYLIDKLHQEGIGVILDWVPSHFPTDAHGLAYFDGTHLYEYEDWRKRWHPDWNSFVFDYGKPEVRSFLLSSAHFWLDKYHADGLRVDAVASMLYLDYSRKEWVPNIYGGKENLEAIEFLRKFNESVYRNFPDVQTIAEESTAWPMVSRPTYVGGLGFGMKWNMGWMNDTLFYFSKDPIYRKYHHEVLTFSIWYAFSENFVLPLSHDEVVHGKGSLIGKMPGDYWQKFANLRALFGYMWAHPGKKLLFMGGEFGQFKEWDHETSLDWHLLEYPSHRGIQRLVKDLNEVYRREKALHETDFSPEGFEWVDFHDWEKSVISFLRKDKSGKEIILVVCNFTPVPRYDYRVGVPKGGYWREIMNTDAKEYWGSGMGNLGGKEADKIPWHGRKFSLSLTLPPLSVIYLKHEG | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 74168
Sequence Length: 630
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q96VA4 | MGTSQAVDSSPPDGTGVIQLDPWLEPFRDALKQRFSFIEGWVKAINETEGGLETFSKGYERFGLNVQSNGDIIYREWAPNAVQAQLVGEFNNWDVTAHPMTKNGFGVWEVTVPAVNGAPAIPHDSKIKISMVIPSGERIYRIPAWIKRVVQDLSVSPTYEAVFWNPPTEKQYKFQYSRPKRPESLRIYEAHVGISSPETKVATYKEFTSNMLPRIKYLGYNAIQLMAIMEHAYYASFGYQVNNFFAASSRYGTPEDLKELVDKAHSMGLVVLLDVVHSHASKNVLDGLNMFDGTDHLYFHGGGKGRHELWDSRLFNYGHHEVLRFLLSNLRFWMEEYGFDGFRFDGVTSMLYTHHGIGTGFSGGYHEYFGSSVDEEGVMYLTLANEMLHNLYPNCITVAEDVSGMPALCLPHSLGGVGFDYRLAMAVPDMYIKLLKEKKDDEWDIGNLSFTLTNRRHGEKTIAYAESHDQALVGDKTLMMWLCDKEMYTHMSVLTEFTPIIERGMALHKLIRLVTHGLGGEGYLNFEGNEFGHPEWLDFPRDGNNNSFWYARRQLNLTEDHLLRYKFLNDFDRAMQLTEEKYGWLHSPQAYVSLKNETDKVLVFERAGLLWIFNFHPTNSFTDYRVGVEQSGTYRIVLDTDDPAFGGLNRNLKETRFFTTDLSWNGRSNFLQVYIPTRTALVLALEETL | 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 | MQLEKQLQHAQCTFPFSHLGLLKTDNAFTITAWVPNATGIKVIDLATDKAIGSLKRQAQSDLFTAEFTKGNPPAVYAFEVKNAQGSYRIIDPYQFQDQAFHAVHFVDHLPKNVYQQLGAQLIDLDVGLKTPIAATRFAVFAPNASAVSVIGDFNYWDGSCLPMQKTDFGYWVLVVPGVKAGDKYKYQIKDAHGNELPHKADPVGFYAEQYPSHASVVFDHEQYQWQDTKWQQQVKGDKYTQAMSIYEVHLGSWKRPDSQSGKTYLSYHELVDELIPYVKDMGYTHLELLPISEFPFDGSWGYQPVGLFAPTSRFGGPDDFKYFVDQCHQNGIGVIIDWVPAHFPEDGHGLARFDGTHVYEYEDPRKGWHPDWNSCIYDFGKDTVRQFLVANALFWLDKYHVDGLRVDAVASMLYLDYSREADEWVPNVDGGNHNYEAISLLQWMNKEVYSHYPNAMTIAEESTSFAKVSRPVFEGGLGFGFKWNMGWMHDSLHYISKDPSYRRYHHGEMTFSMVYAYDESFVLPISHDEVVHGKGSLLRKMPGDEWQQAANLRCYAAFMYAHPGKKLNFMGNEIGQSAEWNHDSSINWHLLDYDKHSGIQALYRDLNTLYAEYPALHELDHDPAGFEWIDHENAEQSTLAMLRQSKGGKQQVYALSNFTPVPRTNFRLGVKAPGEYSILLNTDDKQYWGSGHSQNKTIKADKTPWNNQAYSISVSLPPLATVFILYKGQ | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 83113
Sequence Length: 729
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q9I1W2 | MSEPMSERERWQLELDKLQRGLQGDPFAFLGPQRDPGGEGGVLRAYLPGAQRVELLDEDGATLAELEQSDPGSGLFQRHLERLPPRYRLRVHWPDGVQESEDPYAFGPLLGELDLYLFAEGNHRQLASCLGAQLTRHEGVEGVRFAVWAPNAVRVSVVGDFNGWDGRRHPMRRRYPSGVWELFVPRLGEGELYKYELQGHDGLLPLKADPLALACETPPGTASKTCAALRHEWRDQDWLARRAERQGYAAPLSIYEVHAGSWRHRDGRPPHWSELAEELIPYVRQLGFTHIELMPVMEHPFGGSWGYQPLGLFAPTARYGTPEDFAAFVDACHQAGIGVILDWVPAHFPTDAHGLGRFDGTALYEYEHPFEGFHQDWDTYIYNLGRSEVHGFMLASALHWLRTYHVDGLRVDAVASMLYRDYSRKEGEWLPNRHGGRENLEAIDFLHHLNQVVASETPGALVIAEESTAWPGVSRPVAEGGLGFSHKWNMGWMHDSLAYIGEDPLHRRYHHHQLTFGLLYAFSEHFILPISHDEVVHGKHSLLDKMPGDRWQKFANLRLYLSFMWSHPGKKLLFMGCEFGQWREWNHDGELDWYLLRYPEHQGVQDLVAALNRLYRELPALHARDGEALGFEWLIGDDQANSVYAWLRHAAGEPSLLAVHNFTPVPRQGYRIGVPQGGDWDVLLNSDAQAFAGSGAGSQGRVSSESCGAHGQAQSLVLDLPPLGTLLLRPAG | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 82563
Sequence Length: 732
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q88FN1 | MNVTTRENGGLRQRDLDALARAEHADPFAVLGPHGDGAGGQVVRAFLPNALKVRIQARDDGRVLAEMEQGSLPGLFSAHLDKAQPYQLHIVWAGGEQVTEDPYSFGPQLGDMDLHLFAEGNHRDLSGRFGAQPTQVDGIDGVCFSVWAPNARRVSVVGDFNNWDGRRHPMRLRHGAGVWELFIPRLGVGETYKFEVLGKDGILPLKADPLARATELPPSTASKVAGELSHAWQDHDWMAQRAQRHAYNAPLSIYELHPGSWRCELDEAGEIGRFYNWRELAERLVPYVQELGFTHIELLPIMEHPFGGSWGYQPLSMFAPTSRYGSAEDFAAFIDACHQGGIGVLLDWVPAHFPTDEHGLARFDGTALYEYDNPLEGYHQDWNTLIYNLGRNEVRGFMMASALHWLKHFHIDGLRVDAVASMLYRDYSRKAGEWVPNRHGGRENLEAIDFIRHLNGVAAHEAPGALIIAEESTAWPGVSQPTQQGGLGFAYKWNMGWMHDTLHYIQNDPVHRTYHHNEMSFGLIYAYSEHFILPISHDEVVHGKHSLIDKMPGDRWQKFANLRAYLTFMWAHPGKKLLFMGCEFGQWREWNHDAELDWYLLQYPEHQGVQRLVGDLNRLYREEPALHEQDCQPQGFQWLIGDDAQNSVYAWLRWSSSGEPVLVVANFTPVPREGYRIGVPFGERWQELLNSDAELYAGSNVGNLGAVASDEVASHGQPLSLALNLPPLGVLIMKPA | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 82877
Sequence Length: 736
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q8XT76 | MTSVHDFATATRPATPSAAAQEPAPALPPGLDRNTLDALTHGRLGDPFAVLGPHRLETAEGERPHRVVRAFHPGARRVQAIDPRGQVMAELAPVGRTGLFHGRLPDDAPDADGHPGAYRLRVVWPAGAGHEAVQEAEDPYAFGLLLGDLDLHLIAEGRHWELARCLGAQAMRQDDVAGVRFAVWAPNARRVSVVGDFNQWDGRRHPMRLRHGTGVWELFVPAGLGAGPGSRYKFELVGADGHLLVKADPVARRTEAPPATASVVADPLPFRWSDAAWMETRAARQRPDAPIAIYEVHAGSWLRDVEDGGRSLDWDALGERLIPYVAGLGFTHVELLPVAEHPFGGSWGYQPLGLFAPSARFGPPEAFARFVERCHQAALGVIVDWVPAHFPSDPHGLARFDGTALYEHADPREGFHQDWNTLIYNFGRHEVRGFLIASALEWLEHFHIDGLRVDAVASMLYRDYSRPADAWVPNRYGGRENLEAVAFLQQMNAVVHARCPGAITIAEESTAWPGVTAAVEFNGLGFDYKWNMGWMHDTLHYMQRDPIYRQHHHDGLTFGLVYAFSERFILPLSHDEVVHGKGSLLGKMPGDDWQRLANLRAYLAFMWTHPGKKLLFMGGEFGQLGEWNHDAAPEWHLLDDPRHRGVQRLVHDLNALYRSEPALHARDCAPEGFSWVIGDDRANSVFAYLRLDTAGTPMLIVANMTPVPRDGYRIGVPDVDGAVRWREMLNTDSAVYGGTNLGNGGVVDVEDVESHGWRRSVVVRLPPLAVVVLKV | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 85728
Sequence Length: 775
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q7UVH1 | MNSQLSLSTIQSLVDGSVANPGSLLGRHPVNYRGREATSVRVLEPNAESVWLIDSASGLRRPMRRLHPGGFFEAICDEPITKPSTSRLQMIDKTGKEIKTTSPYTVPSIFSDLDRYLIGEGRHNQLYERLGAQLREVDGVKGVNFAVWAPNARSVQVVGDFNGWDGRGHVAQPVESTGIWELFLPGATVGQKYKFRIQTQHGHWMDKCDPMAFAAELPPLTANIITDINTYSWNDSDWLQQRAEMDPMHTPMNVYEVHLGSWQKGPGRTHGWLDYRDLAKRLVDYCHRMNFTHVELMPISEHPFTGSWGYQSVGYYAPTSRHGSPEDFMFFVDHMHQNGIGVLIDWVPAHFPKDDHGLRQFDGSALYEHADPRQGEHPDWGTMIFNFGRNEVKNFLIANALFWLDKYHIDGLRVDAVASMLYLDYSREDGEWIPNRYGGRENLESIDFLRDFNIAVHENHPGVITAAEESTAWPGVSRPTYDGGLGFTYKWNMGWMNDTLSYMRNEPIHRKFHQNELTFSLIYAFTENFTLPLSHDEVVHGKGSLISQMPGDMWQKFANLRLLYSYMWTHPGKKLLFMGGEIAQWTEWNADDGPQWELLDFDTHRGVQQLVADLNKVVIENPALHWHDFTGDGFEWIDAHNAEDSVLVYLRKGAEGDPPILVCNNFTPVPRDNYRVGVPAQGFWKEIFNSDGEAYGGSNLGNYPGCQTTGIEHHARPDSIEVTLPPLGTTILRLES | 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 chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 83639
Sequence Length: 736
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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Q9CHN1 | MAIEMLGLILAGGQGTRLGKLTKDVAKPAVPFGGRYRIIDFALSNCANSNVKNVGVITQYQPLTLNAHIGNGAPWGLNGINSGVTILQPYSSQEGSKWFEGTSHAVYQNISYIDQQNPEYVLILSGDHIYKMDYEAMLESHKEREASLTVSVMEVPLEEASRFGIMNTDDNDRIIEFEEKPKEPKSNLASMGIYIFNWKRLREVLVNGYSKGNPMEDFGGDVIPAYIEAGENVFAYRFKGYWKDVGTIDSLHQSSMEFLDLNNELNITDKSWRIYSHNDISAPQFITEKSNVKNALVGDGCYVDGTVLHSILSQNVHVQEGTVIEDSFIMSGTFIGENVTIKNAIIGENAKIGDNVEIIGENEVAVIGHGEIKGENKNEQ | 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-glucose + diphosphate
Sequence Mass (Da): 42053
Sequence Length: 380
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.7.27
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P55233 | MDASAAAINVNAHLTEVGKKRFLGERISQSLKGKDLRALFSRTESKGRNVNKPGVAFSVLTSDFNQSVKESLKYEPALFESPKADPKNVAAIVLGGGAGTRLFPLTSRRAKPAVPIGGCYRLIDVPMSNCINSGIRKIFILTQFNSFSLNRHLARTYNFGDGVNFGDGFVEVFAATQTPGESGKKWFQGTADAVRQFFWAFEDSKSKDVEHIVILSGDHLYRMDYMSFWQKHIDTNADITVSCIPMDDSRASDYGLMKIDHTGRIVHFAEKPKGSDLTAMQVDTTVLGLSDLEAMSNPYIASMGVYVFRTDVLMELLNRKYPSSNDFGSEIIPSAVGESNVQAYLFNDYWEDIGTIKSFFDSNLALTQQPPKFEFYDPKTPFYTSARFLPPTKVDRCKIVDSIVSHGCFLQESSIQHSIVGVRSRLESGVEFQDTMMMGADYYQTESEIASLLAEGKVPVGVGQNTKIKNCIIDKNAKIGKDVVIANTDGVEEADRPNEGFYIRSGITIILKNATIQDGLVI | 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 biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.7.7.27
|
Q00081 | NKIKPGVAYSVITTENDTQTVFVDMPRLERRRANPKDVAAVILGGGEGTKLFPLTSRTATPAVPVGGCYRLIDIPMSNCINSAINKIFVLTQYNSAPLNRHIARTYFGNGVSFGDGFVEVLAATQTPGEAGKKWFQGTADAVRKFIWVFEDAKNKNIENIVVLSGDHLYRMDYMELVQNHIDRNADITLSCAPAEDSRASDFGLVKIDSRGRVVQFAEKPKGFDLKAMQVDTTLVGLSPQDAKKSPYIASMGVYVFKTDVLLKLLKWSYPTSNDFGSEIIPAAIDDYNVQAYIFKDYWEDIGTIKSFYNASLALTQEFPEFQFYDPKTPFYTSPRFLPPTKIDNCKIKDAIISHGCFLRDCSVEHSIVGERSRLDCGVELKDTFMMGADYYQTESEIASLLAEGKVPIGIGENTKIRKCIIDKNAKIGKNVSIINKDGVQEADRPEEGFYIRSGIIIILEKATIRDGTVI | 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 biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.7.7.27
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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 biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.7.7.27
|
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 biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.7.7.27
|
P55230 | MESCFPAMKLNQCTFGLNNEIVSERVSAFWGTQVVKPNHLRTTKLRSAPQKKIQTNLIRSVLTPFVDQESHEPLLRTQNADPKNVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNGVNFGDGFVEVLAATQTSGDAGKKWFQGTADAVRQFIWVFEDAKTKNVEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPMDESRASDFGLLKIDQSGKIIQFSEKPKGDDLKAMQVDTSILGLPPKEAAESPYIASMGVYVFRKEVLLKLLRSSYPTSNDFGSEIIPLAVGEHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQFYDQKTPFFTSPRFLPPTKVDKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGADFYQTEAEIASLLAEGKVPVGVGQNTKIKNCIIDKNAKIGKNVVIANADGVEEGDRPEEGFHIRSGITVVLKNATIRDGLHI | 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 biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.7.7.27
|
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 biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.7.7.27
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Q7G065 | MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHHTYLGGGINFTDGSVQVLAATQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHLQDFGSEILPRAVLEHNVKACVFTEYWEDIGTIKSFFDANLALTEQPPKFEFYDPKTPFFTSPRYLPPARLEKCKIKDAIISDGCSFSECTIEHSVIGISSRVSIGCELKDTMMMGADQYETEEETSKLLFEGKVPIGIGENTKIRNCIIDMNARIGRNVIIANTQGVQESDHPEEGYYIRSGIVVILKNATIKDGTVI | 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 enzyme .
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Mass (Da): 57575
Sequence Length: 518
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.7.7.27
|
P12299 | MSSMQFSSVLPLEGKACISPVRREGSASERLKVGDSSSIRHERASRRMCNGGRGPAATGAQCVLTSDASPADTLVLRTSFRRNYADPNEVAAVILGGGTGTQLFPLTSTRATPAVPIGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHRTYLGGGINFTDGSVEVLAATQMPGEAAGWFRGTADAVRKFIWVLEDYYKNKSIEHILILSGDQLYRMDYMELVQKHVDDNADITLSCAPVGESRASEYGLVKFDSSGRVVQFSEKPKGDDLEAMKVDTSFLNFAIDDPAKYPYIASMGVYVFKRDVLLNLLKSRYAELHDFGSEILPRALHDHNVQAYVFTDYWEDIGTIRSFFDANMALCEQPPKFEFYDPKTPFFTSPRYLPPTKSDKCRIKEAIISHGCFLRECKIEHSIIGVRSRLNSGSELKNAMMMGADSYETEDEISRLMSEGKVPIGVGENTKISNCIIDMNARIGRDVVISNKEGVQEADRPEEGYYIRSGIVVIQKNATIKDGTVV | 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 biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.7.7.27
|
P12300 | RASPPSESRAPLRAPQRSATRQHQARQGPRRMCNGGRGPPYWTAGVTSAPARQTPLFSGRPSGGLSDPNEVAAVILGGGTGTQLFPLTSTRATPAVPIGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHRTYLGGGINFTDGSVEVLAATQMPGEAAGWFRGTADAWRKIIWVLEDYYKNKSIEHILILSGDQLYRMDYMELVQKHVDDNADITLSCAPVGESRASEYGLVKFDSSGRVVQFSEQPKGDDLEAMKVDTSFLNFAIDDPAKYPYIASMGVYVFKRDVLLNLLKSRYAELHDFGSEILPRALHDHNVQAYVFTDYWEDIGTIRSFFDANRALCEQPPKFEFYDPKTPFFTSPRYLPPTKSDKCRIKEAIILHGCFLRECKIEHTAFSRLNSGSELKNAMMMGADSYETEDEMSRLMSEGKVPIGVGENTKISNCIIDMNARIGRDVVISNKEGVQEADRPEEGYYIRSGIVVIQKNATIKDGTVV | 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 biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.7.7.27
|
Q0D7I3 | MATCSWAATTAAAAPPRPPARCRSRVAALRRTAAASAAAASCVLAEAPKGLKVEQADAVEPAAAAAARRDVGPDTVASIILGGGAGTRLFPLTRTRAKPAVPVGGCYRLIDIPMSNCINSKINKIYVLTQFNSQSLNRHIARTYNIGEGVGFGDGFVEVLAATQTTGESGKRWFQGTADAVRQFLWLFEDARLKRIENILILSGDHLYRMDYMDFVQKHVDKGADISVACVPVDESRASDFGLMKTDKNGRITDFLEKPKDESLKSMQLDMGTFGLRPEVADTCKYMASMGIYVFRTDILLRLLRGHYPTANDFGSEVIPMAAKDYNVQAYLFDGYWEDIGTIKSFFEANLALTDQSPNFYFYDPVKPIFTSPRFLPPTKVENCKVLNSIVSHGCFLTECSVDRSVIGVRSRLEPGVQLKDTMMMGADYYQTEAERFSELSDGKVPVGVGENTIIRNCIIDKNARIGKNVMIMNSQNVQEAERPLEGFYIRSGITVVLKNAVIPDGTVI | 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
Sequence Mass (Da): 55829
Sequence Length: 509
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.7.7.27
|
A0R2E2 | MRVAMMTREYPPEVYGGAGVHVTELVAQLRKLCDVDVHCMGAPRDGAYVAHPDPTLRGANAALTMLSADLNMVNNAEAATVVHSHTWYTGLAGHLASLLYGVPHVLTAHSLEPLRPWKAEQLGGGYQVSSWVERTAVEAADAVIAVSSGMRDDVLRTYPALDPDRVHVVRNGIDTTVWYPAEPGPDESVLAELGVDLNRPIVAFVGRITRQKGVAHLVAAAHRFAPDVQLVLCAGAPDTPQIAEEVSSAVQQLAQARTGVFWVREMLPTHKIREILSAATVFVCPSVYEPLGIVNLEAMACATAVVASDVGGIPEVVADGRTGLLVHYDANDTEAYEARLAEAVNSLVADPDRAREYGVAGRERCIEEFSWAHIAEQTLEIYRKVSA | 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-alpha-D-glucose + alpha-D-glucose 1-phosphate = ADP + alpha-maltose 1-phosphate + H(+)
Sequence Mass (Da): 41679
Sequence Length: 387
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.342
|
P35409 | MEDRGICPRVLQVLFLVVLILISPVYAAKNDACTKCSCNPKGMVSCFELQEFPPLATFPRNTTTLHVSFSGEISIPSDILQHLEKLKYLTLNNNKIKNIAKFRVKNGYSSLITLSYTHNIIETIENGAFDDLQQLTQLDLSNNRLKEFPIFNKTSSVTKLYLRGNPGITKLPRQSLGNLPSLENLFMERTGIQEIPAGIFRQNTRLINLYFNKTKALERINEDAFDEDSSLKTLVLDETSVTSLPSRGLKNLHFLSLKDVPNFWQLPELDSIREVYLSPYNGFLCCEFESGEKYGKDCTMQKPSTEENNGQTTASSPTKEPATSGLGGGTHLSTQPHTTSGFGGGGFPGGGGGFPGGGGFPAGGSKTSTQPHTTSGFGGGGFPGGGGGFPGGGGFPAGGSKTSTQPHTTSGFGGGGFPGGGGGFPGGGGFPGGSNTSTQPHTTSNSGGGGFPGGGGFPGGGTPFTNQFTIPHIPNVHQSTADPPTLIPHSNHTPNGTQFHQCSKIPVQCVPKSDAFHPCEDIMGYVWLTVVSFMVGAVALVANLVVALVLLTSQRRLNVTRFLMCNLAFADFILGLYIFILTSVSAVTRGDYHNYVQQWQNGAGCKILGFLAVFSSELSLFTLVMMTIERFYAIVHAMHMNARLSFRKTVRFMIGGWIFALVMAVVPLTGVSGYSKVAICLPFDVSDATSTAYVAFLLLVNGASFISVMYLYSRMLYVVVSGGDMEGAPKRNDSKVAKRMAILVFTDMLCWAPIAFFGLLAAFGQTLLTVTQSKILLVFFFPINSICNPFLYAFFTKAFKRELFTALSRIGFCKFRALKYNGTLSSFLYSRSRRHHSTVNAEHSTPKSKHASTMSLRQSHQDLYRKESKTAESLNGICNAGFNAHEETRTSPGSVRYVRSLRGVTKSSSPPHLKLQKQKILQSPS | Function: Probable receptor for a glycoprotein hormone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100060
Sequence Length: 925
Subcellular Location: Cell membrane
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A0JZ25 | MSRLFGTDGVRGLANGLLTAELAMQLAQAAAVVLGHERSTNGARPRAVVARDPRASGEFISAAVSAGLSSSGIDVYDAGVLPTPAAAYLVADLHADFGVMISASHNPAPDNGIKFFAKGGQKLPDEVEDAIEAQMAKDPVRPTGSDVGRIQTFSDAEDRYIVHLLGTLPHRLDGLKVVLDCAHGAASGCSPQLFNDAGAEIVVIGAEPDGLNINDGVGSTHLGALQRAVVEHGADLGIAHDGDADRCLAIDHEGNEVDGDQIMAILALALKESGKLKDNVLVATVMSNLGLKIALRNAGISIRETAVGDRYVLEEMRDGGYNLGGEQSGHVIFADHATTGDGLLTGLQLAAQVALTGKSLKELATVMTKLPQLMINVKKVDKARAGTDEGVLAAVAEASAELGETGRVLLRPSGTEALVRVMVEAADMPTAERICKHLAAVVEERLAVAPAV | 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 | MAKYFGTDGIRGEVGKSVIKAEFMQKLGNAVGTLINDNGYPGFVIIGQDTRSSGKFLKFALVSGLNAAGIDVIDLGVVPTPIVAFMTVKYKAAAGFVITASHNKFTDNGVKLFSSSGFKLDDALEEEVEAKIDSDFIYQTECKFGNYKVAENFIDEYIENLFERFGSLVNYKGKVVIDCANGAASNHFEALLDRFCIDYISVASNPDGLNINVDCGATCTSNIKKAVIEHNADLGISLDGDADRIIIVDENAQEIDGDGILNIIAQYSNICGGTTGIVGTQMTNMSYENHYKSNNIPFIRSKVGDRYVLEDLVKHGYKIGGESSGHVINLNFGTTGDGLSTAIQLLAIFSQSDKPVSAFKLPGELMQQTMINVPLNFKVTSDHLAKLAGDVAKAEERLGSRGRVLLRPSGTEPVLRVMVEADTKDLATKEAEYLVEKVKQKLV | 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 | MGRYFGTDGIRGEANRELTVDKALRLGYALGYYLKNNNPNEEKIKVIMGSDTRISGYMLRSALTAGLTSMGIYIDFVGVIPTPGVAYITKQKKAKAGIMISASHNPAKDNGIKIFNLEGYKLSDEIENQIEDYMDNLDKILANPLAGDKVGKFKYAEDEYFQYKNYLTQCVKGNFKDIKIVLDTANGAAYRAAKDVFLDLRAELVVINDAPNGRNINVKCGSTHPDILSKVVVGYEADLGLAYDGDADRLIAVDKFGNVIDGDKIIGILALGMKNKGTLKNNKVVTTVMSNIGFEKYLKENSIELLRANVGDRYVLEKMLAEDVVIGGEQSGHIILKDYATTGDGVLSSLKLVEVIRDTGKDLHELVSSIKDAPQTLINVKVDNIKKNTWDKNEIIMSFINEANKKYKDEVRILVRKSGTEPLIRVMTEGDDKQLVHKLAEDIAHLIEKELN | 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
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Q74C70 | MKKLFGTDGVRGVANVYPMTTEMAMQIGRAAAYLFKDGNRRHRIVIGKDTRLSGYMLENALVAGICSMGVDVLVVGPLPTPGIANITSSMRADAGVVISASHNPFQDNGIKFFSRDGFKLPDEMELKIEDLIFSGKIDSLRPVATEVGKAYRIDDAVGRYVVFLKNSFPKDLDLAGMKIVLDCANGAAYKVAPAVLEELGAEVIPYGVKPNGTNINAGCGSLYPQVISEAVKEHRADLGIALDGDADRVIFVDEFGNEVDGDHIMAICATQMLKQKKLRKNTLVATVMSNMGLDIAVKRAGGKVVKTAVGDRYVVEEMIKGGYNLGGEQSGHMIFLDPNTTGDGVLSALQVLATMRRADKSLSELAEVMIPLPQVLVNVRVKEKKDITTIPEVALLIGDIEKKLGDEGRILIRYSGTEPLLRIMLEGQDKYQITGWAKEIADLVEKKIGGK | 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
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Q8EHM0 | MSERKFFGTDGIRGKVGSGQMTPELALKLGWAAGRVLSRSGTKKVIIGKDTRISGYMFESALEAGLSAAGLNVMLMGPMPTPAVAYLTRTFRAEAGVVISASHNPYYDNGIKFFSTDGSKLDDNLELEIEAELEKPLVCVESHLLGKVSRIEDARGRYIEYCKGNFPADQTLTGLKIVVDCAHGATYHIAPAVFRELGAEVIAIGDKPNGVNINDKVGATSMAKICETVLAETADLGIALDGDGDRIMMVNSKGEVIDGDQILYILACDAKARGVLRGGVVGTLMSNLGLDLALQALDIPFARSKVGDRYVMELLKELDWRIGGENSGHILNLDHGTTGDGIVAGILVLAAMRRQNATLEQLTAPMEMLPQVLVNVRFEGEHDPLSSDKVKAAQAQVESELGVRGRVLLRKSGTEPLIRVMVEGDDHNTVLAHANLIADAVKSAS | 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
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O84823 | MCGIFGYLGEKNAVPLVLEGLSKLEYRGYDSAGIATLVEGRLFVEKAVGPVSQLCSAVSSDIHSQAAIGHTRWATHGEPSRFNAHPHVDMDASCALVHNGIIENFQKLKEELEEQGVVFSSDTDTEVIVQLFARRYKETRDLIQSFSWTLKRLQGSFACALMHQDHPEVLLCAAHESPLILGLGEDEVFISSDIHAFLKYSGCTQTLASGELAVLRIGKSIETYNFELARIQKEVRCIDHTEDSLDKKGFDYYMLKELYEQPEVFERILHLTCEENGFTESFLKGFSLDEIQSLHIVACGSSYHAGYLAKYVIESIASIPVYVETASEFRYRQPYIAEHSLAILISQSGETADTLAALNEFRKLSKARVLGICNVRESALASRVDHCLFIEAGLEVGVASTKAFTAQLLLLILLGLRLANHRQVIAQEDLAQAIQGLKDLPNLTRLFLDSSIHDWRCRQIEETSFIFLGRRFMYPICMEAALKLKEIAYVEANAYPAGEMKHGPIALIREGTPVIVYCGDRSVYTKTIGAIMEVKARKAYVIALAPESNRDIAAVSDEQIYIPDSHDLAAPILFTIAGQIMAYTMALQRGTEVDRPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q97MN6 | MCGIVGYSGKKEASSILVEGLSKLEYRGYDSAGVAILNDGKINVSKCKGRLVNLENKLEENPIAGNIGIGHTRWATHGEPSDLNAHPHSNKDNTISVVHNGIIENYMQLRTWLKSKGYEFKSETDTEVIPNLVDYFYEGNLLDAVIKAISKVEGSYALGIVSSKEPDKVVAVRKDSPLIVGISEDGNFIASDVPAILNHTRDIYYIKDKEFVVLTSEGVEFYSNEGEKIEKELNHIEWDANAAEKGGYEHFMLKEIYEQPKAIRDTMTSRIIAGQPIKLDDISITKEQIENIDKIYIVACGTAYHAGVVGKYVIEKFARIPVEVDIASEFRYRDPIITKNTLMIVLSQSGETADTLAALREAKSIGARVIAVTNVVGSSVARAADDILYTWAGPEIAVASTKAYTTQLITMYILGLFFAQNKNTLTNEEIEKIKADMLTLPEKAEEVLASKEKVQKFAANTYMHKDMFYLGRGIDYAVAMEGALKLKEISYIHAEAYAGGELKHGTIALIEEGTVVVALGTQSDIYDKMVSNIKEVTTRGAKVLGIAAEGRKGMEEVVDSVIYVPEVNDMLLPVLSVMQLQLLAYYVSVEKGCDVDKPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q8XHZ7 | MCGIVGYVGQKKATDILVEGLSKLEYRGYDSAGVAVLEDNKIKAEKHKGRLANLEGMLNENPIEGGIGIGHTRWATHGEPSDVNSHPHLNNKETIAVVHNGIIENYNELRNWLMEKGYEFKSETDTEVIPNLVDFYYKGDLLDAVMEATKHMEGSYAIGVICNDEPEKLVAVRKDSPLIVGLGEKEYFIASDIPAVLNHTREVYLLEDKEFVVLTNDGVTLFDEEKNPVEKEVYHITWNVDAAEKGGYEDFMLKEINEQPKAIKDTMTSRIMEEKEVTLDDISITKEYLDNVDRVYIVACGTAYHAGVIGKYAIEKLVRIPVEVDIASEFRYRDAVITDKTLIIVLSQSGETADTLAVLRDGQAKGARVLAVTNVVGSSVSREANDVLYTWAGPEIAVASTKAYVTQLIAMYTLALHFAELKGSKSVEEIEEIKKAMLELPEKVEEILKNTDLIKEFAVKASTEKDLYFLGRGMDYGVAMEGSLKLKEISYIHSEAYAGGELKHGPIALIEKDIPVISLLTQRELMDKMISNVQEVVTRGANVLGVCFKGDMEESKRKMFEGLIEIPETLSLLSPVLSVVPLQLFSYYVAKAKGFDVDKPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q8NND3 | MCGIVGYIGQAGDSRDYFALDVVVEGLRRLEYRGYDSAGIAIHANGEISYRKKAGKVAALDAEIAKAPLPDSILGIGHTRWATHGGPTDVNAHPHVVSNGKLAVVHNGIIENFAELRSELSAKGYNFVSDTDTEVAASLLAEIYNTQANGDLTLAMQLTGQRLEGAFTLLAIHADHDDRIVAARRNSPLVIGVGEGENFLGSDVSGFIDYTRKAVELANDQVVTITADDYAITNFDGSEAVGKPFDVEWDAAAAEKGGFGSFMEKEIHDQPAAVRDTLMGRLDEDGKLVLDELRIDEAILRSVDKIVIVACGTAAYAGQVARYAIEHWCRIPTEVELAHEFRYRDPILNEKTLVVALSQSGETMDTLMAVRHAREQGAKVVAICNTVGSTLPREADASLYTYAGPEIAVASTKAFLAQITASYLLGLYLAQLRGNKFADEVSSILDSLREMPEKIQQVIDAEEQIKKLGQDMADAKSVLFLGRHVGFPVALEGALKLKEIAYLHAEGFAAGELKHGPIALVEEGQPIFVIVPSPRGRDSLHSKVVSNIQEIRARGAVTIVIAEEGDEAVNDYANFIIRIPQAPTLMQPLLSTVPLQIFACAVATAKGYNVDQPRNLAKSVTVE | 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
EC: 2.6.1.16
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O19908 | MCGIIGYVGEGSCRDVLINGLDKLSYRGYDSAGIAFIKNSKINVVRSKGRIEKLKEKINDNFQKFEIGNIGIGHTRWATHGEPTEINAHPHLDAEGQFAVVQNGVIENYVQLKNYLTVNGTYFLSDTDAEVIPHLIAYKQKHLKLQIVEAILCALSELKGNFSTVIIARDMPDSIFVYQNKTALTLGKGSNFYSVSSDPIALIPYTKNFIQLHDRELGIISISQLAIYNKGKFTYPSRRFKANLNDLITNKASFDSYTLKEIHDQKKVLRNLIISTLQSEKSIDESGQLHLEYKKIKNFQIIACGSSFNAALVGKVILEKLIRIPVHVYYGSEFKTNLPPLLPCTLTIAVSQSGETGDMLSAIEIEKSRRKFQNTVYKPYLLSITNKNYSSITKKTAQSIDLKAGIEIGVAATKTFTAQTLSFYLLALKLAEHKFTLRKKEINKHLDEIRNLPKAIAHLLIKDESSIKWLSKQLKEISKCFYIGKGLNLGSALEGALKLKEISYIHCDGYAAGEIKHGPIALVENNTLIITITDPEQSQESTFASSQEAKARGAVLLAITHIEDSSIYQTFDFIIKIPKISQICASITSSVSLQLFAYYMAYYKGNDIDKPRNLAKSVTVE | 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: 2.6.1.16
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P17169 | MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q5NHQ9 | MCGIVGANSTRNVTNILIEGLKKLEYRGYDSAGLAIIDDKNNIDICKEVGKVIELEKSVHNLANFKGDIGIAHTRWATHGKPSKNNSHPHASESFCIVHNGVIENFAELKKVLINDGYKFKSDTDTEVIAHLLQKEWRDNFSIVDNIKYIMAMLKGAYAVAIISQKFSDKIVAVRSGSPLVIGVGIDENFISSDALSLLPVTNKFSYLDEGDIAIISKDNVEVFDNNGAAKNLEVEEYNYSSSSASKDGYKHYMLKEIYEQPEAVSNTILASLADGEISLDSFDKRAKELFEKTKHICIVACGTSYNAGMTAKYWIEKYAKVPCSVEIASEIRYRDNVVVDGSLFVSISQSGETADTLESLRKSKKQNYVGSMCICNVPNSSLVRESDIAFMTKAGVEIGVASTKAFTTQLVALAIFTLVIAKLKNSLTDQQIAKYTEELKNIRALVMGALKLDTEIDQISEYFSDKEHTIFLGRGLYYPIAIEGALKLKEISYIHAEAYPSGELKHGPLALVDKNMPIVAVVPNDELLDKTLSNLQEVHARGGKLILFVDKAVKERVNFDNSIVLELDAGHDFSAPVVFTIPLQLLSYHVAIIKGTDVDQPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q8RG65 | MCGIIGYSGSKANAVEVLLEGLEKVEYRGYDSAGIAFVTDSGIQIEKKEGKLENLKNHMKNFEVLSCTGIGHTRWATHGIPTDRNAHPHYSESKDVALIHNGIIENYVEIKKELLEQGVKFSSDTDTEVVAQLFSKLYDGDLYSTLKKVLKRIRGTYAFAIIHKDFPDKMICCRNHSPLIVGLGEHQNFIASDVSAILKYTRDIIYLEDGDVVLVTKDNVTVYDKDEKEVKREVKKVEWNFEQASKGGYAHFMIKEIEEQPEIIEKTLNVYTDKEKNVKFDEQLEGINFHDIDRIYIVACGTAYYAGLQGQYFMKKLLGIDVFTDIASEFRYNDPVITNKTLAIFVSQSGETIDTLMSMKYAKEKGARTLAISNVLGSTITREADNVIYTLAGPEISVASTKAYSSQVLVMYLLSLYMGAKLGKIEEKDYQKYISDISLLKENVVKLISEKEKIHDIAKKIKDIKNGFYLGRGIDEKVAREGSLKMKEINYIHTEALPAGELKHGSIALIEKGVLVVAISTNLEMDEKVVSNIKEVKARGAYVVGACKEGSLVPEVVDDVIQVKDSGELLTPVLTVVGLQYLAYYTSLEKGYDVDKPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q5L3P0 | MCGIVGYIGYQDVKEILLRGLEKLEYRGYDSAGIAVLNESGVHVFKEKGRIADLRRIVDPNVNATVGIGHTRWATHGAPSRVNAHPHQSASGRFTLVHNGVIENYEMVKRDYLADVAFQSDTDTEVIVQLVEKFVRDGLTTEEAFRKTLSLLKGSYAIAMIDAQDENTIYAAKNKSPLLVGLGDGFNVVASDAMAMLQVTNQFVELMDGELVIVTSENVTIQTLNGETVKRKPFTAELDASDIEKGTYPHYMLKEIDEQPFVIRRIIQKYQDDNGELAIDKAIINEVLNADRLYIVACGTSYHAGLVGKQLIESWAKIPVEVHIASEFSYNMPLLSEKPLFIFISQSGETADSRAVLVQTNKLGYKAITITNVPGSTLSREADYTLLLHAGPEIAVASTKAYTAQIAVLAILAAAAAKAKGFELDFDLTKELAIVANVMEMLCDAKEEMEKIASDYLTLTRNCFFIGRAVDYYVCLEGALKLKEISYIQAEGFAGGELKHGTIALIEDGTPVIALATQEHVNLSIRGNVKEVVARGANPCVISMRGLEGDGDRFIIPAVHPDLTPLVSVVPLQLIAYYAALHRGCDVDKPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q74GH6 | MCGIVGYIGAQEATPIILDGLKRLEYRGYDSAGICTLLEGKADKRRSEGKLINLERLIQSTPLAGRIGIGHTRWATHGPPSERNAHPHQAGSIIVVHNGIIENYLELKQRLVTSGRVFNSDTDTEVIAHLIDDKFAGTGDFERAVREALAEVRGAYALCILCEREPGVLIAAKQGSPMVVGLGEGEFFVASDIPAILSHTREMVFMEDGEIVVFRDGHPTFSTVAGAPLDKKSRHIDWSPLMAEKGGYKHFMLKEIFEQPRAVQDTITGRLLEEQGDVRLEEMKLADEQLRGIGRICIVACGTSWHSALVGKFLMEEHCRIPVEVDIASEFRYRNPVIDSKTLLLVISQSGETADTLAALREAKARGAMTAAICNVVDSSIAREAHGVLYTHAGPEIGVASTKAFVTQLVALYLFTIRLGRAVGTIDCEQGRTMIGGLLKVPALLEQALETNEQVERIARRYMNARDFLYLGRGMNYPIALEGALKLKEISYIHAEGYPAGEMKHGPIALIDENMPVVVLVPKNSTYEKVLSNMEEVIARGGRVIAICSAGDEAIAKKAEVTLEVPTDGEELAPIILSVPLQLLAYHVAVLKGTDVDQPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q7NIG8 | MCGIVGYIGGRTALPFLVDGLKRLEYRGYDSAGIATVGESGLELVRAKGKLHNLEEKLNGVAQSTGTVGIGHTRWATHGKPEEHNAHPHTDASGRLAVIQNGIIENYAELRLGLKERGCLFKSETDTEVIPHLIACRLAGHSLLEAVLAAVVELKGAFAIAVVSADFPDELIVVRQQAPLVIGFGEGENYFASDVPAIVSHTTRVLTLQDGECARLTRDEVQIHDFSGARLRRTPRSLNWNPSLVEKRGFRHFMLKEIHEQPGVIRDTLEDRIGDATGPIRLGLSSDLFADLERIYIIACGTSWHASLVGKYLIEELAGIPTEVNYASEFRYCPPPLNARTLVIGVSQSGETGDTNAALTAAKARGVRLLGITNRPESSLGALVGELIDTRAGMEIGVAATKTFTAQLVAFYLLALHLAHLRGTQSGERIREILVGLQQLPAQIEGILDTQERYITELAREFDATRDFIFIGRGLNYPIALEGALKLKEISYIHAEGYPAGEMKHGPIALLDSEVPVVAIAVPGKVYEKTLSNAQEAKARDARLIGVAPLDEPAAVETFDQILPVPVVDEILSPILTVVPLQLLAYHIAARRGLDVDQPRNLAKSVTVE | 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
EC: 2.6.1.16
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P44708 | MCGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINKQNELQRIRCLGKVKALDEAVSEKPLIGGTGIAHTRWATHGEPSETNAHPHSSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRTTDSLLDAVKKAVKQLTGAYGMVVMDSRHPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRTVDIYDTHGNKAKREIHESNLENDAAEKGKFRHFMQKEIYEQPTALINTMEGRINHENVIVDSIGNGAKGILEKVEHIQIVACGTSYNAGMVARYWFESLAGVSCDVEIASEFRYRKFVTRPNSLLITLSQSGETADTLAALRLAKEKGYMAALTICNVAGSSLVRESDLAFMTRAGVEVGVASTKAFTTQLAALLMLVTALGKVKGHISVEKEREIIKAMQSLPAEIEKALAFDTEIEALAEDFAEKHHALFLGRGAFYPIAVEASLKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKVKSNIEEVRARGGQLYVFADKEAGFTPSEGMKIITMPKVNDIVAPIFYTIPMQLLSYYVALIKGTDVDQPRNLAKSVTVE | 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
EC: 2.6.1.16
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Q3AFM0 | MEGIILAAGKGTRMKSDLPKVVHEVAEKPMVLRVYEALVGAGVKRVVAVVGYRKEKVEEILRGRAVIAVQEEQLGTGHAALVAMPYVEDENVIIVPGDTPLLKASTLQALIKKHLETGAYATVLTCFLSNPYGYGRIVRDGYGKIIKIVEEKDATLEEKQIAEVNTGIYCFNTKILKEILPLLKAENAQKEYYLTDVIPLLLERGKVVETITIQDETEVYGVNDRVQLARLTKGVYRRKAEALMQEGVTIIDPETVYIGEEVVVGSDTVIYPNTYLEGKTVIGSGCRLGPNTRITDSVIGNNTEITFSVIIQARVGDEVNVGPFAYLRPGTEIANGVKIGDFVEIKKSFIGEGSKVPHLSYIGDAVVGKGVNIGAGTITCNYDGKNKWETVIEDGAFIGSNTNLVAPIKIGKNAVVGAGSTLTEDVPEKALAIARSRQVNKEDYVK | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 48381
Sequence Length: 446
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q3J3H0 | MDRATVSLIVLAAGQGTRMNSDLPKVLHPLGAAPMLHHALRAGQSLEPERVVVVAGHGAEAVAKAARAFDESIEVVVQAEQLGTAHAVAQAAPLLADAPGEAVVLYGDTPFIRPETLERMLDLRSRHAVVVLGFEATDPGRYGRLVTRGEELDRIVEWKDATDEERTISLCNSGVICAEAGLLLALVSEVGNANAAGEYYLTDVVALARVRGLSAGVAICDEAETLGVNTRAQLAEAEAEFQKRARAAALEDGVTLTAPDTVFFALDTFLGRDAIVGPNVVFGPGVTVESGAEIRAFCHLEGCHISRGATVGPFARLRPGAELAEDVHVGNFVEIKNAVLDEGVKVGHLTYLGDAHVGEHTNIGAGTVTCNYDGVMKHRTEIGAHAFIGSDTMLVAPVTVGARAMTASGSVITENVPAEALALGRARQVTKPGMATRLMEMFRAAKAAKKKEAP | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 47650
Sequence Length: 454
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q1QSD2 | MTLDVVILAAGQGTRMRSAKPKVLHALAGKPLVSHVLDTAEQLGATRTHVVIGHGAEQVETELDGRDVRFALQAEQKGTGHAVAQTLDELGDGKVLILYGDVPLIRAETLTALLDEVDERRLGLLTVTLDDPGGYGRIVRDAEGRVTRIVEHKDASEAERGITECNTGIVAATGTQLKRWLPQLSAENAQGEYYLTDIFAMAAAEGIEVATASPASALEVEGVNNRSQMAALERAYQRDRAERLLTEGVALADPARFDVRGRLQCGHDVFIDVGCVFEGDVTLGDGVSVGPYTLIRDSHVAAGTVIEAHSIIEGAEVAEQAHIGPFARLRPGTRLARQSKVGNFVETKNAEVGEGSKINHLSYVGDASLGGGVNIGAGTITCNYDGANKHRTEIGDDVFVGSNTALVAPVALGAGATIGAGSTISRDVEAGALAVARTRQTTRAGWKRPRKSS | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 47732
Sequence Length: 453
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q8RHM3 | MKSIIMAAGKGTRMKSDLPKVVHLAHGKPMIVRIIDALNTLDVEENILILGHKREKVLEVLGNDVSYVVQEEQLGTGHAVKQAIPKIKDYDGDVLIINGDIPLIRKQTLIDFYNLYKNENADGIILSAIFENPFSYGRVIKDGNKVLRIVEEKEANEEQKKVKEINAGVYIFKAQALVKALEKINNNNEKGEYYITDVIEILSNDKKVISYSLEDSMEIQGVNSKVELALVSKVLRERKNTALMEDGVILIDPATTYIDDEVKIGRDTTIYPNVTLQGNTEIGENSEILSGTRIIDSKIYDNVRIESSVIEESIVENGVTIGPYAHLRPKSHLKENVHIGNFVETKKSTLEKGVKAGHLTYLGDAHIGEKTNIGAGTITCNYDGKNKFKTEIGKDVFIGSDTMLVAPVNIGDNSLIGAGSVITKDVPSDSLSVERSKQIIKEGWKK | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 49315
Sequence Length: 446
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q74GH5 | MDNLAAIILAAGKGTRMKSGIVKVMHPLAGAPMVAWPVAVARQAGAGRIVAVVGHQAERLREHFSNDADITLAVQEEQLGTGHAVACAAGDLSGFSGKVLILCGDVPLIRTETLRAMVTAHEATGAVLTVLTARQENPHGYGRIIRGFDGRVIRIVEEKDATPDERSRTEVNAGIYCAEASFLFDAVKRIGNDNAQGEYYLTDIITMANDRGLRCTAHPVADPVEVMGINDRVQLAEAARHARRRIAEEHMLNGVTLVDPAATYIDQGVVIGADTTIQPGVQIAGGCRVGEGCTIEAGAIIKGSELGDRCVVESRAVIRGCRLGSDVVIKAGTVMEDSTVMDHAAIGPMAHLRPGSELGAHVKIGNFVETKKIVMGEGSKASHLTYLGDATIGRNVNVGCGTITCNYDGVNKHRTVIGDDVFVGSDVQFVAPVTIGSNTLIAAGTTVTRDVPADSLAIARTPQINKEGWKLRKRDQ | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 50314
Sequence Length: 476
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q5FUY6 | MTDSTHRTTAIILAAGLGTRMKSRLPKALHRLGNQPMINHLITTARQVFDDVVVVTGPDMPELEKAVRPFKTVTQVERLGTAHAANTARDLFGTGDVAILYADNPLITAETMRRLLAARREGASLALLGMRPAEPGRYGRIVEDHGRVVKIVEFKDATEDERRITLCNAGVMCAGVDDFRTWLANVGNDNAQGEYYLTDVVEMAAKAGPVVCVEAPEAELAGVNSRSELARAEATLQTRLRNAAMDAGVTLVAPETVFFSTDTVIEADVTIEPNVFFGPGVKVRSGALIRAFSHLEGCEVGENAMIGPYARLRPGTLCAAQTHVGNFVELKNVELGEGAKANHLTYLGDASIGSGTNVGAGTITCNYDGVFKHRTTIGERVFVGSDSILVAPVTVGDDALIAAGSVITSDVPPGDLALGRARQTLKSGQGLQIKQSLKARKEQG | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 47242
Sequence Length: 444
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q92PS3 | MERTCLAIILAAGESTRMKSAMSKVLHPVAGRPMIAHVVDALASASISDVALVVGRDADAVSAAAATDEVAVTSFLQKERLGTAHAVLAAREAIAKGYDDVLVVFGDTPLITAAPLKAARDGLAAGNDVVVIGFQATDPTGYGRLIVKDGALVAIREHRDASDEERRITYCNGGLMAIDGRKALDLLNRIGNANAKGEYYLTDLVEIARSLDGRAIAVEAPEEELTGCNTRAELAYIERLWQQRRRHELMLAGVSMIAPETVFLSWDTALAQDVLLEPNVVFGPGVRVESGAVIHAFSHLEGAHVRAGATVGPFARLRPGADLGAKSKVGNFCEVKNAEIGAGAKVNHLTYIGDAFVGAGSNIGAGTITCNYDGVNKHVTRIGANAFVGSNSSLVAPVSIGDGALVASGSVITEDVPADAVAFGRARQDVKPGRAPILRERYEAEKAARKRAKAAE | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 47775
Sequence Length: 456
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q0S4N3 | MPVQTAVVVLAAGAGTRMRSKTPKVLHTLGGRTMLAHSLYAAAEVDPTHLVTVVGHDKERVGVAVSALEAELGRPIAIAVQDEQNGTGHAVECGLSALPADFRGTVLVTAADVPLLDGRTLHALVDEHHSEPTPSAVTVLTFTAPEPRGYGRIVRLPHDGEIAEIVEEADATEEQAAITEVNAGVYAFDAEFLRSALGQLNANNAQGELYLTDVVKIAREAGAPVFAAHLADSAKVAGANDRVQLSRLAAELNRRTVENWMRAGVTVVDPSTTWIDVGVTLARDVTIHPGVQLLGTTAVGEDAVIGPDTTLTDVTVGEGASVVRTHGSESTIGAGATVGPFSYLRPGTVLGASGKLGAFVETKNADIGAHTKVPHLTYVGDATIGEYSNIGASSVFVNYDGVAKSRTVVGSHVRTGSDTMFVAPVQVGDGAYTGAGTVLRFDVPPGALAVSGGKQRNIDGWVQRNRPGTAAAEAAAAAGLHHSSDLHETEKQDLKDGIEQ | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 51807
Sequence Length: 500
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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A7INP6 | MSDRSLLVVVLAAGEGTRMASRLPKVLHKVAGRTMLHHVLAATRAAGATRTAVVVGPGREDVAAEVRKIVPDAEVFEQTERLGTAHAVLAARAALENGADDVLVLYADTPLVRPETLGLLRAPLKAGAAVAALGFEPADPTGYGRLVTAGDELVAIREEKDASAAEKAIRFCNAGLMALAGAHALSILERIGNANAKGEYYLTDAVEIARADGLSAVAARADADEVAGVNSRVQLAEAEAILQRRLRLAAMAGGATLVAPETVFLSADTVLGRDVIVEPHVVFGPGVSVGDDVVIHSFCHLEGARLESGVTIGPYARLRPGTQLDSGVRIGNFVETKAAHIESGAKVNHLSYVGDAHVGADANLGAGTITCNYDGFGKYRTEIGAGAFIGVNSALVAPVTVGKGAFVGTGAVITSDVPEDALAIARSRQVVKEGWAKAFRAARSKPKG | 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-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
Sequence Mass (Da): 46230
Sequence Length: 448
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Subcellular Location: Cytoplasm
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Q56WN1 | MSLVSDLINLNLSDSTDKIIAEYIWVGGSGMDMRSKARTLPGPVTDPSQLPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRRGNNILVMCDAYTPAGEPIPTNKRHAAAKVFSNPDVAAEVPWYGIEQEYTLLQKDVKWPVGWPIGGYPGPQGPYYCGIGADKSFGRDVVDSHYKACLYAGINISGINGEVMPGQWEFQVGPAVGISAADEIWVARYILERITEIAGVVVSFDPKPIPGDWNGAGAHCNYSTKSMREEGGYEIIKKAIDKLGLRHKEHIAAYGEGNERRLTGHHETADINTFLWGVANRGASIRVGRDTEKEGKGYFEDRRPASNMDPYIVTSMIAETTILWNP | 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 Mass (Da): 39115
Sequence Length: 356
Subcellular Location: Cytoplasm
EC: 6.3.1.2
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Q470D5 | MPTNLPALPMDTTPELLLAARVRDQLKADKQALFADFDLSSHVGTLVTRLRRAVDAALAEAWRGLDMPADAALVAVGGYGRGELFPYSDVDVLLLLRAEPDADTVSRLERFIGMCWDLGLEIGSSVRTVEDCIREARADITIQTSLLEARLLTGNRKLFEALRTQHQADLDPAAFFQAKLLEMRQRHAKYQDTPYALEPNCKESPGGLRDLQVILWMTKAAGLGDSWKELFERGLLTQREAQELSRNERLLKTIRARLHLVAGRRQDVLVFDLQTALAESFGYRQNANKRASEQLMRRYFWAAKAVTQLNSVLLLNIEALLFPSESQVTRVINERFVERQGMLEITSDSLYEDDPHAILETFLLYERTPGIKGLSPRTLRGLYNARTVMDARWRSDPENRRLFLAILQEPQGITHALRLMNQTSVLGRYLINFRRIVGQMQHDLFHVYTVDQHILMVVRNMRRFAIVEHTHEFPFCSQLMASFDKPWVLSVAALFHDIAKGRGGDHSKLGTVDARRFCKQHGIGREDADLICWLVEHHLTMSHVAQKQDLTDPDVVHAFARVVGDERHLTALYLLTVADVRGTSPKVWNAWKGKLLEDLYRITLRVLGGARVDPHSIWAQRQEETISQLRLKAFDPELGKPLWAQLDVAFFLRHDSRDIAWLTRHLFNKVDSPVPVVKARISPAGEGLQVAVYVKDQPDLFARICGYFERKAFSIQDAKIHTTRHGYALDTFQVTDPGLADDGGNYRDILALVEHELGDRLQQQAALPEPSQGRLSRQSRSFPIKPRVDLRPDERGQYYLLSLSANDRTGLLYAITRVLAKHRVSVHTARINTLGERVEDVFLVDGSRLAADNRLQIQLEQDLLAALEI | 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 glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 98722
Sequence Length: 869
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
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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
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
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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
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
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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
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
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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
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
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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
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
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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
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
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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
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
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S3DB78 | MVFTSPSWCQDILMPIPNNELVGEFVMRRGHGLNDVSEDSPSSVCAYTGKSYSIRDIRHNVKSLSKSLSQILGWDFNHGNPEDKVVAVCSLNSIDYVPLTWAIHRLGGICLLLHPTSSASELETLMRKANCKAVFTCKPLMAQCQAAFTAINGDPSNIFLVELPLPEEQPVKISNTTISQLIADGEGLPDLQPLDLQDFDSKERLAYFCPTSGTSGFLKIAKVSHANVMANILQCTTMDSYTTASQTDVTLGILPLSHAYGLLVQHFVTFRGDCIILHPKFDMQIALKSVQQYRIVRLYLVPTIIGALATNPILFKLFDLSSVKRVITGSASLPEQVSKAINQLCPEWEINPGYGLTESFVCMSWTSPNSQYPGSTGCLLPLVEARLLDADGSDITAHGQAGDLLVRSPSVMKEYLDDDLKRDVTFDSDGWLRTGDVATFKQNPKGDSHLFIVDRKKDIMKVKGIQVPPVEIEGHLVAHPAVDDAAVVAISDEDAGERPFAFVVRSQKVMTDIDEKSLKKDISGYIQSTLSEPYWLRQNIRFIDAIPKSHNGKALKFKLKQQLVTSSA | 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 polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
Sequence Mass (Da): 62561
Sequence Length: 568
Domain: Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.
Pathway: Mycotoxin biosynthesis.
EC: 6.2.1.-
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S3E7Q2 | MDYIKQAESTQLSSLSLSRLEGNNAEESKRLLEACAQDGFFYLDLRDHKQLLVDYEALLEIIKQYFNEPLDQKMKDDRKSDTIGYEPVATSAGVLDGLPDYYESFKVSWNQLRDHVQELPTVVETNIEVFDRFAKYVHSILLMILSRLSQTMGRNNDNRFESYHRDSIATRTNLTFLKYPKQDTTEHGVGHNKHTDVGTLTFLLSGQRGLQRLTPEGWCHVEPRSGFAVVNVGDSLRFLSDCVLSSVIHRVLPVGAHQTEDRYTLAYFLRPEDDAVFKDINGNLVSARSWHDRKFDHFRASHNQQKNDTILMGGMEENQKFLQYKFQA | 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-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
Sequence Mass (Da): 37835
Sequence Length: 328
Pathway: Mycotoxin biosynthesis.
EC: 1.14.-.-
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S3D784 | MAIQTLDYRDFQYGGQEQHRTFCHNLCETLSTWGFIKIQNTSIPDAVIDELFSYNKKFFALPEHIKQKARHPAAPNPHRGWSAVGQEQLSRIAGFEKDEETDGFVPEYRESFDQGAADDELFPNRWIDEDDLPGFRKFMENYYEMCYNFHTQLLRAISTGLSLPEDLLLSRHQTDTSELRMNHYPAIACENLKFGMRIGEHSDFGTLTLLLQDSTGGLQVEDQKKLGTFIPVESDSRYEVIVNVGDCLQRWTNRRLRSANHRVHLPEGKNFKSDEVLADRYSVAYFGKPDRNVLVDSFPEFCRGGESKYNDHMNALEYNQTKLLRTYA | 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-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
Sequence Mass (Da): 37988
Sequence Length: 328
Pathway: Mycotoxin biosynthesis.
EC: 1.14.-.-
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S3DQP8 | MTENFPLPPLLGVDWDHLGFEPLEVNGHVECTFSTTTSCWTEPVFVTNPYLPVHGLAPGLNYGQQIFEGMKAFRNPSGDVQLFRPDQNALRFARSALRVAIPPVPTDLFLRAVNTAVGMNTDFVPPHGTGASLYIRPMAFASSPTVGLFLASQFKFCVYVLPVSPLHGKATQEGASVLVIEDFDRAAPLGTGNVKVGGNYGPVLGLIDEAKKQGFNLTLHLDSLSHSLIDEFSTSGFIGVLNDGEVPTIVVSDSQQVVSSITVDSICELARAFDWHVQKRPISFLEVARFSEVYAAGTAAVLVPVESILRRSTGEHVVYSVEYSSPTSCFSRLSTALRDIQQGLVPDDRSWIKLVTKP | 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 synthesized by the reducing polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 38895
Sequence Length: 358
Pathway: Mycotoxin biosynthesis.
EC: 2.6.1.42
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S3E7P8 | MPKPTISYSLNGLPAAAVDSIGSLLEILARIRGIVLTEQSNDETASIIISAPDVHRLVVGSDDSHYDSTTLYIEDFLNRLCEALDAVGKKAEAGAFRHALQLYHTDRELGALKHGESVTNRQLKNDSFEDLEFLVEAWLVALNSEESARKLPAPLPVKSPDTRAMTLAEKILAHHAFSLPSSGGLKSGELGMKHGMVSIGELPSVWRNDRFWLAGDHTVEPRTYDQPRVRELLNGLNDAKQEFKMTENQGSNYTILHTEFVRERAEPGMLALGSDSHTCSAGAVSCLAIGLGAADVMTALATGETWIKVPESIRIDFTGEPAWYIRGKDVILYILKELKRNTFAADRIVEFGGLGARFLSCDARFAITNMCTELGGVTGIFVPDEVTNTFVSGRPQSKYKSNSIYFQPDKDASYAATFQIDLTMVESFIALHPSPDNVVPVSEKLDMSFEGCFIGACTTTEEELVLGALVLEAGLKNGLGLAPGKRMVVPGSIPIVNSLRELGLLEIYAQTGFEQPAVGCSLCLGMGADRAGEGENWISSQNRNFKNRMGKGSTGHICSAATVAASSFSMRLTNPAALLAQVSPDRYKALLESCQSYKNRVRKVKSSKKESVKRSVSVMPSYVEPYLHFRSPLTEKHTQMHAPSGGEGEQCGNLDIIESKIYALGDFVDTDAVSRDLFLHLSDVSGETMTSGVLTMLEIIPAAFILESPTDTLLGSHALEFTNPDFRDKVRQGMRVVVAGKAFGCGSSREEAPRALKGLGVQCVIAKSFSFIYGRNQPSIGLLGINIADDRFYELAKTGAGIKIDVPGRVVRLEGQNFPFVLDDMELSLIKNNGLATAYKKYGKNVFALLCNTKSSLRPSELAELQLKGVSDGMQTSLEW | 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 . The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 95683
Sequence Length: 880
Pathway: Mycotoxin biosynthesis.
EC: 4.2.1.33
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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
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C4ZGB4 | MAKYIMALDAGTTSNRCILFNEKGEMCSVAQKEFTQFFPKPGWVEHDAEEIWATQLEVAKEAMANIQATAADICAIGITNQRETTIVWDKNTGEPVYHAIVWQCRRTAEYADSLKEKGLTETFRKKTGLVIDAYFSATKLKWLLDNVPGARERAERGELLFGTVETWLIWKLTQGQVHVTDYSNASRTMMFNINTLKWDDEILKELDIPKSMLPKPMPSSCVYGEVNPVYFGGPIPIAGAAGDQQAALFGQTCFRAGEAKNTYGTGCFLLMNTGEMPVSSKNGLVTTIAWGIDGKVVYALEGSIFVAGASIQWLRDEMKFIDSSTDSEYMARKVKDTNGCYVVPAFTGLGAPYWDQYARGTIVGLTRGVNKYHVIRATLESMAFQVNDVLEAMKADSGINLTSLKVDGGASANNLLMQMQADISNAPVNRPVCVETTAMGAAYLAGLAVGYWDSMDDIKRNWAIDRVFEPEIADDMREKKRKMWKKAVACAFNWAKDD | 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 via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
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Q0VRN6 | MPYILSIDQGTTSSRAIVFDANGHACGQAQKEFRQYFPEDGWVEHDAMEIWNDTLAMCQQALRNARVEAQQLVAIGITNQRETTVLWDRETGDPLARAIVWQDRRTASTCEALRDQGHENQVRSKTGLLLDPYFSATKLAWLLDNVPNARQRAEAGELAFGTIDSWLLWQLTRGKVHATDATNASRTLLFNIHEQCWDEELLTLFNVPASVLPDVRDSAADFGTTCPELLGAAVPVTGIAGDQQAALVGQACFAPGMVKSTYGTGCFMVMNTGEAVESHNRLLTTVGYRLNGKTTYALEGSIFVAGAAIQWLRDGLHLIRDARETEALARRVGSAGGVYLVPAFTGLGAPWWDPHARGALMGLTRDTGIAEVVTAGLEAVCYQSRDLLDAMAADCGTRPTTLRVDGGMVVNNWLSQTLSDVLGVCVDRPVVTETTALGAAYLAGLGVGLYASLESIAEQWRCERGFSPALAEPERQKRYQGWRDAVARVCQTSRGAN | 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 via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
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Q8EVD0 | MDNTKKYIVSLDSGTTSCRTIIFDQNGNMVSSAQTEFTQYFPQSGWVEHDAIEIWTTQLGTLQSAKSRANIKSHNMAAIGITNQRETVVLWDKETGLPVYNAIVWQDRRTSEYCDELIKQGKANIISSKTGLIINPYFSGTKIRWILKNVPEAAQKLQEHKLLAGTIDTWLIWKLTDGKVHATDVTNASRTMLYNINTLEWDQEILDLLEIPREILPVVKSSSELYGTINPKYLSQRATAAVPIMGVAGDQQSSLFGQLCTEPGMVKNTYGTGCFTLINTGERAIFSKNKLVTTIAWKLGNQKPIYALEGSVFIAGSGIKWLRDSIKVIYNAQECDFYCGLADQEPQNVYMVPSFTGLGAPYWDSSSRGAIFGLERGTKREHIVKATIEAIAFQSNDLLSAMQKDIGKKINIMKVDGGASNSNYLMQFQSSISDVTIMRPTNIETTALGAAYLAGSASGFWKSIDELKKLNPIDKSFRPGLSKEVVNKKLKGWQEAVKRTFNWTNSI | 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 via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
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B1ZGW7 | MPDAVGAIDQGTTSTRFIVFDRRGTIRAQAQREHEQIFPRPGWVEHDPREIWRNTHAVMREGLARAGLVPGDLAAIGLTNQRETALLWDRRTGEPLHNALVWQDTRTDRTVAALARDGGRDRFRAVTGLPLASYFSASKLAWLLDHVEGARAKAEDGTALFGTIDSWLVWNLTGGPDGGLHVTDVTNASRTQLMSLATLDWDEAMLGVFRIPRAVLPEIVSSSAVLGETRDPFPGVPVGGILGDQQAALFGQTCFAPGEAKNTYGTGCFALMNTGPEPVASTAGLVTTVAYRLDGRPPAYALEGSIAITGALVQWLRDNLGLIGASSEIEGLARSVEDNGGVYVVPAFSGLYAPHWRDDARGLIIGLTRYANKGHIARACLEATAYQTREVLEAMERDSGCPLSELRCDGGMTVNDLLMQFQADILDRPTLRPKVSETTALGAAYAAGLATGFWKTLEDLRDNWAVDKRWHPHIAAEERRALFAGWGRAVERSFGWVEENA | 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 via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
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P47284 | MDLKKQYIIALDEGTSSCRSIVFDHNLNQIAIAQNEFNTFFPNSGWVEQDPLEIWSAQLATMQSAKNKAQIKSHEVIAVGITNQRETIVLWNKENGLPVYNAIVWQDQRTAALCQKFNEDKLIQTKVKQKTGLPINPYFSATKIAWILKNVPLAKKLMEQKKLLFGTIDSWLIWKLTNGKMHVTDVSNASRTLLFDIVKMEWSKELCDLFEVPVSILPKVLSSNAYFGDIETNHWSSNAKGIVPIRAVLGDQQAALFGQLCTEPGMVKNTYGTGCFVLMNIGDKPTLSKHNLLTTVAWQLENHPPVYALEGSVFVAGAAIKWLRDALKIIYSEKESDFYAELAKENEQNLVFVPAFSGLGAPWWDASARGIILGIEASTKREHIVKASLESIAFQTNDLLNAMASDLGYKITSIKADGGIVKSNYLMQFQADIADVIVSIPKNKETTAVGVCFLAGLACGFWKDIHQLEKLTTLDKKFKSTMDPNIRKTKINSWHKAVERALKWKEID | 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 via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
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