Detail Information for IndEnz0001000412
IED ID IndEnz0001000412
Enzyme Type ID amylase000412
Protein Name Cell wall alpha-1,3-glucan synthase ags1
EC 2.4.1.183
Cell wall alpha-1,4-glucan synthase
Gene Name ags1 mok1 SPCC1281.01 SPCC17A7.01 SPCC338.01c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Enzyme Sequence MHGLQGLCFRRAVIALALLLFHSVFAAPYSEDEEPWNLNQNKNASSVLEYSGEWADHDFFPSPDNWRMSFITVILDRWYDGDPSNNDIEKTPFEYDISEVSFRNGGDIVGLELSLDYLEGLGTQGIYIAGTPFVNMPWGADQYSPLDYTILDHHLGTIDQWRSTITAMHERGMYLVVDLTVATLGDLIGMVGHLNDTSGVDFNLNEYNAMWKTSEYRYVDFNFTNVYNTSCEYPRFWGEDGGPVSIQFKGCYVSDFDHYGDTEAFGSHPDWQRQLSKFASVQDRLRDWKPDVAEKLMHLSCLVISMLDVDGFRIDKATQMTADFIVDWSMYVRECAAKYNKKNFLIVGEVTGSSSYGSIYYNRGRQPDQRPPNVTAAFNYTSDESQYSLRDSDHYGFDGSAFHYSIYRALLRFLGMDSKMEIDFDVSSVLTTAWNGIQINEDAVNINTGTVEPLHMYGVANHDVFRWGAIENGTARLILGTMITSLLFPGIPLLYYGDEQGMYVLDNSANNYLYGRQAMNSARAWYIHGCYNGSATSYPTVDLSPAQRGCQDSWNYLDHFDIASAHRNVYRNIHSIRRHYLSLSEGWRFDHIANWTDDVYFPDSQPYASPMGLYSVLRGPMKEIQDFDSITNASNVSKSEVWVLYANRNDTHLWSYDCTDEDSAIIGPWKSGTTLRNLIYPYDTIELEDSWNSSWGCIPNIELDPYAFKLYVPEEDFIENDPIITSLTPEHDARVVASGNEIDLTIEFSRSMDCDSIKNALSVVSSTRPKNTTAVIDVDSSFCRNYSEDASTSLHGQTAGRFAWYGTLTNIDPGIHRISLKSVPTSDFSSRTLSTDNFLIRVGSTNNPIVHYSANYSDTLLIMQDGDLYINHSAPGAVLFRYSTDFQSHWSDWEEYNGGLTKVQASNWTGTRRQGWEGHHIHVQYWSDLGGSANHMQQSDYGFKYRRFLPHMFLEGDFNEYGYDSGVENRFLQKSDFYWEAGFISETYPAAIQLNVWGMNPDGIPDKTRVYGSQGNSTVLSRSDPASLVGNNITIYHPPPHGYLSYKILLRDDDMIYRLAPSGEWGVSIAIYVLCIVIPPLSAIVVSWAFKNSFYTVKFNKHGNNDLGKFYPLKSLVPFRKKNDLDSPAKVTPVVSGVSARKKKCVLIATLEYDITDWKIRIKIGGLGVMAQLMAQHLKHEDLVWVVPCVGDVVYPEAEEASPIEVKIIDQTYTINVYHHYLDNIKYVLLDAPVFRRQTSKEPYPARMDDLGSAIFYSAWNQCIAEVIRRNPIDIYHINDYHGALAPCYLLPDIIPCALSLHNAEFQGLWPLRTPEEKEEVCAVYNISQRVCTKYVQFGNVFNLLHAAVSYIRIHQKGFGAVGVSNKYGKRSWARYPIFWGLKKIGKLPNPDPTDTDEIVDDKAVAITDIDPDMEKSKVEHKRLAQEWAGLEVNEKYDLLVFVGRWSSQKGIDLIADIAPSLLESYKVQLICVGPIIDLYGKFAAEKLDVLQKKYPTRVFSQPKFTQLPPYIFSGADFALIPSRDEPFGLVAVEFGRKGALGIGARVGGLGQMPGWWYSVESSATPHLLKQFEQACQQALSSSQRTRARLRARSAKQRFPVSQWKAKLEALTDGCIKCSQKYGRNSRSRSSFYSLIHESFSRSSEVLPTSSDTNLDAKRAEEAEMIMIETPPTAEANTGAKLDRSLSLGSRRGPGHTTEDDASDGLDTIQEESMTAGDSTSGGSDISRYRAERLNPDSHSPSEYSFDSGDYEFDPQRSYYYDDLFDDDTTIRNAPSFRPQMGSFDAEHAVGATFSQDDLSDPARSVDSDSVSPPLPPFVAGSNPNARNNNNPYFYGNLHTESSLSLASVMSGKEKRDFSLTRVEETFTDEDGQALRSFSEKLQKLNAKNSKDDLCIEQYLMKSERSFFHERRAIKLGLQKPNKLHVNELSSHSGTEESESLSNGQTSYDDIIAMTDESNYTQLGDDDFKTIHGLKKFMLFKIYDWPIYSIFLALGQILAATAYQLTLFTGTSNIQTYEIYSVCAFFIGASFVWWFMFARLPSYYVLSIPWLFYAVALFLVGLPAFDTVAPGRVWITNVAAWIYAIASASGSIFFSLNFGEEGAVQTRIWVFRACLVQGVQQVWSAALWYWGAHLNKRLTAGEANTFKMSPAIPSITWPLSAVSILIFALLFKGLPEYYRQLSGSIPAFYKSLLRRKLVVWFCISVFLQNFWLSSLNGRSWSYLWDIGNIHQWQIFLLIVAFYIVLWALLLGVLAWISRTHSWIICVFGVGLGAPRWLQQFWATSNIGLYLPWAGYSGPYLGRTLWLWLGVLDAIQSVGIGMILLQTLTRRHVASTLMTGQIVGAVATMIGRGASPNREGPANVFIDFTKWNHGDGSSILASAPFWINIICQLAICVGYLAFFRRENLSRP
Enzyme Length 2410
Uniprot Accession Number Q9USK8
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378, ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.183;
DNA Binding
EC Number 2.4.1.183
Enzyme Function FUNCTION: Required for alpha-1,3-glucan and alpha-1,4-glucan production which are required for cell wall synthesis. {ECO:0000269|PubMed:17472966}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Modified residue (6); Mutagenesis (1); Region (2); Sequence conflict (3)
Keywords Cell wall biogenesis/degradation;Glycosyltransferase;Multifunctional enzyme;Phosphoprotein;Reference proteome;Transferase
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 1643; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517; MOD_RES 1644; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517; MOD_RES 1651; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517; MOD_RES 1653; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:18257517; MOD_RES 1738; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517; MOD_RES 1812; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12206652; 16420355; 18793338; 19547744; 20473289; 21712547; 22633491; 22891259; 23297348; 23697806; 23934882; 24763107; 25720772; 26412298; 27298342; 29996109; 30726745; 32101745; 32142608; 34296454;
Motif
Gene Encoded By
Mass 272,106
Kinetics
Metal Binding
Rhea ID RHEA:19749
Cross Reference Brenda 2.4.1.B3;