ID A0A0L0T0E9_ALLM3 Unreviewed; 342 AA. AC A0A0L0T0E9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 27-NOV-2024, entry version 45. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160}; DE EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160}; GN ORFNames=AMAG_12934 {ECO:0000313|EMBL:KNE68263.1}; OS Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var. OS macrogynus). OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota; OC Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces. OX NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE68263.1, ECO:0000313|Proteomes:UP000054350}; RN [1] {ECO:0000313|EMBL:KNE68263.1, ECO:0000313|Proteomes:UP000054350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE68263.1, RC ECO:0000313|Proteomes:UP000054350}; RG The Broad Institute Genome Sequencing Platform; RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N., RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "Annotation of Allomyces macrogynus ATCC 38327."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000054350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350}; RG The Broad Institute Genome Sequencing Platform; RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B., RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C., RA Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W., RA Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., RA Lander E., Nusbaum C.; RT "The Genome Sequence of Allomyces macrogynus strain ATCC 38327."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = (2R)-3- CC phospho-glyceroyl phosphate + NADH + H(+); Xref=Rhea:RHEA:10300, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; CC Evidence={ECO:0000256|RuleBase:RU361160}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869, CC ECO:0000256|RuleBase:RU361160}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881, CC ECO:0000256|RuleBase:RU361160}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG745356; KNE68263.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0L0T0E9; -. DR STRING; 578462.A0A0L0T0E9; -. DR EnsemblFungi; KNE68263; KNE68263; AMAG_12934. DR VEuPathDB; FungiDB:AMAG_12934; -. DR eggNOG; KOG0657; Eukaryota. DR OMA; TCQMIRL; -. DR OrthoDB; 275384at2759; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000054350; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR FunFam; 3.30.360.10:FF:000001; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000266; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01534; GAPDH-I; 1. DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361160}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000149-3}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU361160}; KW Reference proteome {ECO:0000313|Proteomes:UP000054350}. FT DOMAIN 3..152 FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P) FT binding" FT /evidence="ECO:0000259|SMART:SM00846" FT ACT_SITE 152 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1" FT BINDING 12..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 151..153 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 182 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 211..212 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 234 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 316 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT SITE 179 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4" SQ SEQUENCE 342 AA; 36439 MW; E2D6386A37F76BB5 CRC64; MTVKVGINGF GRIGRLVFRA SLENPDVQVV AINDPFIDLE YMTYLLRYDS THGRYKGTIA VENGKLVVNG HAITVFNSMK PTEIAWGSAG AVYVVESTGV FLSIEKASQH FQGGAKKVVV TAPSPDAPMF VMGVNQDKYD PSTMNVVSNA SCTTNCLAPL AKVINDEFGI VEGLMTTVHA TTATQKTVDG PSGKDWRSGR GAAQNIIPAS TGAAKAVGKV IPALNGKLTG MAFRVPTPDV SVVDLTVRLA KPATYDQIKA VIKQASQSSL KGILGYTEDA VVSNDFVGDS HSSIFDADAG IALNDTFVKL ISWYDNEFGY SCRVIDLVKH IAKKDAEAGL KL //