ID A0A0L0T0E9_ALLMA Unreviewed; 342 AA. AC A0A0L0T0E9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-SEP-2016, entry version 10. 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 ATCC 38327. OC Eukaryota; Fungi; Blastocladiomycota; Blastocladiomycetes; OC 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., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., RA Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., RA Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Stolte C., Sykes S., Wortman J., 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., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Burger G., Gray M.W., Holland P.W.H., King N., RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., 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: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC {ECO:0000256|RuleBase:RU361160}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC {ECO:0000256|RuleBase:RU361160}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. {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 EnsemblFungi; KNE68263; KNE68263; AMAG_12934. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000054350; Unassembled WGS sequence. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. 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 Gene3D; 3.40.50.720; -; 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; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10836; PTHR10836; 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; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054350}; KW Glycolysis {ECO:0000256|RuleBase:RU361160}; KW NAD {ECO:0000256|RuleBase:RU361160}; KW Oxidoreductase {ECO:0000256|RuleBase:RU361160}; KW Reference proteome {ECO:0000313|Proteomes:UP000054350}. FT DOMAIN 3 152 Gp_dh_N. {ECO:0000259|SMART:SM00846}. FT ACT_SITE 152 152 Nucleophile. {ECO:0000256|PIRSR: FT PIRSR000149-1}. FT SITE 179 179 Activates thiol group during catalysis. FT {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 //