ID A0A3N6GRA7_9ACTN Unreviewed; 482 AA. AC A0A3N6GRA7; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 22-FEB-2023, entry version 13. DE RecName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00030823}; GN Name=gap3 {ECO:0000313|EMBL:RPK54909.1}; GN ORFNames=EES44_29120 {ECO:0000313|EMBL:RPK54909.1}; OS Streptomyces sp. ADI96-15. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1522761 {ECO:0000313|EMBL:RPK54909.1, ECO:0000313|Proteomes:UP000279576}; RN [1] {ECO:0000313|EMBL:RPK54909.1, ECO:0000313|Proteomes:UP000279576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ADI96-15 {ECO:0000313|EMBL:RPK54909.1, RC ECO:0000313|Proteomes:UP000279576}; RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C., RA Busche T., Kalinowski J., Zotchev S.B.; RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of RT secondary metabolite biosynthesis gene clusters and some of their RT products."; RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000256|RuleBase:RU000397}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RPK54909.1}. 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; RPGX01000352; RPK54909.1; -; Genomic_DNA. DR RefSeq; WP_023416565.1; NZ_ML123112.1. DR AlphaFoldDB; A0A3N6GRA7; -. DR EnsemblBacteria; RPK54909; RPK54909; EES44_29120. DR Proteomes; UP000279576; 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 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; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43454; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR43454:SF1; GP_DH_N DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:RPK54909.1}. FT DOMAIN 129..289 FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P) FT binding" FT /evidence="ECO:0000259|SMART:SM00846" SQ SEQUENCE 482 AA; 52713 MW; E9F607B70F43B05A CRC64; MTVNEDSFTN WKNREEIAES MIPIIGKLQR ERDVTVLLHS RSLVNKSVVS ILKTHRFARQ IAGAELSVTE TMPFLQALTT LDLGPSQIDI GMLAATYKAD DRGLSVAEFT ADAVSGATGD QKIDRRQPRD VVLYGFGRIG RLVARLLIEK AGSGNGLRLR AIVVRRGKGQ DIVKRASLLR RDSIHGQFQG TITVDEAHDK IIANGHEIQV IYSDDPAQVD YTEYGIKEAI LIDNTGRWRD REGLSNHLRP GIAKVVLTAP GKGDVPNIVH GVNHEDVKPD EQILSCASCT TNAIVPPLKA MADEYGVLRG HVETVHSFTN DQNLLDNYHA SDRRGRSAPL NMVITETGAA SAVAKALPEL KAPITGSSIR VPVPDVSIAI LSLRLGRETT REEVLDHLRE VSLTSPLKRQ IDFITAPDAV SSDFIGSRHA SIVDAGATKV DGDNAILYLW YDNEFGYSCQ VIRVVQHVSG VEYPTFPAPE AV //