ID G3P_BUCAI Reviewed; 332 AA. AC P57384; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 27-MAR-2024, entry version 139. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2}; DE Short=GAPDH {ECO:0000250|UniProtKB:P0A9B2}; DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P0A9B2}; DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2}; GN Name=gapA; OrderedLocusNames=BU298; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3- CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor CC NAD. The first reaction step involves the formation of a hemiacetal CC intermediate between G3P and a cysteine residue, and this hemiacetal CC intermediate is then oxidized to a thioester, with concomitant CC reduction of NAD to NADH. The reduced NADH is then exchanged with the CC second NAD, and the thioester is attacked by a nucleophilic inorganic CC phosphate to produce BPG. {ECO:0000250|UniProtKB:P0A9B2}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3- CC phospho-glyceroyl phosphate + H(+) + NADH; 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:0000250|UniProtKB:P0A9B2}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9B2}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB13007.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; BA000003; BAB13007.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_240121.1; NC_002528.1. DR RefSeq; WP_009874251.1; NC_002528.1. DR AlphaFoldDB; P57384; -. DR SMR; P57384; -. DR STRING; 563178.BUAP5A_292; -. DR EnsemblBacteria; BAB13007; BAB13007; BAB13007. DR KEGG; buc:BU298; -. DR PATRIC; fig|107806.10.peg.309; -. DR eggNOG; COG0057; Bacteria. DR HOGENOM; CLU_030140_0_3_6; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000001806; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB. 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; 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 Cytoplasm; Glycolysis; NAD; Nucleotide-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1..332 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_0000145638" FT ACT_SITE 150 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 12..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 78 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 120 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 149..151 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 180 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 209..210 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 232 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 314 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT SITE 177 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" SQ SEQUENCE 332 AA; 36475 MW; BDA01457D9EB81E4 CRC64; MTIKVGINGF GRIGRVLFRL AQKRSDIEII AINDLLAPEY IAYMLKYDST HGVFKKHITF DKDNIIINGK NIRVTSIKDP EKLMWHDLSI DVVIESTGLF LKREQAYKHI LAGSKKVVVT GPSKDDIPMF VRGANFHKYQ GESIVSNASC TTNCLAPLSK VIDDNFGIIE GLMTTVHAST ATQKIVDGAS DKDWRGGRGA LQNIIPSSTG AAIAVGKVLP NLNGKLTGMA FRVPVSNVSV VDLTVRYKKS ATYSEICQKI QQASQKEMKG IMGYTEDEVV STDFNGEELT SIFDAKAGLS LNKNFVKLIA WYDNETGYSS KVLDLVSLVS KK //