ID G3P_CERSP Reviewed; 333 AA. AC P29272; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 04-NOV-2026, entry version 125. 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=gapB; OS Cereibacter sphaeroides (Rhodobacter sphaeroides). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodobacterales; Paracoccaceae; Cereibacter. OX NCBI_TaxID=1063; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1939098; DOI=10.1016/s0021-9258(18)54944-9; RA Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.; RT "Identification, expression, and deduced primary structure of transketolase RT and other enzymes encoded within the form II CO2 fixation operon of RT Rhodobacter sphaeroides."; RL J. Biol. Chem. 266:20447-20452(1991). 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 + 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: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 -!- MISCELLANEOUS: This protein is encoded within the form II ribulose- CC bisphosphate carboxylase operon. {ECO:0000305|PubMed:1939098}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {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; M68914; AAA26156.1; -; Genomic_DNA. DR PIR; C41080; C41080. DR RefSeq; WP_011339168.1; NZ_BJXO01000007.1. DR AlphaFoldDB; P29272; -. DR SMR; P29272; -. DR GeneID; 48981334; -. DR OMA; AACWNIV; -. DR UniPathway; UPA00109; UER00184. 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 CDD; cd18126; GAPDH_I_C; 1. DR CDD; cd05214; GAPDH_I_N; 1. DR FunFam; 3.30.360.10:FF:000002; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000001; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 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; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 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. FT CHAIN 1..333 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_0000145675" FT ACT_SITE 151 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 36 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 80 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 150..152 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 181 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 196 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 178 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" SQ SEQUENCE 333 AA; 35679 MW; B072F443A20C3AFD CRC64; MTIRVAINGF GRIGRNVLRA IVESGRTDIE VVAINDLGQV ETNAHLLRFD SVHGRFPAKV TSGDDWIDVG RGPIKVTAIR NPAELPWAGV DMAMECTGIF TTKEKAAAHL QNGAKRVLVS APCDGADRTI VYGVNHATLT ADDLVVSNAS CTTNCLSPVA KVLHDAIGIA KGFMTTIHSY TGDQPTLDTM HKDLYRARAA ALSMIPTSTG AAKAVGLVLP ELKGRLDGVS IRVPTPNVSV VDLVFEAARD TTVEEVNAAI EAAACGPLKG VLGFTTEPNV SSDFNHDPHS SVFHMDQTKV MEGRMVRILS WYDNEWGFSN RMADTAVAMG RLL //