ID G3P2_CAEBR Reviewed; 341 AA. AC P32809; A8XJE1; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 143. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000250|UniProtKB:E3VWI2}; DE Short=GAPDH-2 {ECO:0000250|UniProtKB:E3VWI2}; DE EC=1.2.1.12 {ECO:0000250|UniProtKB:E3VWI2}; GN ORFNames=CBG14137 {ECO:0000312|WormBase:CBG14137}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6238; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1446820; DOI=10.1016/0378-1119(92)90126-a; RA Lee Y.H., Huang X.Y., Hirsh D., Fox G.E., Hecht R.M.; RT "Conservation of gene organization and trans-splicing in the RT glyceraldehyde-3-phosphate dehydrogenase-encoding genes of Caenorhabditis RT briggsae."; RL Gene 121:227-235(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., RA Durbin R.M., Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative RT genomics."; RL PLoS Biol. 1:166-192(2003). 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:0000255|PROSITE-ProRule:PRU10009}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P04406}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04406}. 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; M86669; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; HE600983; CAP32766.1; -; Genomic_DNA. DR PIR; JH0769; JH0769. DR AlphaFoldDB; P32809; -. DR SMR; P32809; -. DR FunCoup; P32809; 625. DR STRING; 6238.P32809; -. DR EnsemblMetazoa; CBG14137.1; CBG14137.1; WBGene00000332. DR KEGG; cbr:CBG_14137; -. DR WormBase; CBG14137; CBP18173; WBGene00000332; -. DR eggNOG; KOG0657; Eukaryota. DR HOGENOM; CLU_030140_0_3_1; -. DR InParanoid; P32809; -. DR OMA; YGYTCNM; -. DR OrthoDB; 1152826at2759; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000008549; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. 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:0019682; P:glyceraldehyde-3-phosphate metabolic process; IEA:UniProtKB-ARBA. 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:000001; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000266; 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; 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; Oxidoreductase; Reference proteome. FT CHAIN 1..341 FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2" FT /id="PRO_0000145508" FT ACT_SITE 158 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009" FT BINDING 13..14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P04406" FT BINDING 35 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P04406" FT BINDING 85 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P04406" FT BINDING 157..159 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 188 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P00362" FT BINDING 217..218 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 240 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT BINDING 322 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" FT SITE 185 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000250|UniProtKB:P0A9B2" SQ SEQUENCE 341 AA; 36509 MW; C93984A33A4A253E CRC64; MSKPTVGING FGRIGRLVLR AAVEKDSVNV VAVNDPFISI DYMVYLFQYD STHGRFKGTV KHEGDYLIVA NEGKSQHKIK VYNSKDPAEI QWGAAGADYV VESTGVFTTI EKANAHLKGG AKKVIISAPS ADAPMFVVGV NHEKYDHAND HIISNASCTT NCLAPLAKVI NDNFGIIEGL MTTVHAVTAT QKTVDGPSGK LWRDGRGAGQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR VPTPDVSVVD LTARLEKPAS LDDIKRVIKA AAEGPLKGVL AYTEDQVVST DFVSDTHSSI FDAGASIILN PNFVKLISWY DNEFGYSNRV VDLISYIATK A //