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   03-AUG-2022, entry version 130.
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   Name=gpd-3.2 {ECO:0000312|WormBase:CBG14137};
GN   Synonyms=gpd-2 {ECO:0000312|WormBase:CBG14137};
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 + 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: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}.
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DR   EMBL; M86669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; HE600983; CAP32766.1; -; Genomic_DNA.
DR   PIR; JH0769; JH0769.
DR   RefSeq; XP_002644328.1; XM_002644282.1.
DR   AlphaFoldDB; P32809; -.
DR   SMR; P32809; -.
DR   STRING; 6238.CBG14137; -.
DR   EnsemblMetazoa; CBG14137.1; CBG14137.1; WBGene00000332.
DR   GeneID; 8586323; -.
DR   KEGG; cbr:CBG_14137; -.
DR   CTD; 8586323; -.
DR   WormBase; CBG14137; CBP18173; WBGene00000332; Cbr-gpd-3.2.
DR   eggNOG; KOG0657; Eukaryota.
DR   HOGENOM; CLU_030140_0_3_1; -.
DR   InParanoid; P32809; -.
DR   OMA; YVQITTI; -.
DR   OrthoDB; 945145at2759; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
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; IBA:GO_Central.
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   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   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