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G3P3_CAEEL
ID   G3P3_CAEEL              Reviewed;         341 AA.
AC   P17330;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 3;
DE            Short=GAPDH-3;
DE            EC=1.2.1.12;
GN   Name=gpd-3; ORFNames=K10B3.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=2716055; DOI=10.1016/0022-2836(89)90490-7;
RA   Huang X.Y., Barrios L.A.M., Vonkhorporn P., Honda S., Albertson D.G.,
RA   Hecht R.M.;
RT   "Genomic organization of the glyceraldehyde-3-phosphate dehydrogenase gene
RT   family of Caenorhabditis elegans.";
RL   J. Mol. Biol. 206:411-424(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: There are four nearly identical glyceraldehyde 3-
CC       phosphate dehydrogenases in Caenorhabditis elegans.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X15254; CAA33327.1; -; Genomic_DNA.
DR   EMBL; FO080552; CCD64599.1; -; Genomic_DNA.
DR   PIR; S03914; DEKWG3.
DR   RefSeq; NP_508534.3; NM_076133.5.
DR   AlphaFoldDB; P17330; -.
DR   SMR; P17330; -.
DR   BioGRID; 45544; 24.
DR   DIP; DIP-26747N; -.
DR   IntAct; P17330; 4.
DR   MINT; P17330; -.
DR   STRING; 6239.K10B3.7.1; -.
DR   EPD; P17330; -.
DR   PaxDb; P17330; -.
DR   PeptideAtlas; P17330; -.
DR   EnsemblMetazoa; K10B3.7.1; K10B3.7.1; WBGene00001685.
DR   GeneID; 180601; -.
DR   KEGG; cel:CELE_K10B3.7; -.
DR   UCSC; K10B3.7.1; c. elegans.
DR   CTD; 180601; -.
DR   WormBase; K10B3.7; CE07370; WBGene00001685; gpd-3.
DR   eggNOG; KOG0657; Eukaryota.
DR   GeneTree; ENSGT00940000153298; -.
DR   HOGENOM; CLU_030140_0_3_1; -.
DR   InParanoid; P17330; -.
DR   OMA; NCVAPMA; -.
DR   OrthoDB; 945145at2759; -.
DR   PhylomeDB; P17330; -.
DR   Reactome; R-CEL-70171; Glycolysis.
DR   Reactome; R-CEL-70263; Gluconeogenesis.
DR   SignaLink; P17330; -.
DR   UniPathway; UPA00109; UER00184.
DR   PRO; PR:P17330; -.
DR   Proteomes; UP000001940; 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 3"
FT                   /id="PRO_0000145512"
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"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..159
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..218
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         322
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            185
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  36459 MW;  88938B34676637F6 CRC64;
     MTKPSVGING FGRIGRLVLR AAVEKDSVNV VAVNDPFISI DYMVYLFQYD STHGRFKGTV
     AHEGDYLLVA KEGKSQHKIK VYNSRDPAEI QWGASGADYV VESTGVFTTI EKANAHLKGG
     AKKVIISAPS ADAPMFVVGV NHEKYDHAND HIISNASCTT NCLAPLAKVI NDNFGIIEGL
     MTTVHAVTAT QKTVDGPSGK LWRDGRGAGQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR
     VPTPDVSVVD LTARLEKPAS LDDIKKVIKA AADGPMKGIL AYTEDQVVST DFVSDTNSSI
     FDAGASISLN PHFVKLVSWY DNEFGYSNRV VDLISYIATK A
 
 
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