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
