G3P4_CAEEL
ID G3P4_CAEEL Reviewed; 341 AA.
AC P17331;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 4;
DE Short=GAPDH-4;
DE EC=1.2.1.12;
GN Name=gpd-4; ORFNames=F33H1.2;
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; X52673; CAA36899.1; -; Genomic_DNA.
DR EMBL; Z48783; CAA88697.1; -; Genomic_DNA.
DR PIR; S03912; DEKWG4.
DR RefSeq; NP_496192.1; NM_063791.4.
DR AlphaFoldDB; P17331; -.
DR SMR; P17331; -.
DR BioGRID; 39897; 10.
DR DIP; DIP-25637N; -.
DR IntAct; P17331; 1.
DR STRING; 6239.F33H1.2; -.
DR iPTMnet; P17331; -.
DR EPD; P17331; -.
DR PaxDb; P17331; -.
DR PeptideAtlas; P17331; -.
DR EnsemblMetazoa; F33H1.2.1; F33H1.2.1; WBGene00001686.
DR GeneID; 174578; -.
DR KEGG; cel:CELE_F33H1.2; -.
DR UCSC; F33H1.2.2; c. elegans.
DR CTD; 174578; -.
DR WormBase; F33H1.2; CE01568; WBGene00001686; gpd-4.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000153298; -.
DR HOGENOM; CLU_030140_0_1_1; -.
DR InParanoid; P17331; -.
DR OMA; QCIVEST; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; P17331; -.
DR Reactome; R-CEL-70171; Glycolysis.
DR Reactome; R-CEL-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:P17331; -.
DR Proteomes; UP000001940; Chromosome II.
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 4"
FT /id="PRO_0000145513"
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; 36427 MW; 0DBED0FFD65D60F8 CRC64;
MSKANVGING FGRIGRLVLR AAVEKDTVQV VAVNDPFITI DYMVYLFKYD STHGQFKGTV
TYDGDFLIVQ KDGKSSHKIK VFNSKDPAAI AWGSVKADFV VESTGVFTTK EKASAHLQGG
AKKVIISAPS ADAPMYVVGV NHEKYDASND HVISNASCTT NCLAPLAKVI NDNFGIIEGL
MTTVHAVTAT QKTVDGPSGK LWRDGRGAGQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR
VPTPDVSVVD LTVRLEKPAS MDDIKKVVKA AADGPMKGIL AYTEDQVVST DFVSDPHSSI
FDTGACISLN PNFVKLVSWY DNEYGYSNRV VDLIGYIATR G
