G3P3_CAEBR
ID G3P3_CAEBR Reviewed; 341 AA.
AC P32810; A8XJE0;
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 3.1;
DE Short=GAPDH-3;
DE EC=1.2.1.12;
GN Name=gpd-3.1; Synonyms=gpd-3; ORFNames=CBG14136;
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.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; CAP32765.1; -; Genomic_DNA.
DR PIR; JH0770; JH0770.
DR RefSeq; XP_002644327.1; XM_002644281.1.
DR AlphaFoldDB; P32810; -.
DR SMR; P32810; -.
DR STRING; 6238.CBG14136; -.
DR EnsemblMetazoa; CBG14136.1; CBG14136.1; WBGene00000333.
DR GeneID; 8586322; -.
DR KEGG; cbr:CBG_14136; -.
DR CTD; 8586322; -.
DR WormBase; CBG14136; CBP09851; WBGene00000333; Cbr-gpd-3.1.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; P32810; -.
DR OMA; NRMLDNC; -.
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 3.1"
FT /id="PRO_0000145509"
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; 36453 MW; 10EC13A5BB5A662A CRC64;
MSKPSVGING FGRIGRLVLR AAVEKDSVNV VAVNDPFISI DYMVYLFQYD STHGRFKGTV
AHEGDYLLVA KEGKSQHKIK VYNSRDPAEI QWGSAGADYV VESTGVFTTI EKANAHLKGG
AKKVIISAPS ADAPMFVVGV NHEKYDHAND HIISNASCTT NCLAPLAKVI NDNFGIIEGL
MTTVHAVTAT QKTVDGPSGK LWRDGRGAGQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR
VPTPDVSVVD LTARLEKPAS LDDIKKVVKA AAEGPLKGVL AYTEDQVVST DFVSDTHSSI
FDAGASIILN PNFVKLISWY DNEFGYSNRV VDLISYIATK A
