ID   G3PC_GRAGA              Reviewed;         335 AA.
AC   P54270;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE            EC=1.2.1.12;
GN   Name=GAPC;
OS   Gracilaria gracilis (Red alga).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Gracilaria.
OX   NCBI_TaxID=2777;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8590478; DOI=10.1007/bf00326430;
RA   Zhou Y.H., Ragan M.A.;
RT   "The nuclear gene and cDNAs encoding cytosolic glyceraldehyde-3-phosphate
RT   dehydrogenase from the marine red alga Gracilaria verrucosa: cloning,
RT   characterization and phylogenetic analysis.";
RL   Curr. Genet. 28:324-332(1995).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; L38661; AAB01379.1; -; Genomic_DNA.
DR   PIR; S59579; S59579.
DR   AlphaFoldDB; P54270; -.
DR   SMR; P54270; -.
DR   UniPathway; UPA00109; UER00184.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
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.
FT   CHAIN           1..335
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase, cytosolic"
FT                   /id="PRO_0000145601"
FT   ACT_SITE        152
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         80
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..153
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         211..212
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            179
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   335 AA;  36144 MW;  5B97F5BF3D40ACB0 CRC64;
     MTVPQVGING FGRIGRLVLR AAIEKDTMSV VAINDPFIDL EYMAYMFKFD STHGRYAGSV
     ETKDGKLIVN GKSITIYGHR DPAEIPWAEA GADYVVESTG VFTLKEKAEK HFTGGAKKVI
     ISAPSKDAPM FVCGVNEDKY TPDLNVISNA SCTTNCLAPL VKVIHEKYGI EEGLMTTVHA
     TTATQKTVDG PSQKDWRGGR GAGANIIPSS TGAAKAVGKV LPELNGKLTG MAFRVPTSDV
     SVVDLTVRLA TETSYDDIKA TMKAAAEDSM KGILKYTEEA VVSTDFIHEE ASCVFDAGAG
     IMLNSRFCKL VAWYDNEWGY SNRVVDLIAH VAKLQ