ID   G3PC_ANTMA              Reviewed;         337 AA.
AC   P25861;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE            EC=1.2.1.12;
GN   Name=GAPC; Synonyms=GAPDH;
OS   Antirrhinum majus (Garden snapdragon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX   NCBI_TaxID=4151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Martin W., Gierl A., Seadler H.;
RT   "Molecular evidence for pre-Cretaceous angiosperm origins.";
RL   Nature 339:46-48(1989).
CC   -!- FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the
CC       pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-
CC       phospho-D-glyceroyl phosphate. Essential for the maintenance of
CC       cellular ATP levels and carbohydrate metabolism (By similarity).
CC       {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- MISCELLANEOUS: Plants contain two types of GAPDH: cytosolic forms which
CC       participate in glycolysis and chloroplast forms which participate in
CC       photosynthesis. All the forms are encoded by distinct genes.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA42103.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X59517; CAA42103.1; ALT_INIT; mRNA.
DR   PIR; S17991; DESKG.
DR   AlphaFoldDB; P25861; -.
DR   SMR; P25861; -.
DR   PRIDE; P25861; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN           1..337
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase, cytosolic"
FT                   /id="PRO_0000145593"
FT   ACT_SITE        154
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         82
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         153..155
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         213..214
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            181
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   337 AA;  36685 MW;  0E0E69F1F474F0D7 CRC64;
     MAPIKIGING FGRIGRLVAR VALQRDDVEL VAVNDPFIST DYMTYMFKYD SVHGAWKHHE
     LKVKDEKTLL FGEKPVVVFG RRNPEEIPRA STGAEYIVES TGVFTDKDKA AAHLKGGAKK
     VIISAPSKDA PMFVVGVNEK EYKSDLHIVS NASCTTNCLA PLAKVINDRF GIVEGLMTTV
     HSITATQKTV DGPSAKDWRG GRAASFNIIP SSTGAAKAVG KVLPQLNGKL TGMSFRVPTV
     DVSVVDLTVR LEKKATYEQI KAAIKEESEG KLKGILGYTE DDVVSTDFVG DSRSSIFDAK
     AGIALNDNFV KLVSWYDNEW GYSTRVVDLI VHMASVQ