ID   G3PC1_HORVU             Reviewed;         337 AA.
AC   P26517;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1, cytosolic;
DE            EC=1.2.1.12;
GN   Name=GAPC;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Martin W., Gierl A., Saedler 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   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X60343; CAA42901.1; -; mRNA.
DR   PIR; S18482; DEBHG.
DR   AlphaFoldDB; P26517; -.
DR   SMR; P26517; -.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0583650.1; HORVU.MOREX.r2.7HG0583650.1; HORVU.MOREX.r2.7HG0583650.
DR   Gramene; HORVU.MOREX.r2.7HG0583650.1; HORVU.MOREX.r2.7HG0583650.1; HORVU.MOREX.r2.7HG0583650.
DR   UniPathway; UPA00109; UER00184.
DR   ExpressionAtlas; P26517; baseline and differential.
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 1,
FT                   cytosolic"
FT                   /id="PRO_0000145602"
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;  36514 MW;  8150135A6FDA6726 CRC64;
     MGKIKIGING FGRIGRLVAR VALQSDDVEL VAVNDPFITT EYMTYMFKYD TVHGHWKHSD
     IKLKDDKTLL FGEKPVTVFG VRNPEEIPWG EAGADYVVES TGVFTDKDKA AAHLKGGAKK
     VVISAPSKDA PMFVVGVNED KYTSDVNIVS NASCTTNCLA PLAKVINDNF GIIEGLMTTV
     HAITATQKTV DGPSSKDWRG GRAASFNIIP SSTGAAKAVG KVLPELNGKL TGMSFRVPTV
     DVSVVDLTVR TEKAASYDDI KKAIKAASEG KLKGIMGYVE EDLVSTDFVG DSRSSIFDAK
     AGIALNDHFV KLVSWYDNEW GYSNRVVDLI RHMAKTQ