ID   G3PC2_HORVU             Reviewed;         305 AA.
AC   P08477;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2, cytosolic;
DE            EC=1.2.1.12;
DE   Flags: Fragment;
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   Chojecki J.;
RT   "Identification and characterisation of a cDNA clone for cytosolic
RT   glyceraldehyde-3-phosphate dehydrogenase in barley.";
RL   Carlsberg Res. Commun. 51:203-210(1986).
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}.
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DR   EMBL; M36650; AAA32956.1; -; mRNA.
DR   PIR; A24159; A24159.
DR   AlphaFoldDB; P08477; -.
DR   SMR; P08477; -.
DR   IntAct; P08477; 1.
DR   UniPathway; UPA00109; UER00184.
DR   ExpressionAtlas; P08477; 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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN           <1..305
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase 2,
FT                   cytosolic"
FT                   /id="PRO_0000145603"
FT   ACT_SITE        122
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT   BINDING         3
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         121..123
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         181..182
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            149
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   305 AA;  33236 MW;  4F82FA362F222AC5 CRC64;
     VNDPFITTDY MTYMFKYDTV HGQWKHHEVK VKDSKTLLFG EKEVAVFGCR NPEEIPWAAA
     GAEYVVESTG VFTDKDKAAA HIKGGAKKVI ISAPSKDAPM FVCGVNEKEY KSDIDIVSNA
     SCTTNCPAPL AKVINDRFGI VEGLMTTVHA MTATQKTVDG PSSKDWRGGR AASFNIIPSS
     TGAAKAVGKV LPELNGKLTG MAFRVPTVDV SVVDLTVRLA KPATYEQIKA AIKEESEGNL
     KGILGYVDED LVSTDFQGDS RSSIFDAKAG IALNDNFVKL VSWYDNEWGY STRVVDLIRH
     MHSTK