G3PC_PEA
ID G3PC_PEA Reviewed; 338 AA.
AC P34922;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE EC=1.2.1.12;
GN Name=GAPC1;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8095691; DOI=10.1093/oxfordjournals.molbev.a039989;
RA Martin W., Lydiate D., Brinkmann H., Forkmann G., Saedler H., Cerff R.;
RT "Molecular phylogenies in angiosperm evolution.";
RL Mol. Biol. Evol. 10:140-162(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Rosakrone;
RX PubMed=8114942; DOI=10.1038/367387a0;
RA Kersanach R., Brinkmann H., Liaud M.-F., Zhang D.-X., Martin W., Cerff R.;
RT "Five identical intron positions in ancient duplicated genes of eubacterial
RT origin.";
RL Nature 367:387-389(1994).
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; L07500; AAA33667.1; -; mRNA.
DR EMBL; X73150; CAA51675.1; -; Genomic_DNA.
DR PIR; T06781; T06781.
DR AlphaFoldDB; P34922; -.
DR SMR; P34922; -.
DR PRIDE; P34922; -.
DR SABIO-RK; P34922; -.
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..338
FT /note="Glyceraldehyde-3-phosphate dehydrogenase, cytosolic"
FT /id="PRO_0000145610"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 14..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 154..156
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 214..215
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 182
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 338 AA; 36609 MW; 09B55960BE03EA27 CRC64;
MGAKIKIGIN GFGRIGRLVA RVALKRDDVE LVAVNDPFIT TDYMTYMFKY DSVHGQWKND
ELTVKDSNTL LFGQKPVTVF AHRNPEEIPW ASTGADIIVE STGVFTDKDK AAAHLKGGAK
KVIISAPSKD APMFVVGVNE NEYKPEFDII SNASCTTNCL APLAKVINDR FGIVEGLMTT
VHSITATQKT VDGPSSKDWR GGRAASFNII PSSTGAAKAV GKVLPALNGK LTGMSFRVPT
VDVSVVDLTV RLEKAATYDE IKAAIKEESE GKLKGILGYT EDDVVSTDFI GDTRSSIFDA
KAGIALNDKF VKLVSWYDNE LGYSTRVVDL IVHIAKQL
