G3PC3_MAIZE
ID G3PC3_MAIZE Reviewed; 337 AA.
AC Q43247; Q06476;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 3, cytosolic;
DE EC=1.2.1.12;
GN Name=GAPC3; Synonyms=GPC3;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73; TISSUE=Root;
RX PubMed=9037163; DOI=10.1023/a:1005729112038;
RA Manjunath S., Sachs M.M.;
RT "Molecular characterization and promoter analysis of the maize cytosolic
RT glyceraldehyde 3-phosphate dehydrogenase gene family and its expression
RT during anoxia.";
RL Plant Mol. Biol. 33:97-112(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 104-337.
RC STRAIN=cv. Berkeley Fast; TISSUE=Coleoptile;
RX PubMed=2535522; DOI=10.2307/3868988;
RA Russell D.A., Sachs M.M.;
RT "Differential expression and sequence analysis of the maize glyceraldehyde-
RT 3-phosphate dehydrogenase gene family.";
RL Plant Cell 1:793-803(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 104-337.
RC STRAIN=B73;
RX PubMed=1717817; DOI=10.1007/bf00272159;
RA Russell D.A., Sachs M.M.;
RT "The maize cytosolic glyceraldehyde-3-phosphate dehydrogenase gene family:
RT organ-specific expression and genetic analysis.";
RL Mol. Gen. Genet. 229:219-228(1991).
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; U45856; AAA87579.1; -; mRNA.
DR EMBL; L13431; AAA33465.1; -; mRNA.
DR PIR; PQ0179; PQ0179.
DR PIR; T02722; T02722.
DR RefSeq; NP_001105385.1; NM_001111915.2.
DR AlphaFoldDB; Q43247; -.
DR SMR; Q43247; -.
DR STRING; 4577.GRMZM2G071630_P01; -.
DR PaxDb; Q43247; -.
DR PRIDE; Q43247; -.
DR EnsemblPlants; Zm00001eb184000_T001; Zm00001eb184000_P001; Zm00001eb184000.
DR GeneID; 542333; -.
DR Gramene; Zm00001eb184000_T001; Zm00001eb184000_P001; Zm00001eb184000.
DR KEGG; zma:542333; -.
DR eggNOG; KOG0657; Eukaryota.
DR OMA; TRIMMED; -.
DR OrthoDB; 945145at2759; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; Q43247; baseline and differential.
DR Genevisible; Q43247; ZM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; TAS:AgBase.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; TAS:AgBase.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0042301; F:phosphate ion binding; TAS:AgBase.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0034059; P:response to anoxia; IEP:AgBase.
DR GO; GO:0009408; P:response to heat; IEP:AgBase.
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; Reference proteome.
FT CHAIN 1..337
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 3,
FT cytosolic"
FT /id="PRO_0000145607"
FT REGION 1..151
FT /note="Binding to NAD"
FT REGION 152..337
FT /note="Catalytic"
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; 36449 MW; B2C73B1961CA45EC CRC64;
MAKIKIGING FGRIGRLVAR VALQSDDVEL VAVNDPFIST DYMTYMFKYD TVHGQWKHHE
VKVKDSKTLL FGEKEVAVFG CRNPEEIPWG SVGAEYVVES TGVFTDQEKA AAHLKGGAKK
VVISAPSKDA PMFVVGVNEK EYKSDINIVS NASCTTNCLA PLAKVINDKF GIVEGLMTTV
HAITATQKTV DGPSSKDWRG GRAASFNIIP SSTGAAKAVG KVLPVLNGKL TGMSFRVPTV
DVSVVDLTVR LEKSATYDEI KAAVKAEAEG SLKGILGYVE EDLVSTDFQG DSRSSIFDAK
AGIALNGNFV KLVSWYDNEW GYSTRVVDLI RHMNSTK
