G3PA_MAIZE
ID G3PA_MAIZE Reviewed; 403 AA.
AC P09315; P15985;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic;
DE EC=1.2.1.13;
DE AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase subunit A;
DE Flags: Precursor;
GN Name=GAPA; Synonyms=GPA1;
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.
RX PubMed=2515291; DOI=10.1007/bf02602911;
RA Quigley F., Brinkmann H., Martin W.F., Cerff R.;
RT "Strong functional GC pressure in a light-regulated maize gene encoding
RT subunit GAPA of chloroplast glyceraldehyde-3-phosphate dehydrogenase:
RT implications for the evolution of GAPA pseudogenes.";
RL J. Mol. Evol. 29:412-421(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3357887; DOI=10.1073/pnas.85.8.2672;
RA Quigley F., Martin W.F., Cerff R.;
RT "Intron conservation across the prokaryote-eukaryote boundary: structure of
RT the nuclear gene for chloroplast glyceraldehyde-3-phosphate dehydrogenase
RT from maize.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2672-2676(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-125 AND 301-403.
RC STRAIN=cv. W64 X W128E; TISSUE=Leaf;
RX PubMed=16666879; DOI=10.1104/pp.90.3.792;
RA Gowri G., Campbell W.H.;
RT "cDNA clones for corn leaf NADH: nitrate reductase and chloroplast
RT NAD(P)(+): glyceraldehyde-3-phosphate dehydrogenase.";
RL Plant Physiol. 90:792-798(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.13;
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Tetramer of either four A chains (GAPDH 2) or two A and two B
CC chains (GAPDH 1). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {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; X15408; CAA33455.1; -; Genomic_DNA.
DR EMBL; M18976; AAA33464.1; -; Genomic_DNA.
DR EMBL; M31481; AAA33484.1; -; mRNA.
DR EMBL; M31483; AAA33485.1; -; mRNA.
DR PIR; A30890; DEZMG3.
DR RefSeq; NP_001105414.1; NM_001111944.1.
DR AlphaFoldDB; P09315; -.
DR SMR; P09315; -.
DR STRING; 4577.GRMZM2G162845_P01; -.
DR PRIDE; P09315; -.
DR GeneID; 542368; -.
DR KEGG; zma:542368; -.
DR MaizeGDB; 13872; -.
DR eggNOG; KOG0657; Eukaryota.
DR OrthoDB; 945145at2759; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P09315; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0009416; P:response to light stimulus; 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; PTHR43148; PTHR43148; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 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 Calvin cycle; Chloroplast; NADP; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT CHAIN 67..403
FT /note="Glyceraldehyde-3-phosphate dehydrogenase A,
FT chloroplastic"
FT /id="PRO_0000010422"
FT ACT_SITE 220
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 77..78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 219..221
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 278..279
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 247
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 403 AA; 42867 MW; 0505124C3F458DD8 CRC64;
MASSMLSATT VPLQQGGGLS EFSGLRSSAS LPMRRNATSD DFMSAVSFRT HAVGTSGGPR
RAPTEAKLKV AINGFGRIGR NFLRCWHGRG DASPLDVIAI NDTGGVKQAS HLLKYDSTLG
IFDADVKPVG DNAISVDGKV IKVVSDRNPS NLPWGELGID LVIEGTGVFV DREGAGKHIQ
AGAKKVLITA PGKGDIPTYV VGVNADQYNP DEPIISNASC TTNCLAPFVK VLDQKFGIIK
GTMTTTHSYT GDQRLLDASH RDLRRARAAA LNIVPTSTGA AKAVSLVLPN LKGKLNGIAL
RVPTPNVSVV DLVVQVSKKT LAEEVNQAFR DAAANELTGI LEVCDVPLVS VDFRCSDVSS
TIDASLTMVM GDDMVKVISW YDNEWGYSQR VVDLADICAN QWK
