G3PA_SINAL
ID G3PA_SINAL Reviewed; 233 AA.
AC P09672;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 117.
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: Fragment;
GN Name=GAPA;
OS Sinapis alba (White mustard) (Brassica hirta).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX NCBI_TaxID=3728;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3530755; DOI=10.1111/j.1432-1033.1986.tb09871.x;
RA Martin W.F., Cerff R.;
RT "Prokaryotic features of a nucleus-encoded enzyme. cDNA sequences for
RT chloroplast and cytosolic glyceraldehyde-3-phosphate dehydrogenases from
RT mustard (Sinapis alba).";
RL Eur. J. Biochem. 159:323-331(1986).
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; X04302; CAA27845.1; -; mRNA.
DR PIR; B24796; B24796.
DR AlphaFoldDB; P09672; -.
DR SMR; P09672; -.
DR UniPathway; UPA00116; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; 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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43148; PTHR43148; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 2: Evidence at transcript level;
KW Calvin cycle; Chloroplast; NADP; Oxidoreductase; Plastid.
FT CHAIN <1..233
FT /note="Glyceraldehyde-3-phosphate dehydrogenase A,
FT chloroplastic"
FT /id="PRO_0000145617"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 49..51
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 108..109
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 77
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 233 AA; 25103 MW; EE1502C53AC556F3 CRC64;
DREGAGKHIQ AGAKKVLITA PGKGDIPTYV VGVNAELYSH EDTIISNASC TTNCLAPFVK
VLDQKFGIIK GTMTTTHSYT GDQRLLDASH RDLRRARAAA LNIVPTSTGA AKAVALVLPN
LKGKLNGIAL RVPTPNVSVV DLVVQVSKKT FAEEVNAAFR DAAEKELKGI LDVCDEPLVS
VDFRCSDVSS TIDSSLTMVM GDDMVKVIAW YDNEWGYSQR VVDLADIVAN NWK