G3PA_GRAGA
ID G3PA_GRAGA Reviewed; 416 AA.
AC P30724;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, chloroplastic;
DE EC=1.2.1.13;
DE AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase;
DE Flags: Precursor;
GN Name=GAPA;
OS Gracilaria gracilis (Red alga).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Gracilaria.
OX NCBI_TaxID=2777;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Norway;
RX PubMed=7916671; DOI=10.1007/bf00312639;
RA Zhou Y.H., Ragan M.A.;
RT "cDNA cloning and characterization of the nuclear gene encoding chloroplast
RT glyceraldehyde-3-phosphate dehydrogenase from the marine red alga
RT Gracilaria verrucosa.";
RL Curr. Genet. 23:483-489(1993).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=7954900; DOI=10.1007/bf00326308;
RA Zhou Y.H., Ragan M.A.;
RT "Cloning and characterization of the nuclear gene encoding plastid
RT glyceraldehyde-3-phosphate dehydrogenase from the marine red alga
RT Gracilaria verrucosa.";
RL Curr. Genet. 26:79-86(1994).
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: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z15102; CAA78811.1; -; mRNA.
DR EMBL; L22011; AAA33355.1; -; Genomic_DNA.
DR PIR; S45484; S45484.
DR AlphaFoldDB; P30724; -.
DR SMR; P30724; -.
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:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; 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; 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; Transit peptide.
FT TRANSIT 1..78
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 79..416
FT /note="Glyceraldehyde-3-phosphate dehydrogenase,
FT chloroplastic"
FT /id="PRO_0000010420"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 90..91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 232..234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 291..292
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 260
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 416 AA; 44338 MW; 33B9437E84230BD8 CRC64;
MAFVAPVSSV FSTSSKSAVC SGRSSFAQFS GLKKVNNTAR LQTAEQGSAF GGVSDANDAF
FNAVNTMGAP ARTSNAPSMK VRVAINGFGR IGRNFIRCWA GRTDSNMDVV CINDTSGVKT
ASHLLKYDSI LGTFDSDVVA GEDSITVDGK TIKVVSNRNP LELPWKEMEI DIVVEATGVF
VDAVGAGKHI QAGAKKVLIT APGKGEGVGT FVVGVNDHLY SHDKFDIVSN ASCTTNCMAP
FMKVLDDEFG VVRGMMTTTH SYTGDQRLLD AGHRDLRRAR SAALNIVPTT TGAAKAVALV
VPTLAGKLNG IALRVPTPNV SVCDVVMQVS KKTFKEEVNG ALLKAANGSM KGIIKYSDEP
LVSCDYRGTD ESTIIDSSLT MVMGDDMLKV VAWYDNEWGY SQRVVDLGEV MASQWK
