G3PA_CHLRE
ID G3PA_CHLRE Reviewed; 374 AA.
AC P50362;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
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;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1132;
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).
RN [2]
RP SUBUNIT, AND INTERACTION WITH CP12.
RX PubMed=12846565; DOI=10.1021/bi034474x;
RA Graciet E., Gans P., Wedel N., Lebreton S., Camadro J.-M., Gontero B.;
RT "The small protein CP12: a protein linker for supramolecular complex
RT assembly.";
RL Biochemistry 42:8163-8170(2003).
RN [3]
RP INTERACTION WITH CP12.
RX PubMed=12492483; DOI=10.1046/j.1432-1033.2003.03372.x;
RA Graciet E., Lebreton S., Camadro J.-M., Gontero B.;
RT "Characterization of native and recombinant A4 glyceraldehyde 3-phosphate
RT dehydrogenase. Kinetic evidence for conformation changes upon association
RT with the small protein CP12.";
RL Eur. J. Biochem. 270:129-136(2003).
RN [4]
RP 3D-STRUCTURE MODELING OF 35-374.
RA Li A.D., Stevens F.J., Huppe H.C., Kersanach R., Anderson L.E.;
RT "Chlamydomonas reinhardtii NADP-linked glyceraldehyde-3-phosphate
RT dehydrogenase contains the cysteine residues identified as potentially
RT domain-locking in the higher plant enzyme and is light activated.";
RL Photosyn. Res. 51:167-177(1997).
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. Component of a complex that contains two dimers
CC of PRK, two tetramers of GAPDH and CP12. CP12 associates with GAPDH,
CC causing its conformation to change. This GAPDH/CP12 complex binds PRK
CC to form a half-complex (one unit). This unit probably dimerizes due
CC partially to interactions between the enzymes of each unit.
CC {ECO:0000269|PubMed:12846565}.
CC -!- INTERACTION:
CC P50362; A6Q0K5: CP12; NbExp=2; IntAct=EBI-9538536, EBI-9538486;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- MISCELLANEOUS: GAPDHB, the second subunit found in plants, is absent in
CC algae.
CC -!- MISCELLANEOUS: Algae contain three forms of GAPDH: two cytosolic forms
CC which participate in glycolysis and one chloroplastic form which
CC participates in photosynthesis. These three forms are encoded by
CC distinct genes.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; L27668; AAA86855.1; -; Genomic_DNA.
DR PIR; T07990; T07990.
DR RefSeq; XP_001689871.1; XM_001689819.1.
DR AlphaFoldDB; P50362; -.
DR SMR; P50362; -.
DR IntAct; P50362; 1.
DR MINT; P50362; -.
DR STRING; 3055.EDP09609; -.
DR PRIDE; P50362; -.
DR ProMEX; P50362; -.
DR EnsemblPlants; PNW88018; PNW88018; CHLRE_01g010900v5.
DR GeneID; 5715019; -.
DR Gramene; PNW88018; PNW88018; CHLRE_01g010900v5.
DR KEGG; cre:CHLRE_01g010900v5; -.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_2_1; -.
DR OrthoDB; 945145at2759; -.
DR UniPathway; UPA00116; -.
DR GO; GO:0009507; C:chloroplast; IDA:CAFA.
DR GO; GO:0099080; C:supramolecular complex; IDA:CAFA.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0019900; F:kinase binding; IPI:CAFA.
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 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 1: Evidence at protein level;
KW Calvin cycle; Chloroplast; Disulfide bond; NADP; Oxidoreductase; Plastid;
KW Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 35..374
FT /note="Glyceraldehyde-3-phosphate dehydrogenase A,
FT chloroplastic"
FT /id="PRO_0000010418"
FT ACT_SITE 190
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 47..48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 189..191
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 248..249
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 217
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT DISULFID 55..325
FT /evidence="ECO:0000250"
SQ SEQUENCE 374 AA; 40304 MW; 8CEB02897930D34C CRC64;
MAAMMQKSAF TGSAVSSKSG VRAKAARAVV DVRAEKKIRV AINGFGRIGR NFLRCWHGRQ
NTLLDVVAIN DSGGVKQASH LLKYDSTLGT FAADVKIVDD SHISVDGKQI KIVSSRDPLQ
LPWKEMNIDL VIEGTGVFID KVGAGKHIQA GASKVLITAP AKDKDIPTFV VGVNEGDYKH
EYPIISNASC TTNCLAPFVK VLEQKFGIVK GTMTTTHSYT GDQRLLDASH RDLRRARAAA
LNIVPTTTGA AKAVSLVLPS LKGKLNGIAL RVPTPTVSVV DLVVQVEKKT FAEEVNAAFR
EAANGPMKGV LHVEDAPLVS IDFKCTDQST SIDASLTMVM GDDMVKVVAW YDNEWGYSQR
VVDLAEVTAK KWVA
