ID   G3PA_CHOCR              Reviewed;         414 AA.
AC   P34919;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, 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   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Stackhouse;
RX   PubMed=8007000; DOI=10.1007/bf00163149;
RA   Liaud M.-F., Valentin C., Martin W., Bouget F.Y., Kloareg B., Cerff R.;
RT   "The evolutionary origin of red algae as deduced from the nuclear genes
RT   encoding cytosolic and chloroplast glyceraldehyde-3-phosphate
RT   dehydrogenases from Chondrus crispus.";
RL   J. Mol. Evol. 38:319-327(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; X73035; CAA51516.1; -; mRNA.
DR   AlphaFoldDB; P34919; -.
DR   SMR; P34919; -.
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..76
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           77..414
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase,
FT                   chloroplastic"
FT                   /id="PRO_0000010419"
FT   ACT_SITE        231
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT   BINDING         88..89
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..232
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         289..290
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         394
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            258
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   414 AA;  44459 MW;  065DE62CE1064111 CRC64;
     MAFVAPVATV RATTKSSVCQ VQGRSTFAQF SGMKKVNQSS RLQPAQSGSA FGGYSDANDA
     FYTRVSGIVA ATFGPTMKVR VAINGFGRIG RNFIRCWAGR SDSNMEVVCI NDTSGVKTAS
     HLLKYDSILG TFDADVSAGE DTISVNGKTI KIVSNRNPLQ LPWKEMNIDI VVEATGVFVD
     APGAGKHIEA GAKKVLITAP GKGDGIGTFV VGVNEKDYSH DKYDIVSNAS CTTNCMAPFM
     KVLDDEFGVV RGMMTTTHSY TGDQRLLDAG HRDLRRARSA ALNIVPTTTG AAKAVALVVP
     SLKGKLNGIA LRVPTPNVSV CDVVMQVNKK TFKEEVNGAL LKASEGAMKG IIKYSDEPLV
     SCDHRGTDES TIIDSSLTMV MGDDMIKVVA WYDNEWGYSQ RVVDLGEVMA RQWK