ID   G3PA_GRAVE              Reviewed;         416 AA.
AC   P30724;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-NOV-2008, entry version 60.
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 verrucosa (Red alga).
OC   Eukaryota; Rhodophyta; Florideophyceae; Gracilariales; Gracilariaceae;
OC   Gracilaria.
OX   NCBI_TaxID=2777;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Norway;
RX   MEDLINE=93306755; PubMed=7916671; DOI=10.1007/BF00312639;
RA   Zhou Y.H., Ragan M.A.;
RT   "cDNA cloning and characterization of the nuclear gene encoding
RT   chloroplast glyceraldehyde-3-phosphate dehydrogenase from the marine
RT   red alga Gracilaria verrucosa.";
RL   Curr. Genet. 23:483-489(1993).
RN   [2]
RP   SEQUENCE REVISION.
RX   MEDLINE=95042840; 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: D-glyceraldehyde 3-phosphate + phosphate +
CC       NADP(+) = 3-phospho-D-glyceroyl phosphate + NADPH.
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; Z15102; CAA78811.1; -; mRNA.
DR   EMBL; L22011; AAA33355.1; -; Genomic_DNA.
DR   PIR; S45484; S45484.
DR   HSSP; P19866; 1NBO.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (N...; IEA:EC.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR000173; GlycerAld_3-P_DHase.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DHase_1.
DR   PANTHER; PTHR10836; GAP_DH; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
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   Transit peptide.
FT   TRANSIT       1     78       Chloroplast (Potential).
FT   CHAIN        79    416       Glyceraldehyde-3-phosphate dehydrogenase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000010420.
FT   NP_BIND      90     91       NADP (By similarity).
FT   REGION      232    234       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      291    292       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    233    233       Nucleophile (By similarity).
FT   BINDING     114    114       NADP (By similarity).
FT   BINDING     158    158       NADP; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     263    263       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     278    278       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     314    314       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     396    396       NADP (By similarity).
FT   SITE        260    260       Activates thiol group during catalysis
FT                                (By similarity).
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
//