ID G3PA_ARATH Reviewed; 396 AA. AC P25856; Q41184; Q9LSE6; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2002, sequence version 3. DT 25-NOV-2008, entry version 87. 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; OrderedLocusNames=At3g26650; ORFNames=MLJ15.4, MLJ15_5; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=92009205; PubMed=1916285; DOI=10.1016/0378-1119(91)90242-4; RA Shih M.-C., Heinrich P., Goodman H.M.; RT "Cloning and chromosomal mapping of nuclear genes encoding chloroplast RT and cytosolic glyceraldehyde-3-phosphate-dehydrogenase from RT Arabidopsis thaliana."; RL Gene 104:133-138(1991). RN [2] RP ERRATUM. RX MEDLINE=93013005; PubMed=1398114; DOI=10.1016/0378-1119(92)90290-6; RA Shih M.-C., Heinrich P., Goodman H.M.; RL Gene 119:317-319(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=cv. Columbia; TISSUE=Shoot; RX MEDLINE=97086699; PubMed=8932388; DOI=10.1093/nar/24.21.4313; RA Quigley F., Dao P., Cottet A., Mache R.; RT "Sequence analysis of an 81 kb contig from Arabidopsis thaliana RT chromosome III."; RL Nucleic Acids Res. 24:4313-4318(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20277480; PubMed=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RX MEDLINE=22745486; PubMed=12766230; DOI=10.1074/mcp.M300030-MCP200; RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., RA Garin J., Joyard J., Rolland N.; RT "Proteomics of the chloroplast envelope membranes from Arabidopsis RT thaliana."; RL Mol. Cell. Proteomics 2:325-345(2003). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NADP(+) = 3-phospho-D-glyceroyl phosphate + NADPH. CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle. CC -!- SUBUNIT: Tetramer of either four A chains (GAPDH 2) or two A and CC two B chains (GAPDH 1) (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral CC membrane protein. Plastid, chloroplast stroma. CC -!- MISCELLANEOUS: Plants contain three forms of GAPDH: a cytosolic CC form which participates in glycolysis and two chloroplast forms CC which participates in photosynthesis. These three forms are CC encoded by distinct genes. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M64114; AAD10209.1; ALT_INIT; mRNA. DR EMBL; M64117; AAA32793.1; -; Genomic_DNA. DR EMBL; S45910; AAB23532.1; -; Genomic_DNA. DR EMBL; X98130; CAA66816.1; -; Genomic_DNA. DR EMBL; AB026648; BAB01730.1; -; Genomic_DNA. DR EMBL; AY058140; AAL25556.1; -; mRNA. DR EMBL; AY058107; AAL24215.1; -; mRNA. DR EMBL; AF428431; AAL16200.1; -; mRNA. DR EMBL; AY075637; AAL91645.1; -; mRNA. DR EMBL; AY142053; AAM98317.1; -; mRNA. DR PIR; JQ1285; JQ1285. DR RefSeq; NP_566796.2; -. DR UniGene; At.23357; -. DR HSSP; P19866; 1NBO. DR SMR; P25856; 61-396. DR SWISS-2DPAGE; P25856; -. DR ProMEX; P25856; -. DR GeneID; 822277; -. DR GenomeReviews; BA000014_GR; AT3G26650. DR KEGG; ath:AT3G26650; -. DR NMPDR; fig|3702.1.peg.14942; -. DR TAIR; At3g26650; -. DR BioCyc; MetaCyc:AT3G26650-MON; -. DR ArrayExpress; P25856; -. DR GermOnline; AT3G26650; Arabidopsis thaliana. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; 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 PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 1: Evidence at protein level; KW Calvin cycle; Chloroplast; Complete proteome; Membrane; NADP; KW Oxidoreductase; Plastid; Transit peptide. FT TRANSIT 1 60 Chloroplast (By similarity). FT CHAIN 61 396 Glyceraldehyde-3-phosphate dehydrogenase FT A, chloroplastic. FT /FTId=PRO_0000010416. FT NP_BIND 71 72 NADP (By similarity). FT REGION 212 214 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 271 272 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 213 213 Nucleophile (By similarity). FT BINDING 95 95 NADP (By similarity). FT BINDING 140 140 NADP; via carbonyl oxygen (By FT similarity). FT BINDING 243 243 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 258 258 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 294 294 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 376 376 NADP (By similarity). FT SITE 240 240 Activates thiol group during catalysis FT (By similarity). FT CONFLICT 172 172 I -> M (in Ref. 1 and 3). SQ SEQUENCE 396 AA; 42490 MW; FFD7FD662FB222FC CRC64; MASVTFSVPK GFTEFSGLRS SSASLPFGKK LSSDEFVSIV SFQTSAMGSS GGYRKGVTEA KLKVAINGFG RIGRNFLRCW HGRKDSPLDI IAINDTGGVK QASHLLKYDS TLGIFDADVK PSGETAISVD GKIIQVVSNR NPSLLPWKEL GIDIVIEGTG VFVDREGAGK HIEAGAKKVI ITAPGKGDIP TYVVGVNADA YSHDEPIISN ASCTTNCLAP FVKVLDQKFG IIKGTMTTTH SYTGDQRLLD ASHRDLRRAR AAALNIVPTS TGAAKAVALV LPNLKGKLNG IALRVPTPNV SVVDLVVQVS KKTFAEEVNA AFRDSAEKEL KGILDVCDEP LVSVDFRCSD FSTTIDSSLT MVMGDDMVKV IAWYDNEWGY SQRVVDLADI VANNWK //