ID G3PC_ORYSJ Reviewed; 337 AA. AC Q0J8A4; Q42977; Q6ZK60; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; DE EC=1.2.1.12; DE AltName: Full=PP38; GN Name=GAPC; Synonyms=GPC; GN OrderedLocusNames=Os08g0126300, LOC_Os08g03290; GN ORFNames=OJ1163_G08.15, OsJ_024858; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Ilpoombyeo; TISSUE=Seed; RA Yoon U.H., Kim Y.H.; RT "Molecular cloning of glyceraldehyde-3-phosphate dehydrogenase genes RT in rice seeds."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=17210932; DOI=10.1101/gr.5509507; RG The rice annotation project (RAP); RT "Curated genome annotation of Oryza sativa ssp. japonica and RT comparative genome analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [5] RP PROTEIN SEQUENCE OF 2-11; 30-39 AND 140-149. RC STRAIN=cv. Nipponbare; RC TISSUE=Anther, Callus, Embryo, Panicle, and Stem; RX PubMed=14681440; DOI=10.1093/nar/gkh020; RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.; RT "Rice proteome database based on two-dimensional polyacrylamide gel RT electrophoresis: its status in 2003."; RL Nucleic Acids Res. 32:D388-D392(2004). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND PHOSPHORYLATION. RC STRAIN=cv. Nipponbare; RX PubMed=16028114; DOI=10.1007/s11103-005-4013-1; RA Khan M.M.K., Jan A., Karibe H., Komatsu S.; RT "Identification of phosphoproteins regulated by gibberellin in rice RT leaf sheath."; RL Plant Mol. Biol. 58:27-40(2005). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: By gibberellin. CC -!- PTM: Phosphorylated after gibberellin treatment. 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; EF122472; ABL74559.1; -; mRNA. DR EMBL; AP003886; BAD08850.1; -; Genomic_DNA. DR EMBL; AP008214; BAF22811.1; -; Genomic_DNA. DR EMBL; CM000145; EAZ41375.1; -; Genomic_DNA. DR RefSeq; NP_001060897.1; -. DR UniGene; Os.12168; -. DR HSSP; P56649; 1IHX. DR GeneID; 4344564; -. DR KEGG; osa:4344564; -. DR Gramene; Q42977; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:EC. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000173; GlycerAld_3-P_DH. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_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 Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase. FT INIT_MET 1 1 Removed. FT CHAIN 2 337 Glyceraldehyde-3-phosphate dehydrogenase, FT cytosolic. FT /FTId=PRO_0000145609. FT NP_BIND 13 14 NAD (By similarity). FT REGION 153 155 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 213 214 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 154 154 Nucleophile (By similarity). FT BINDING 35 35 NAD (By similarity). FT BINDING 82 82 NAD; via carbonyl oxygen (By similarity). FT BINDING 184 184 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 236 236 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 318 318 NAD (By similarity). FT SITE 181 181 Activates thiol group during catalysis FT (By similarity). SQ SEQUENCE 337 AA; 36413 MW; 3A8154CF7A06A603 CRC64; MGKIKIGING FGRIGRLVAR VALQSEDVEL VAVNDPFITT DYMTYMFKYD TVHGQWKHSD IKIKDSKTLL LGEKPVTVFG IRNPDEIPWA EAGAEYVVES TGVFTDKEKA AAHLKGGAKK VVISAPSKDA PMFVCGVNED KYTSDIDIVS NASCTTNCLA PLAKVIHDNF GIIEGLMTTV HAITATQKTV DGPSSKDWRG GRAASFNIIP SSTGAAKAVG KVLPDLNGKL TGMSFRVPTV DVSVVDLTVR IEKAASYDAI KSAIKSASEG KLKGIIGYVE EDLVSTDFVG DSRSSIFDAK AGIALNDNFV KLVAWYDNEW GYSNRVIDLI RHMAKTQ //