ID G3PC_CRAPL Reviewed; 337 AA. AC Q42671; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 56. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; DE EC=1.2.1.12; GN Name=GAPC; OS Craterostigma plantagineum. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Lamiales; Linderniaceae; Craterostigma. OX NCBI_TaxID=4153; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RX MEDLINE=95036031; PubMed=7948905; DOI=10.1007/BF00039567; RA Velasco R., Salamini F., Bartels D.; RT "Dehydration and ABA increase mRNA levels and enzyme activity of RT cytosolic GAPDH in the resurrection plant Craterostigma RT plantagineum."; RL Plant Mol. Biol. 26:541-546(1994). 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 -!- 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; X78307; CAA55116.1; -; mRNA. DR PIR; S42479; S42479. DR HSSP; P56649; 1IHX. DR BRENDA; 1.2.1.12; 280962. 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 2: Evidence at transcript level; KW Cytoplasm; Glycolysis; NAD; Oxidoreductase. FT CHAIN 1 337 Glyceraldehyde-3-phosphate dehydrogenase, FT cytosolic. FT /FTId=PRO_0000145598. 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; 36477 MW; BF73D81E417580E5 CRC64; MAKVKIGING FGRIGRLVAR VALVRDDVEL VAVNDPFITV DYMAYMFKYD TVHGQYKHHE LKVKDEKTLL FGDKPVAVFG LRNPEEIPWA ETGAEYVVES TGVFTEKEKA AAHLKGGAKK VIISAPSKDA PMFVVGVNEK TYTPDIDVVS NASCTTNCLA PLAKVIHDRF GIVEGLMTTV HSITATQKTV DGPSSKDWRG GRAASFNIIP SSTGAAKAVG KVLPDLNGKL TGMAFRVPTV DVSVVDLTVT LAKEASYDEI KAAIKEESEG KLKGILGYTE EDVVSSDFVG DSRSSIFDAK AGIALSKKFV KIVAWYDNEW GYSSRVVDLI RHMAAAK //