ID G3PC_PINSY Reviewed; 340 AA. AC P34924; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 25-NOV-2008, entry version 55. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; DE EC=1.2.1.12; GN Name=GAPC; OS Pinus sylvestris (Scots pine). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Coniferopsida; Coniferales; Pinaceae; Pinus; Pinus. OX NCBI_TaxID=3349; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93196483; PubMed=8095691; RA Martin W., Lydiate D., Brinkmann H., Forkmann G., Saedler H., RA Cerff R.; RT "Molecular phylogenies in angiosperm evolution."; RL Mol. Biol. Evol. 10:140-162(1993). 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; L07501; AAA33779.1; -; mRNA. DR PIR; T09663; T09663. DR HSSP; P00357; 4GPD. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro. DR GO; GO:0051287; F:NAD 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_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 ProDom; PD007761; GAPDH_like; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Glycolysis; NAD; Oxidoreductase. FT CHAIN 1 340 Glyceraldehyde-3-phosphate dehydrogenase, FT cytosolic. FT /FTId=PRO_0000145614. FT NP_BIND 16 17 NAD (By similarity). FT REGION 156 158 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 216 217 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 157 157 Nucleophile (By similarity). FT BINDING 38 38 NAD (By similarity). FT BINDING 85 85 NAD; via carbonyl oxygen (By similarity). FT BINDING 187 187 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 239 239 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 321 321 NAD (By similarity). FT SITE 184 184 Activates thiol group during catalysis FT (By similarity). SQ SEQUENCE 340 AA; 36530 MW; 1E81ACA460086F01 CRC64; MGSTGKIKIG INGFGRIGRL VARVALTRDD IELVGVNDPF ISTDYMSYMF KYDSVHGKWK HHEVNVKDSK TLLFGEKSVA VFGCRNPEEI PWGEVGAEYV VESTGVFTDK EKASAHLKAG AKKVVISAPS KDAPMFVVGV NEHQYKSDVN IVSNASCTTN CLAPLAKVIN DKFGIVEGLM TTVHSITATQ KTVDGPSNKD WRGGRGAGFN IIPSSTGAAK AVGKVLPALN GKLTGMAFRV PTPDVSVVDL TVRLEKSATY DEIKAAIKAE SEGNLKGILG YTEDAVVSTD FIGDSRSSIF DAQAGIALSD NFVKLVSWYD NEWGYSSRVV DLIVHMAATQ //