ID G3PC_HORVU Reviewed; 305 AA. AC P08477; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 16-JUN-2009, entry version 67. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; DE EC=1.2.1.12; DE Flags: Fragment; GN Name=GAPC; OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Triticeae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Chojecki J.; RT "Identification and characterisation of a cDNA clone for cytosolic RT glyceraldehyde-3-phosphate dehydrogenase in barley."; RL Carlsberg Res. Commun. 51:203-210(1986). 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; M36650; AAA32956.1; -; mRNA. DR PIR; A24159; A24159. DR UniGene; Hv.9630; -. DR HSSP; P56649; 1DSS. DR Gramene; P08477; -. DR BRENDA; 1.2.1.12; 283. 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; PARTIAL. PE 2: Evidence at transcript level; KW Cytoplasm; Glycolysis; NAD; Oxidoreductase. FT CHAIN <1 305 Glyceraldehyde-3-phosphate dehydrogenase, FT cytosolic. FT /FTId=PRO_0000145603. FT REGION 121 123 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 181 182 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 122 122 Nucleophile (By similarity). FT BINDING 3 3 NAD (By similarity). FT BINDING 50 50 NAD; via carbonyl oxygen (By similarity). FT BINDING 152 152 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 204 204 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 286 286 NAD (By similarity). FT SITE 149 149 Activates thiol group during catalysis FT (By similarity). FT NON_TER 1 1 SQ SEQUENCE 305 AA; 33236 MW; 4F82FA362F222AC5 CRC64; VNDPFITTDY MTYMFKYDTV HGQWKHHEVK VKDSKTLLFG EKEVAVFGCR NPEEIPWAAA GAEYVVESTG VFTDKDKAAA HIKGGAKKVI ISAPSKDAPM FVCGVNEKEY KSDIDIVSNA SCTTNCPAPL AKVINDRFGI VEGLMTTVHA MTATQKTVDG PSSKDWRGGR AASFNIIPSS TGAAKAVGKV LPELNGKLTG MAFRVPTVDV SVVDLTVRLA KPATYEQIKA AIKEESEGNL KGILGYVDED LVSTDFQGDS RSSIFDAKAG IALNDNFVKL VSWYDNEWGY STRVVDLIRH MHSTK //