ID G3P2_AGABI STANDARD; PRT; 338 AA. AC P32636; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Glyceraldehyde-3-phosphate dehydrogenase 2 (EC 1.2.1.12) (GAPDH 2). GN Name=gpd2; OS Agaricus bisporus (Common mushroom). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes; OC Agaricales; Agaricaceae; Agaricus. OX NCBI_TaxID=5341; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Horst U3; RX MEDLINE=93113715; PubMed=1473176; RA Harmsen M.C., Schuren F.H.J., Moukha S.M., van Zuilen C.M., Punt P.J., RA Wessels J.G.H.; RT "Sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase RT genes from the basidiomycetes Schizophyllum commune, Phanerochaete RT chrysosporium and Agaricus bisporus."; RL Curr. Genet. 22:447-454(1992). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC -!- PATHWAY: Second phase of glycolysis; first step. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; M81728; AAA32634.1; -. DR PIR; S26976; S26976. DR HSSP; P00357; 4GPD. DR InterPro; IPR000173; GAP_dhdrogenase. DR InterPro; IPR006424; GAPDH-I. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Multigene family; NAD; Oxidoreductase. FT BINDING 150 150 Glyceraldehyde 3-phosphate. FT ACT_SITE 177 177 Activates thiol group during catalysis. SQ SEQUENCE 338 AA; 36570 MW; 3381DBBF73B84469 CRC64; MVKVGINGFG RIGRIVLRNA LQFQDIEVVA VNDPFIDLEY MAYMFKYDSV HGRFKGTVEV KNGSFVVDGR PMKVFAERDP AAIPWGSVGA DYVVESTGVF TTIDKASAHL KGGAKKVVIS APSADAPMYV CGVNLDKYNP KDTIISNASC TTNCLATLAK VIHDNFGIVE GLMTTVHATT ATQKTVDGPS HKDWRGGRGV GNNIIPSSTG AAKAVGKVIP SLNGKLTGLS MRVPTQDVSV VDLVVRLEKP ASYEQIKEVM RKAAEGEYKG IIAYTDEDVV STDFISDNNS CVFDAKAGIQ LSPNFVKLIA WYDNEWGYSR RVCNLLQYVA KEDAKAGI //