ID G3P_SCHCO STANDARD; PRT; 337 AA. AC P32638; 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 (EC 1.2.1.12) (GAPDH). GN Name=GPD; OS Schizophyllum commune (Bracket fungus). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes; OC Agaricales; Schizophyllaceae; Schizophyllum. OX NCBI_TaxID=5334; RN [1] RP NUCLEOTIDE SEQUENCE. 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; M81724; AAA33926.1; -. DR PIR; S26973; S26973. DR HSSP; P56649; 1IHX. 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; NAD; Oxidoreductase. FT BINDING 151 151 Glyceraldehyde 3-phosphate. FT ACT_SITE 178 178 Activates thiol group during catalysis. SQ SEQUENCE 337 AA; 36055 MW; CBBCB4118F8F779B CRC64; MAVKVGINGF GRIGRIVLRN ALQLGNIEVV AINDPFIALD YMVYMFKYDT VHGRYKGTVE VKDGKLVVDG HAITVFAEKN PADIKWGSAG ADYIVESTGV FTTVEKASLH LQGGAKKVVI SAPSADAPMF VVGVNLDKYD SKYQVISNAS CTTNCLAPLA KVIHDKYGIA EGLMTTVHAT TATQKTVDGP SHKDWRGGRS VNNNIIPSST GAAKAVGKVI PSLNGRLTGL AFRVPTLDVS VVDLVVRLEK EASYDEIVAT VKEASEGPLK GILGFTDESV VSTDFTGANE SSIFDSKAGI AISKSFVKLI AWYDNEWGYS RRVCDLLVYA AKQDGAL //