ID G3P2_TRIKO STANDARD; PRT; 337 AA. AC P17730; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 2. DT 04-APR-2006, entry version 52. DE Glyceraldehyde-3-phosphate dehydrogenase 2 (EC 1.2.1.12) (GAPDH2). GN Name=gpd2; OS Trichoderma koningii. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea. OX NCBI_TaxID=55202; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=M3947; RX MEDLINE=93176825; PubMed=8439569; DOI=10.1016/0167-4781(93)90267-H; RA Watanabe H., Hasumi K., Fukushima Y., Sakai K., Endo A.; RT "Cloning of two isozymes of Trichoderma koningii RT glyceraldehyde-3-phosphate dehydrogenase with different sensitivity to RT koningic acid."; RL Biochim. Biophys. Acta 1172:43-48(1993). RN [2] RP PROTEIN SEQUENCE OF 1-31. RC STRAIN=M3947; RX MEDLINE=91031446; PubMed=2226438; RA Sakai K., Hasumi K., Endo A.; RT "Two glyceraldehyde-3-phosphate dehydrogenase isozymes from the RT koningic acid (heptelidic acid) producer Trichoderma koningii."; RL Eur. J. Biochem. 193:195-202(1990). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC -!- ENZYME REGULATION: Inhibited by koningic acid through the CC interaction of cysteine residues with koningic acid even at very CC low concentrations. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from CC D-glyceraldehyde 3-phosphate: step 1. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: This protein is a koningic acid (antibiotic)- CC sensitive GAPDH isozyme. It is present only when no antibiotic is CC produced. 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; D14518; BAA03391.1; -; mRNA. DR HSSP; P56649; 1CRW. DR InterPro; IPR000173; GAP_DH. DR InterPro; IPR006424; GAPDH_I. DR PANTHER; PTHR10836; GAP_dhdrogenase; 1. 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 Direct protein sequencing; Glycolysis; NAD; Oxidoreductase. FT INIT_MET 0 0 FT CHAIN 1 337 Glyceraldehyde-3-phosphate dehydrogenase FT 2. FT /FTId=PRO_0000145586. FT NP_BIND 12 13 NAD (By similarity). FT REGION 150 152 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 210 211 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 151 151 Nucleophile (By similarity). FT BINDING 34 34 NAD (By similarity). FT BINDING 79 79 NAD; via carbonyl oxygen (By similarity). FT BINDING 181 181 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 233 233 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 315 315 NAD (By similarity). FT SITE 178 178 Activates thiol group during catalysis FT (By similarity). FT CONFLICT 24 24 H -> K (in Ref. 2). FT CONFLICT 26 26 D -> N (in Ref. 2). SQ SEQUENCE 337 AA; 35975 MW; 098FA3C4BF56C615 CRC64; APIKVGINGF GRIGRIVFRN AVEHPDIEVV AVNDPFIETT YAAYMLKYDS SHGLFKGEVE VDGKDLVVNG KKVRFYTERN PADIKWSETG AEYVVESTGV FTTTEKAKAH LVGGAKKVII SAPSADAPMY VMGVNESDYD GSADVISNAS CTTNCLAPLA KVINDNYGIV EGLMTTVHSY TATQKTVDGP SAKDWRGGRG AAQNIIPSST GAAKAVGKVI PALNGKLTGM SIRVPTANVS VVDLTVRIEK GASYEEITET IKKAADGPLK GVLAYTGDDV VSSDMLGNTN SSIFDIKAGI SLNKNFVKLV SWYDNEWGYS RRVLDLLAHV AKVDASK //