ID MTDH_AGABI STANDARD; PRT; 261 AA. AC O93868; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE NADP-dependent mannitol dehydrogenase (EC 1.1.1.138) (MtDH) (Mannitol DE 2-dehydrogenase [NADP+]). GN Name=mtdH; OS Agaricus bisporus (Common mushroom). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes; OC Agaricales; Agaricaceae; Agaricus. OX NCBI_TaxID=5341; RN [1] RP NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 1-19 AND 210-229, AND RP CHARACTERIZATION. RC STRAIN=Horst U1; RX MEDLINE=99054901; PubMed=9835550; RA Stoop J.M.H., Mooibroek H.; RT "Cloning and characterization of NADP-mannitol dehydrogenase cDNA from RT the button mushroom, Agaricus bisporus, and its expression in response RT to NaCl stress."; RL Appl. Environ. Microbiol. 64:4689-4696(1998). RN [2] RP PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS. RX PubMed=11320313; DOI=10.1107/S0907444901002542; RA Sassoon J., Hoerer S., Stoop J., Mooibroek H., Baumann U.; RT "Crystallization and preliminary crystallographic analysis of mannitol RT dehydrogenase (MtDH) from the common mushroom Agaricus bisporus."; RL Acta Crystallogr. D 57:711-713(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NADP, AND RP HOMOTETRAMERIZATION. RX PubMed=11335726; DOI=10.1074/jbc.M102850200; RA Horer S., Stoop J., Mooibroek H., Baumann U., Sassoon J.; RT "The crystallographic structure of the mannitol 2-dehydrogenase NADP+ RT binary complex from Agaricus bisporus."; RL J. Biol. Chem. 276:27555-27561(2001). CC -!- CATALYTIC ACTIVITY: D-mannitol + NADP(+) = D-fructose + NADPH. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) 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; AF053764; AAC79985.1; -. DR PDB; 1H5Q; X-ray; A/B/C/D/E/F/G/H/I/J/K/L=1-261. DR InterPro; IPR002198; ADH_short. DR InterPro; IPR002347; Adh_short_C2. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase. FT INIT_MET 0 0 FT NP_BIND 18 43 NADP. FT NP_BIND 149 173 NADP. FT ACT_SITE 168 168 Proton acceptor. FT BINDING 148 148 Substrate. FT STRAND 4 6 FT TURN 9 10 FT STRAND 11 16 FT TURN 17 19 FT HELIX 21 32 FT TURN 33 34 FT STRAND 35 41 FT TURN 45 46 FT HELIX 47 58 FT TURN 59 59 FT STRAND 62 66 FT TURN 69 70 FT HELIX 72 85 FT STRAND 89 94 FT HELIX 104 106 FT HELIX 109 119 FT TURN 120 120 FT HELIX 121 137 FT TURN 138 138 FT STRAND 141 146 FT HELIX 149 151 FT TURN 152 152 FT STRAND 156 158 FT TURN 159 160 FT STRAND 161 162 FT HELIX 166 186 FT HELIX 187 189 FT TURN 190 190 FT STRAND 191 198 FT STRAND 201 201 FT HELIX 204 208 FT HELIX 211 219 FT TURN 220 220 FT TURN 222 223 FT STRAND 227 227 FT HELIX 229 232 FT HELIX 233 240 FT HELIX 242 244 FT TURN 245 246 FT STRAND 251 254 FT TURN 256 257 FT HELIX 258 261 SQ SEQUENCE 261 AA; 27888 MW; D90C541720D647DC CRC64; APGFTISFVN KTIIVTGGNR GIGLAFTRAV AAAGANVAVI YRSAKDAVEV TEKVGKEFGV KTKAYQCDVS NTDIVTKTIQ QIDADLGAIS GLIANAGVSV VKPATELTHE DFKFVYDVNV FGVFNTCRAV AKLWLQKQQK GSIVVTSSMS SQIINQSSLN GSLTQVFYNS SKAACSNLVK GLAAEWASAG IRVNALSPGY VNTDQTAHMD KKIRDHQASN IPLNRFAQPE EMTGQAILLL SDHATYMTGG EYFIDGGQLI W //