ID T4HR_MAGGR Reviewed; 283 AA. AC Q12634; A4R3G6; Q5I7G0; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 16-JUN-2009, entry version 72. DE RecName: Full=Tetrahydroxynaphthalene reductase; DE EC=1.1.1.252; DE AltName: Full=T4HN reductase; DE Short=THNR; GN ORFNames=MGG_02252; OS Magnaporthe grisea (Rice blast fungus) (Pyricularia grisea). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Magnaporthales; Magnaporthaceae; OC Magnaporthe. OX NCBI_TaxID=148305; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND RP CHARACTERIZATION. RC STRAIN=Guyane 11; RX MEDLINE=94155906; PubMed=8112349; RX DOI=10.1111/j.1432-1033.1994.tb18581.x; RA Vidal-Cros A., Viviani F., Labesse G., Boccara M., Gaudry M.; RT "Polyhydroxynaphthalene reductase involved in melanin biosynthesis in RT Magnaporthe grisea. Purification, cDNA cloning and sequencing."; RL Eur. J. Biochem. 219:985-992(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX AGRICOLA=IND43821857; DOI=10.1111/j.1439-0434.2006.01111.x; RA Zhang C.-Q., Zhu G.N., Ma Z.H., Zhou M.-G.; RT "Isolation, characterization and preliminary genetic analysis of RT laboratory tricyclazole-resistant mutants of the rice blast fungus, RT Magnaporthe grisea."; RL J. Phytopathol. 154:392-397(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70-15 / FGSC 8958; RX PubMed=15846337; DOI=10.1038/nature03449; RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., RA Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., RA Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., RA Birren B.W.; RT "The genome sequence of the rice blast fungus Magnaporthe grisea."; RL Nature 434:980-986(2005). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NADP AND RP INHIBITOR. RC STRAIN=4091-5-8; RX MEDLINE=97094973; PubMed=8939741; DOI=10.1016/S0969-2126(96)00124-4; RA Andersson A., Jordan D.B., Schneider G., Lindqvist Y.; RT "Crystal structure of the ternary complex of 1,3,8- RT trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and RT an active-site inhibitor."; RL Structure 4:1161-1170(1996). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP AND RP FUNGICIDE. RX PubMed=11342131; DOI=10.1016/S0969-2126(00)00548-7; RA Liao D.-I., Basarab G.S., Gatenby A.A., Valent B., Jordan D.B.; RT "Structures of trihydroxynaphthalene reductase-fungicide complexes: RT implications for structure-based design and catalysis."; RL Structure 9:19-27(2001). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 1,3,6,8- CC tetrahydroxynaphthalene (T4HN) into (+)-scytalone and 1,3,8- CC trihydroxynaphthalene into (-)-vermelone. This enzyme is the CC biochemical target of several commercially important fungicides CC which are used to prevent blast disease in rice plants. CC -!- CATALYTIC ACTIVITY: Scytalone + NADP(+) = 1,3,6,8- CC tetrahydroxynaphthalene + NADPH. CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) 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; L22309; AAA19514.1; -; mRNA. DR EMBL; AY846878; AAW55623.1; -; Genomic_DNA. DR EMBL; CH476830; EDJ98831.1; -; Genomic_DNA. DR PIR; S41412; S41412. DR RefSeq; XP_365550.1; -. DR UniGene; Mgr.5801; -. DR PDB; 1DOH; X-ray; 2.10 A; A/B=1-283. DR PDB; 1G0N; X-ray; 2.00 A; A/B=1-283. DR PDB; 1G0O; X-ray; 1.70 A; A/B/C/D=1-283. DR PDB; 1YBV; X-ray; 2.80 A; A/B=3-283. DR PDBsum; 1DOH; -. DR PDBsum; 1G0N; -. DR PDBsum; 1G0O; -. DR PDBsum; 1YBV; -. DR GeneID; 2681349; -. DR KEGG; mgr:MGG_02252; -. DR NMPDR; fig|242507.1.peg.7289; -. DR OMA; Q12634; DIARVVC. DR BRENDA; 1.1.1.252; 5953. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0047039; F:tetrahydroxynaphthalene reductase activity; IEA:EC. DR GO; GO:0006583; P:melanin biosynthetic process from tyrosine; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR19410; ADH_short_C2; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Melanin biosynthesis; NADP; Oxidoreductase. FT INIT_MET 1 1 Removed. FT CHAIN 2 283 Tetrahydroxynaphthalene reductase. FT /FTId=PRO_0000054782. FT NP_BIND 39 63 NADP. FT ACT_SITE 178 178 Proton acceptor. FT BINDING 164 164 Substrate. FT HELIX 12 14 FT HELIX 21 25 FT STRAND 31 34 FT TURN 35 38 FT HELIX 40 51 FT STRAND 55 62 FT HELIX 64 76 FT STRAND 81 85 FT HELIX 91 105 FT STRAND 108 113 FT HELIX 123 125 FT HELIX 128 138 FT HELIX 140 152 FT STRAND 153 162 FT HELIX 165 167 FT HELIX 176 195 FT HELIX 196 199 FT STRAND 202 208 FT HELIX 214 219 FT HELIX 220 223 FT HELIX 232 242 FT HELIX 252 263 FT HELIX 265 267 FT STRAND 274 280 SQ SEQUENCE 283 AA; 30054 MW; E079638A96DF19CA CRC64; MPAVTQPRGE SKYDAIPGPL GPQSASLEGK VALVTGAGRG IGREMAMELG RRGCKVIVNY ANSTESAEEV VAAIKKNGSD AACVKANVGV VEDIVRMFEE AVKIFGKLDI VCSNSGVVSF GHVKDVTPEE FDRVFTINTR GQFFVAREAY KHLEIGGRLI LMGSITGQAK AVPKHAVYSG SKGAIETFAR CMAIDMADKK ITVNVVAPGG IKTDMYHAVC REYIPNGENL SNEEVDEYAA SAWSPLHRVG LPIDIARVVC FLASNDGGWV TGKVIGIDGG ACM //