T4HR_MAGO7
ID T4HR_MAGO7 Reviewed; 283 AA.
AC Q12634; A4R3G6; G4MQ18; Q5I7G0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
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 oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC STRAIN=Guyane 11;
RX PubMed=8112349; 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 laboratory
RT tricyclazole-resistant mutants of the rice blast fungus, Magnaporthe
RT grisea.";
RL J. Phytopathol. 154:392-397(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / 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., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., 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 INHIBITOR.
RC STRAIN=4091-5-8;
RX 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-trihydroxynaphthalene
RT reductase from Magnaporthe grisea with NADPH and an active-site
RT inhibitor.";
RL Structure 4:1161-1170(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP AND 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 which
CC are used to prevent blast disease in rice plants.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + scytalone = H(+) + NADPH + naphthalene-1,3,6,8-
CC tetrol; Xref=Rhea:RHEA:21908, ChEBI:CHEBI:15378, ChEBI:CHEBI:16945,
CC ChEBI:CHEBI:18365, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.252;
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11342131,
CC ECO:0000269|PubMed:8939741}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; L22309; AAA19514.1; -; mRNA.
DR EMBL; AY846878; AAW55623.1; -; Genomic_DNA.
DR EMBL; CM001231; EHA56411.1; -; Genomic_DNA.
DR PIR; S41412; S41412.
DR RefSeq; XP_003709023.1; XM_003708975.1.
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=1-283.
DR PDBsum; 1DOH; -.
DR PDBsum; 1G0N; -.
DR PDBsum; 1G0O; -.
DR PDBsum; 1YBV; -.
DR AlphaFoldDB; Q12634; -.
DR SMR; Q12634; -.
DR STRING; 318829.MGG_02252T0; -.
DR EnsemblFungi; MGG_02252T0; MGG_02252T0; MGG_02252.
DR GeneID; 2681349; -.
DR KEGG; mgr:MGG_02252; -.
DR VEuPathDB; FungiDB:MGG_02252; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR InParanoid; Q12634; -.
DR OMA; HEHQPRV; -.
DR OrthoDB; 913128at2759; -.
DR BRENDA; 1.1.1.252; 5238.
DR BRENDA; 1.1.1.B57; 3152.
DR UniPathway; UPA00785; -.
DR EvolutionaryTrace; Q12634; -.
DR PHI-base; PHI:2022; -.
DR PHI-base; PHI:685; -.
DR Proteomes; UP000009058; Chromosome 1.
DR GO; GO:0047039; F:tetrahydroxynaphthalene reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Melanin biosynthesis; NADP;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..283
FT /note="Tetrahydroxynaphthalene reductase"
FT /id="PRO_0000054782"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11342131,
FT ECO:0000269|PubMed:8939741"
FT BINDING 39..63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11342131,
FT ECO:0000269|PubMed:8939741"
FT BINDING 164
FT /ligand="substrate"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1G0N"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:1G0O"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1G0O"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:1G0O"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:1G0O"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:1G0O"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:1G0O"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 176..196
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1G0O"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:1G0O"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 252..263
FT /evidence="ECO:0007829|PDB:1G0O"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1G0O"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1G0O"
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
