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Q12634 (T4HR_MAGO7) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tetrahydroxynaphthalene reductase

EC=1.1.1.252
Alternative name(s):
T4HN reductase
Short name=THNR
Gene names
ORF Names:MGG_02252
OrganismMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) [Complete proteome]
Taxonomic identifier242507 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of 1,3,6,8-tetrahydroxynaphthalene (T4HN) into (+)-scytalone and 1,3,8-trihydroxynaphthalene into (-)-vermelone. This enzyme is the biochemical target of several commercially important fungicides which are used to prevent blast disease in rice plants.

Catalytic activity

Scytalone + NADP+ = 1,3,6,8-tetrahydroxynaphthalene + NADPH.

Pathway

Pigment biosynthesis; melanin biosynthesis.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processMelanin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processmelanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiontetrahydroxynaphthalene reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 283282Tetrahydroxynaphthalene reductase
PRO_0000054782

Regions

Nucleotide binding39 – 6325NADP

Sites

Active site1781Proton acceptor
Binding site1641Substrate

Secondary structure

............................................... 283
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12634 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E079638A96DF19CA

FASTA28330,054
        10         20         30         40         50         60 
MPAVTQPRGE SKYDAIPGPL GPQSASLEGK VALVTGAGRG IGREMAMELG RRGCKVIVNY 

        70         80         90        100        110        120 
ANSTESAEEV VAAIKKNGSD AACVKANVGV VEDIVRMFEE AVKIFGKLDI VCSNSGVVSF 

       130        140        150        160        170        180 
GHVKDVTPEE FDRVFTINTR GQFFVAREAY KHLEIGGRLI LMGSITGQAK AVPKHAVYSG 

       190        200        210        220        230        240 
SKGAIETFAR CMAIDMADKK ITVNVVAPGG IKTDMYHAVC REYIPNGENL SNEEVDEYAA 

       250        260        270        280 
SAWSPLHRVG LPIDIARVVC FLASNDGGWV TGKVIGIDGG ACM 

« Hide

References

« Hide 'large scale' references
[1]"Polyhydroxynaphthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Purification, cDNA cloning and sequencing."
Vidal-Cros A., Viviani F., Labesse G., Boccara M., Gaudry M.
Eur. J. Biochem. 219:985-992(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Strain: Guyane 11.
[2]"Isolation, characterization and preliminary genetic analysis of laboratory tricyclazole-resistant mutants of the rice blast fungus, Magnaporthe grisea."
Zhang C.-Q., Zhu G.N., Ma Z.H., Zhou M.-G.
J. Phytopathol. 154:392-397(2006) [AGRICOLA] [Europe PMC]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The genome sequence of the rice blast fungus Magnaporthe grisea."
Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M. expand/collapse author list , Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.
Nature 434:980-986(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 70-15 / ATCC MYA-4617 / FGSC 8958.
[4]"Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor."
Andersson A., Jordan D.B., Schneider G., Lindqvist Y.
Structure 4:1161-1170(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NADP AND INHIBITOR.
Strain: 4091-5-8.
[5]"Structures of trihydroxynaphthalene reductase-fungicide complexes: implications for structure-based design and catalysis."
Liao D.-I., Basarab G.S., Gatenby A.A., Valent B., Jordan D.B.
Structure 9:19-27(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP AND FUNGICIDE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L22309 mRNA. Translation: AAA19514.1.
AY846878 Genomic DNA. Translation: AAW55623.1.
CM001231 Genomic DNA. Translation: EHA56411.1.
PIRS41412.
RefSeqXP_003709023.1. XM_003708975.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DOHX-ray2.10A/B1-283[»]
1G0NX-ray2.00A/B1-283[»]
1G0OX-ray1.70A/B/C/D1-283[»]
1YBVX-ray2.80A/B1-283[»]
ProteinModelPortalQ12634.
SMRQ12634. Positions 3-283.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING148305.Q12634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiMGG_02252T0; MGG_02252T0; MGG_02252.
GeneID2681349.
KEGGmgr:MGG_02252.

Phylogenomic databases

eggNOGCOG1028.
KOK17739.
OrthoDBEOG75J0ZQ.

Enzyme and pathway databases

UniPathwayUPA00785.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ12634.

Entry information

Entry nameT4HR_MAGO7
AccessionPrimary (citable) accession number: Q12634
Secondary accession number(s): A4R3G6, G4MQ18, Q5I7G0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways