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Q12634 (T4HR_MAGO7) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. 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

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: 8112349] [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: IND43821857]
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: 15846337] [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: 8939741] [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: 11342131] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP AND FUNGICIDE.
+Additional computationally mapped references.

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_365550.1. XM_365550.1.

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/B3-283[»]
ProteinModelPortalQ12634.
SMRQ12634. Positions 3-283.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2681349.
KEGGmgr:MGG_02252.
NMPDRfig|242507.1.peg.7289.

Phylogenomic databases

OrthoDBEOG4HX88X.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00059.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families