Q12634 (T4HR_MAGO7) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tetrahydroxynaphthalene reductase
EC=1.1.1.252

Alternative name(s):
T4HN reductase
Short name=THNR

Gene names

ORF Names:

MGG_02252

Organism

Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) [Complete proteome]

Taxonomic identifier

242507 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Magnaporthales › Magnaporthaceae › Magnaporthe › Magnaporthe oryzae

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Melanin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro tetrahydroxynaphthalene reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 283

282

Tetrahydroxynaphthalene reductase

PRO_0000054782

Regions

Nucleotide binding

39 – 63

25

NADP

Sites

Active site

178

1

Proton acceptor

Binding site

164

1

Substrate

Secondary structure

1

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283

Helix Strand Turn

Details...

Helix

12 – 14

3

Helix

22 – 25

4

Beta strand

31 – 34

4

Turn

35 – 38

4

Helix

40 – 51

12

Beta strand

55 – 62

8

Helix

64 – 76

13

Beta strand

81 – 85

5

Helix

91 – 105

15

Beta strand

110 – 113

4

Helix

123 – 125

3

Helix

128 – 138

11

Helix

140 – 152

13

Beta strand

158 – 162

5

Helix

165 – 167

3

Helix

176 – 196

21

Helix

197 – 199

3

Beta strand

202 – 208

7

Beta strand

211 – 213

3

Helix

214 – 219

6

Helix

220 – 223

4

Helix

232 – 242

11

Helix

252 – 263

12

Helix

265 – 267

3

Beta strand

274 – 278

5

Sequences

	Sequence		Length	Mass (Da)
	Q12634 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E079638A96DF19CA	FASTA	283	30,054
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

S41412.

RefSeq

XP_003709023.1. XM_003708975.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DOH	X-ray	2.10	A/B	1-283	[»]
1G0N	X-ray	2.00	A/B	1-283	[»]
1G0O	X-ray	1.70	A/B/C/D	1-283	[»]
1YBV	X-ray	2.80	A/B	3-283	[»]

ProteinModelPortal

Q12634.

SMR

Q12634. Positions 3-283.

ModBase

Search...

Protein-protein interaction databases

STRING

148305.Q12634.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

MGG_02252T0; MGG_02252T0; MGG_02252.

GeneID

2681349.

KEGG

mgr:MGG_02252.

Phylogenomic databases

eggNOG

COG1028.

KO

K00059.

OrthoDB

EOG4HX88X.

Enzyme and pathway databases

UniPathway

UPA00785.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q12634.

Entry information

Entry name

T4HR_MAGO7

Accession

Primary (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:	April 3, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program