P56221 (SCYD_MAGO7) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Scytalone dehydratase
EC=4.2.1.94

Gene names

Name:	SDH1
ORF Names:	MGG_05059

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	172 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes two steps in melanin biosynthesis. From scytalone they are two dehydration steps and one reduction step to yield melanin.
Catalytic activity	Scytalone = 1,3,8-trihydroxynaphthalene + H2O.
Pathway	Pigment biosynthesis; melanin biosynthesis.
Subunit structure	Homotrimer. Each subunit contains an active site, located in the central part of the hydrophobic core of the monomer, which functions independently.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway mycelium development Inferred from expression pattern PubMed 17156450. Source: PAMGO_MGG
Molecular_function	scytalone dehydratase 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

Chain

1 – 172

172

Scytalone dehydratase

PRO_0000097639

Secondary structure

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172

Helix Strand Turn

Details...

Helix

13 – 32

20

Helix

35 – 39

5

Beta strand

42 – 49

8

Helix

51 – 54

4

Beta strand

57 – 62

6

Helix

63 – 71

9

Turn

73 – 76

4

Beta strand

81 – 83

3

Beta strand

86 – 96

11

Beta strand

99 – 115

17

Beta strand

121 – 138

18

Beta strand

141 – 155

15

Helix

158 – 161

4

Helix

163 – 169

7

Sequences

	Sequence		Length	Mass (Da)
	P56221 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: 2FA56296D5EE00DC	FASTA	172	20,250
	10 20 30 40 50 60 MGSQVQKSDE ITFSDYLGLM TCVYEWADSY DSKDWDRLRK VIAPTLRIDY RSFLDKLWEA 70 80 90 100 110 120 MPAEEFVGMV SSKQVLGDPT LRTQHFIGGT RWEKVSEDEV IGYHQLRVPH QRYKDTTMKE 130 140 150 160 170 VTMKGHAHSA NLHWYKKIDG VWKFAGLKPD IRWGEFDFDR IFEDGRETFG DK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, expression, and mutagenesis of scytalone dehydratase needed for pathogenicity of the rice blast fungus, Pyricularia oryzae." Motoyama T., Imanishi K., Yamaguchi I. Biosci. Biotechnol. Biochem. 62:564-566(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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.
[3]	"Crystal structure of scytalone dehydratase -- a disease determinant of the rice pathogen, Magnaporthe grisea." Lundqvist T., Rice J., Hodge C.N., Basarab G.S., Pierce J., Lindqvist Y. Structure 2:937-944(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[4]	"Cryogenic X-ray crystal structure analysis for the complex of scytalone dehydratase of a rice blast fungus and its tight-binding inhibitor, carpropamid: the structural basis of tight-binding inhibition." Nakasako M., Motoyama T., Kurahashi Y., Yamaguchi I. Biochemistry 37:9931-9939(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[5]	"Structure-based design of potent inhibitors of scytalone dehydratase: displacement of a water molecule from the active site." Chen J.M., Xu S.L., Wawrzak Z., Basarab G.S., Jordan D.B. Biochemistry 37:17735-17744(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[6]	"High-resolution structures of scytalone dehydratase-inhibitor complexes crystallized at physiological pH." Wawrzak Z., Sandalova T., Steffens J.J., Basarab G.S., Lundqvist T., Lindqvist Y., Jordan D.B. Proteins 35:425-439(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB004741 mRNA. Translation: BAA34046.1.
CM001233 Genomic DNA. Translation: EHA52765.1.

RefSeq

XP_003712572.1. XM_003712524.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IDP	X-ray	1.45	A/B/C	1-172	[»]
1STD	X-ray	2.90	A	1-172	[»]
2STD	X-ray	2.10	A	1-172	[»]
3STD	X-ray	1.65	A/B/C	10-172	[»]
4STD	X-ray	2.15	A/B/C	10-172	[»]
5STD	X-ray	1.95	A/B/C	10-172	[»]
6STD	X-ray	1.80	A/B/C	10-172	[»]
7STD	X-ray	1.80	A/B/C	10-172	[»]

ProteinModelPortal

P56221.

SMR

P56221. Positions 10-172.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

MGG_05059T0; MGG_05059T0; MGG_05059.

GeneID

2675492.

KEGG

mgr:MGG_05059.

Phylogenomic databases

eggNOG

NOG135608.

OrthoDB

EOG4WHCWB.

Enzyme and pathway databases

UniPathway

UPA00785.

Family and domain databases

InterPro

IPR004235. Scytalone_dehydratase.
[Graphical view]

Pfam

PF02982. Scytalone_dh. 1 hit.
[Graphical view]

PIRSF

PIRSF024851. SCD1. 1 hit.

ProDom

PD022193. Scytalone_dehydratase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Other

BindingDB

P56221.

ChEMBL

CHEMBL2578.

EvolutionaryTrace

P56221.

Entry information

Entry name

SCYD_MAGO7

Accession

Primary (citable) accession number: P56221
Secondary accession number(s): A4QTI6, G4N445

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program