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P56221 (SCYD_MAGO7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 attributes

Sequence length172 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processMelanin biosynthesis
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processmelanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

mycelium development

Inferred from expression pattern PubMed 17156450. Source: PAMGO_MGG

   Molecular_functionscytalone dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172Scytalone dehydratase
PRO_0000097639

Secondary structure

............................ 172
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56221 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 2FA56296D5EE00DC

FASTA17220,250
        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 

« Hide

References

« Hide '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. 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.
[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.
RefSeqXP_003712572.1. XM_003712524.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IDPX-ray1.45A/B/C1-172[»]
1STDX-ray2.90A1-172[»]
2STDX-ray2.10A1-172[»]
3STDX-ray1.65A/B/C10-172[»]
4STDX-ray2.15A/B/C10-172[»]
5STDX-ray1.95A/B/C10-172[»]
6STDX-ray1.80A/B/C10-172[»]
7STDX-ray1.80A/B/C10-172[»]
ProteinModelPortalP56221.
SMRP56221. Positions 10-172.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP56221.
ChEMBLCHEMBL2578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiMGG_05059T0; MGG_05059T0; MGG_05059.
GeneID2675492.
KEGGmgr:MGG_05059.

Phylogenomic databases

eggNOGNOG135608.
KOK17740.
OrthoDBEOG7RV9TJ.

Enzyme and pathway databases

UniPathwayUPA00785.

Family and domain databases

InterProIPR004235. Scytalone_dehydratase.
[Graphical view]
PfamPF02982. Scytalone_dh. 1 hit.
[Graphical view]
PIRSFPIRSF024851. SCD1. 1 hit.
ProDomPD022193. Scytalone_dehydratase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP56221.

Entry information

Entry nameSCYD_MAGO7
AccessionPrimary (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: February 19, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways