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P56221

- SCYD_MAGO7

UniProt

P56221 - SCYD_MAGO7

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Protein

Scytalone dehydratase

Gene

SDH1

Organism
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes two steps in melanin biosynthesis. From scytalone they are two dehydration steps and one reduction step to yield melanin.

Catalytic activityi

Scytalone = 1,3,8-trihydroxynaphthalene + H2O.

Pathwayi

GO - Molecular functioni

  1. scytalone dehydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. melanin biosynthetic process Source: UniProtKB-UniPathway
  2. mycelium development Source: PAMGO_MGG
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Melanin biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00785.

Names & Taxonomyi

Protein namesi
Recommended name:
Scytalone dehydratase (EC:4.2.1.94)
Gene namesi
Name:SDH1
ORF Names:MGG_05059
OrganismiMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Taxonomic identifieri242507 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe
ProteomesiUP000009058: Chromosome 3

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172Scytalone dehydratasePRO_0000097639Add
BLAST

Interactioni

Subunit structurei

Homotrimer. Each subunit contains an active site, located in the central part of the hydrophobic core of the monomer, which functions independently.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 3220Combined sources
Helixi35 – 395Combined sources
Beta strandi42 – 498Combined sources
Helixi51 – 544Combined sources
Beta strandi57 – 626Combined sources
Helixi63 – 719Combined sources
Turni73 – 764Combined sources
Beta strandi81 – 833Combined sources
Beta strandi86 – 9611Combined sources
Beta strandi99 – 11517Combined sources
Beta strandi121 – 13818Combined sources
Beta strandi141 – 15515Combined sources
Helixi158 – 1614Combined sources
Helixi163 – 1697Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP56221.
SMRiP56221. Positions 10-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56221.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG135608.
InParanoidiP56221.
KOiK17740.
OrthoDBiEOG7RV9TJ.

Family and domain databases

InterProiIPR004235. Scytalone_dehydratase.
[Graphical view]
PfamiPF02982. Scytalone_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF024851. SCD1. 1 hit.
ProDomiPD022193. Scytalone_dehydratase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P56221-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSQVQKSDE ITFSDYLGLM TCVYEWADSY DSKDWDRLRK VIAPTLRIDY
60 70 80 90 100
RSFLDKLWEA MPAEEFVGMV SSKQVLGDPT LRTQHFIGGT RWEKVSEDEV
110 120 130 140 150
IGYHQLRVPH QRYKDTTMKE VTMKGHAHSA NLHWYKKIDG VWKFAGLKPD
160 170
IRWGEFDFDR IFEDGRETFG DK
Length:172
Mass (Da):20,250
Last modified:July 15, 1998 - v1
Checksum:i2FA56296D5EE00DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004741 mRNA. Translation: BAA34046.1.
CM001233 Genomic DNA. Translation: EHA52765.1.
RefSeqiXP_003712572.1. XM_003712524.1.

Genome annotation databases

EnsemblFungiiMGG_05059T0; MGG_05059T0; MGG_05059.
GeneIDi2675492.
KEGGimgr:MGG_05059.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004741 mRNA. Translation: BAA34046.1 .
CM001233 Genomic DNA. Translation: EHA52765.1 .
RefSeqi XP_003712572.1. XM_003712524.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P56221.
SMRi P56221. Positions 10-172.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P56221.
ChEMBLi CHEMBL2578.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii MGG_05059T0 ; MGG_05059T0 ; MGG_05059 .
GeneIDi 2675492.
KEGGi mgr:MGG_05059.

Phylogenomic databases

eggNOGi NOG135608.
InParanoidi P56221.
KOi K17740.
OrthoDBi EOG7RV9TJ.

Enzyme and pathway databases

UniPathwayi UPA00785 .

Miscellaneous databases

EvolutionaryTracei P56221.

Family and domain databases

InterProi IPR004235. Scytalone_dehydratase.
[Graphical view ]
Pfami PF02982. Scytalone_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF024851. SCD1. 1 hit.
ProDomi PD022193. Scytalone_dehydratase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiSCYD_MAGO7
AccessioniPrimary (citable) accession number: P56221
Secondary accession number(s): A4QTI6, G4N445
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: October 29, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3