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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Scytalone dehydratase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:9571787). Within the pathway, catalyzes the dehydration of scytalone as well as of vermelone (PubMed:9571787, PubMed:9466791, PubMed:9466792, PubMed:9539706, PubMed:10320327, PubMed:10386945, PubMed:10386946, PubMed:10694394, PubMed:10913266, PubMed:10636235, PubMed:11790103, PubMed:12413868, PubMed:15056895). Is also able to dehydrate the alternate substrate 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one (DDBO) to 5-hydroxy-4H-1-benzopyran-4-one (HBO) (PubMed:9466791, PubMed:9466792, PubMed:10320327, PubMed:10386945, PubMed:11790103).13 Publications

Catalytic activityi

Scytalone = 1,3,8-trihydroxynaphthalene + H2O.13 Publications

Enzyme regulationi

(N-phenoxypropyl)-carboxamides such as carpropamid and derivatives of norephedrine act as inhibitors of scytalone dehydratase activity.6 Publications

Kineticsi

  1. KM=15 µM for 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one (DDBO)2 Publications
  2. KM=33 µM for scytalone1 Publication
  3. KM=31 µM for vermelone2 Publications

    Pathwayi: melanin biosynthesis

    This protein is involved in the pathway melanin biosynthesis, which is part of Pigment biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway melanin biosynthesis and in Pigment biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei30Substrate1 Publication1
    Binding sitei50Substrate1 Publication1
    Binding sitei53Substrate; via carbonyl oxygen1 Publication1
    Active sitei851 Publication1
    Active sitei1101 Publication1
    Binding sitei131Substrate3 Publications1

    GO - Molecular functioni

    GO - Biological processi

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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Melanin biosynthesis

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi4.2.1.94. 3152.
    UniPathwayiUPA00785.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Scytalone dehydratase1 Publication (EC:4.2.1.946 Publications)
    Short name:
    SD1 Publication
    Short name:
    SDH1 Publication
    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
    Proteomesi
    • UP000009058 Componenti: Chromosome 3

    Organism-specific databases

    EuPathDBiFungiDB:MGG_05059.

    Subcellular locationi

    • Endosome By similarity

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi30Y → F: Results in a 9-fold decrease of activity with scytalone as the substrate and increases binding of salicylamide inhibitors. 2 Publications1
    Mutagenesisi31D → N: Reduces catalysis 5000-fold and substrate affinity about 4-fold with scytalone as the substrate. 1 Publication1
    Mutagenesisi50Y → F: Results in a 500-fold decrease of activity with scytalone as the substrate and increases binding of salicylamide inhibitors. 2 Publications1
    Mutagenesisi53F → A: Leads to significantly higher relative substrate specificities (DDBO/vermelone). 1 Publication1
    Mutagenesisi53F → L: Affects the binding of inhibitors and has significantly higher relative substrate specificities (DDBO/vermelone). 2 Publications1
    Mutagenesisi69M → L: Affects the binding of inhibitors. 1 Publication1
    Mutagenesisi75V → A: Affects the binding of inhibitors and reduces more than 200-fold inhibition by carpropamid. 2 Publications1
    Mutagenesisi75V → M: Reduces strongly inhibition by carpropamid. 1 Publication1
    Mutagenesisi85H → N: Greatly decreases catalytic efficiency and decreases binding to salicylamide inhibitors. 2 Publications1
    Mutagenesisi110H → N: Causes a 250-fold decrease of activity and a 6-fold increase in Km with scytalone as the substrate, decreases binding of salicylamide inhibitors, and has significantly higher relative substrate specificities (DDBO/vermelone). 3 Publications1
    Mutagenesisi129S → A: Results in a 80-fold decrease of activity and a 7-fold increase in Km with scytalone as the substrate. 1 Publication1
    Mutagenesisi129S → T: Results in a 120-fold decrease of activity and a 23-fold increase in Km with scytalone as the substrate. 1 Publication1
    Mutagenesisi131N → A: Decreases turnover by nearly 90-fold and increases Km 8-fold with scytalone as the substrate, decreases strongly binding of salicylamide inhibitors, and has significantly higher relative substrate specificities (DDBO/vermelone). 3 Publications1
    Mutagenesisi158F → L: Affects the binding of inhibitors. 1 Publication1
    Mutagenesisi162F → L: Affects the binding of inhibitors. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL2578.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000976391 – 172Scytalone dehydrataseAdd BLAST172

    Expressioni

    Inductioni

    Expression is induced in the stationary phase, when melanin synthesis occurs (PubMed:9571787). Expression is specifically induced during appressorium formation (PubMed:15378734).2 Publications

    Interactioni

    Subunit structurei

    Homotrimer (PubMed:7866745). Each subunit contains an active site, located in the central part of the hydrophobic core of the monomer, which functions independently (PubMed:7866745).1 Publication

    Chemistry databases

    BindingDBiP56221.

    Structurei

    Secondary structure

    1172
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi13 – 32Combined sources20
    Helixi35 – 39Combined sources5
    Beta strandi42 – 49Combined sources8
    Helixi51 – 54Combined sources4
    Beta strandi57 – 62Combined sources6
    Helixi63 – 71Combined sources9
    Turni73 – 76Combined sources4
    Beta strandi81 – 83Combined sources3
    Beta strandi86 – 96Combined sources11
    Beta strandi99 – 115Combined sources17
    Beta strandi121 – 138Combined sources18
    Beta strandi141 – 155Combined sources15
    Helixi158 – 161Combined sources4
    Helixi163 – 169Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56221.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the scytalone dehydratase family.Curated

    Phylogenomic databases

    InParanoidiP56221.
    KOiK17740.
    OrthoDBiEOG092C4YYV.

    Family and domain databases

    Gene3Di3.10.450.50. 1 hit.
    InterProiIPR032710. NTF2-like_dom.
    IPR004235. 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]
    SUPFAMiSSF54427. SSF54427. 1 hit.

    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.
    RefSeqiXP_003712572.1. XM_003712524.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiP56221.
    ChEMBLiCHEMBL2578.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    EuPathDBiFungiDB:MGG_05059.

    Phylogenomic databases

    InParanoidiP56221.
    KOiK17740.
    OrthoDBiEOG092C4YYV.

    Enzyme and pathway databases

    UniPathwayiUPA00785.
    BRENDAi4.2.1.94. 3152.

    Miscellaneous databases

    EvolutionaryTraceiP56221.
    PROiP56221.

    Family and domain databases

    Gene3Di3.10.450.50. 1 hit.
    InterProiIPR032710. NTF2-like_dom.
    IPR004235. 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]
    SUPFAMiSSF54427. SSF54427. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 104 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, Direct protein sequencing, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.