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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei30 – 301Substrate1 Publication
    Binding sitei50 – 501Substrate1 Publication
    Binding sitei53 – 531Substrate; via carbonyl oxygen1 Publication
    Active sitei85 – 8511 Publication
    Active sitei110 – 11011 Publication
    Binding sitei131 – 1311Substrate3 Publications

    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

    Keywords - Cellular componenti

    Endosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301Y → F: Results in a 9-fold decrease of activity with scytalone as the substrate and increases binding of salicylamide inhibitors. 2 Publications
    Mutagenesisi31 – 311D → N: Reduces catalysis 5000-fold and substrate affinity about 4-fold with scytalone as the substrate. 1 Publication
    Mutagenesisi50 – 501Y → F: Results in a 500-fold decrease of activity with scytalone as the substrate and increases binding of salicylamide inhibitors. 2 Publications
    Mutagenesisi53 – 531F → A: Leads to significantly higher relative substrate specificities (DDBO/vermelone). 1 Publication
    Mutagenesisi53 – 531F → L: Affects the binding of inhibitors and has significantly higher relative substrate specificities (DDBO/vermelone). 2 Publications
    Mutagenesisi69 – 691M → L: Affects the binding of inhibitors. 1 Publication
    Mutagenesisi75 – 751V → A: Affects the binding of inhibitors and reduces more than 200-fold inhibition by carpropamid. 2 Publications
    Mutagenesisi75 – 751V → M: Reduces strongly inhibition by carpropamid. 1 Publication
    Mutagenesisi85 – 851H → N: Greatly decreases catalytic efficiency and decreases binding to salicylamide inhibitors. 2 Publications
    Mutagenesisi110 – 1101H → 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 Publications
    Mutagenesisi129 – 1291S → A: Results in a 80-fold decrease of activity and a 7-fold increase in Km with scytalone as the substrate. 1 Publication
    Mutagenesisi129 – 1291S → T: Results in a 120-fold decrease of activity and a 23-fold increase in Km with scytalone as the substrate. 1 Publication
    Mutagenesisi131 – 1311N → 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 Publications
    Mutagenesisi158 – 1581F → L: Affects the binding of inhibitors. 1 Publication
    Mutagenesisi162 – 1621F → L: Affects the binding of inhibitors. 1 Publication

    Chemistry

    ChEMBLiCHEMBL2578.

    PTM / Processingi

    Molecule processing

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

    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

    BindingDBiP56221.

    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

    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
    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...

    Chemistry

    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: September 7, 2016
    This is version 102 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.