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A7ESB8

- KYNU_SCLS1

UniProt

A7ESB8 - KYNU_SCLS1

Protein

Kynureninase

Gene

bna5

Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (11 Sep 2007)
      Previous versions | rss
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    • Comment

    Functioni

    Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.UniRule annotation

    Catalytic activityi

    L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
    L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

    Cofactori

    Pyridoxal phosphate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei141 – 1411Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei142 – 1421Pyridoxal phosphateUniRule annotation
    Binding sitei254 – 2541Pyridoxal phosphateUniRule annotation
    Binding sitei257 – 2571Pyridoxal phosphateUniRule annotation
    Binding sitei279 – 2791Pyridoxal phosphateUniRule annotation
    Binding sitei319 – 3191Pyridoxal phosphateUniRule annotation
    Binding sitei347 – 3471Pyridoxal phosphateUniRule annotation

    GO - Molecular functioni

    1. kynureninase activity Source: UniProtKB-HAMAP
    2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
    2. anthranilate metabolic process Source: UniProtKB-HAMAP
    3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
    4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
    5. tryptophan catabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00329.
    UPA00334; UER00455.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
    Alternative name(s):
    Biosynthesis of nicotinic acid protein 5UniRule annotation
    L-kynurenine hydrolaseUniRule annotation
    Gene namesi
    Name:bna5
    ORF Names:SS1G_08223
    OrganismiSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
    Taxonomic identifieri665079 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia
    ProteomesiUP000001312: Unassembled WGS sequence

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 475475KynureninasePRO_0000360872Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei280 – 2801N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi665079.A7ESB8.

    Structurei

    3D structure databases

    ProteinModelPortaliA7ESB8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni169 – 1724Pyridoxal phosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3844.
    KOiK01556.
    OMAiGWYGGDK.
    OrthoDBiEOG7V1G0J.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01970. Kynureninase.
    InterProiIPR000192. Aminotrans_V/Cys_dSase.
    IPR010111. Kynureninase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR14084. PTHR14084. 1 hit.
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038800. KYNU. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01814. kynureninase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A7ESB8-1 [UniParc]FASTAAdd to Basket

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    MGSIAKEEQP SKVEKPTFSS KANTLEYAQS LDANDHMRRF RDQFIIPSKA    50
    NIKATKLEKP GLSDESSIYF CGNSLGLQPK CVKEYLQAHL DTWSSIGVHG 100
    HFRDLEDSPL TQWQLLAEHA SKQCAPIVGA KASEVAMMGT LTTNLHLLMA 150
    SFYTPTPEKN KIIMEWKAFP SDHYAIESQI RGHGYNPQEA MVMIGPEEGS 200
    YEISTEKILR TIDEHASTTA LVLLPGIQYY TGQLFDVKTI TAYAQSKGLI 250
    VGWDLAHAAG NVPLQLHDWN VDFAVWCTYK YMNAGPGSIA GAFIHERHGE 300
    VDYSEGEEKP KYRHRLMGWY GGDQSCRFLM NNKFRPSPGA SGYQVSNPSV 350
    VDLTSLCAAL SIFNQTSMEE ISQKTLHLTA YLEHLLLTSN PSNTNPAFRI 400
    ITPSDPSARG TQLSVLLKPG RLETLSDMLE EAGIVADKRK PDVIRVAPVP 450
    LYNTYEDVWR FVQIFNAALE KCEEA 475
    Length:475
    Mass (Da):52,956
    Last modified:September 11, 2007 - v1
    Checksum:iDC42B2E8ED59B7C4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476631 Genomic DNA. Translation: EDN92360.1.
    RefSeqiXP_001590483.1. XM_001590433.1.

    Genome annotation databases

    EnsemblFungiiEDN92360; EDN92360; SS1G_08223.
    GeneIDi5486837.
    KEGGissl:SS1G_08223.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476631 Genomic DNA. Translation: EDN92360.1 .
    RefSeqi XP_001590483.1. XM_001590433.1.

    3D structure databases

    ProteinModelPortali A7ESB8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 665079.A7ESB8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EDN92360 ; EDN92360 ; SS1G_08223 .
    GeneIDi 5486837.
    KEGGi ssl:SS1G_08223.

    Phylogenomic databases

    eggNOGi COG3844.
    KOi K01556.
    OMAi GWYGGDK.
    OrthoDBi EOG7V1G0J.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_01970. Kynureninase.
    InterProi IPR000192. Aminotrans_V/Cys_dSase.
    IPR010111. Kynureninase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR14084. PTHR14084. 1 hit.
    Pfami PF00266. Aminotran_5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038800. KYNU. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01814. kynureninase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
      Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
      , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
      PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 18683 / 1980 / Ss-1.

    Entry informationi

    Entry nameiKYNU_SCLS1
    AccessioniPrimary (citable) accession number: A7ESB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 20, 2009
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 46 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

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3