Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A2S925

- KYNU_BURM9

UniProt

A2S925 - KYNU_BURM9

Protein

Kynureninase

Gene

kynU

Organism
Burkholderia mallei (strain NCTC 10229)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • 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 sitei97 – 971Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei98 – 981Pyridoxal phosphateUniRule annotation
    Binding sitei172 – 1721Pyridoxal phosphateUniRule annotation
    Binding sitei201 – 2011Pyridoxal phosphateUniRule annotation
    Binding sitei204 – 2041Pyridoxal phosphateUniRule annotation
    Binding sitei226 – 2261Pyridoxal phosphateUniRule annotation
    Binding sitei256 – 2561Pyridoxal phosphateUniRule annotation
    Binding sitei282 – 2821Pyridoxal 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

    BioCyciBMAL412022:GJI8-2486-MONOMER.
    UniPathwayiUPA00253; UER00329.
    UPA00334; UER00455.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
    Alternative name(s):
    L-kynurenine hydrolaseUniRule annotation
    Gene namesi
    Name:kynUUniRule annotation
    Ordered Locus Names:BMA10229_A2486
    OrganismiBurkholderia mallei (strain NCTC 10229)
    Taxonomic identifieri412022 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000002283: Chromosome I

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416KynureninasePRO_0000356996Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei227 – 2271N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi412022.BMA10229_A2486.

    Structurei

    3D structure databases

    ProteinModelPortaliA2S925.
    SMRiA2S925. Positions 3-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 1324Pyridoxal phosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3844.
    HOGENOMiHOG000242437.
    KOiK01556.
    OMAiVWDLAHS.
    OrthoDBiEOG6N67XP.

    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.

    A2S925-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTREEALAL DRDDPLAPLR EQFALPAGVI YLDGNSLGAQ PRAAAARAQQ    50
    VIGAEWGEGL IRSWNTAGWF ALPRRLGDRL APLIGAADDE VAITDTISIN 100
    LFKLLAAMLR HQARHAPKRR VIVSERSNFP TDLYIAQGLI AQLDRDYELR 150
    LIDDPADLPD ALDDETAVAM ITHVNYRTGY MHDMPSVTQT VRQAGALMLW 200
    DLAHSAGAVP VDLNGALADG AVGCTYKYLN GGPGSPAFVW VPKRHQRAFE 250
    QPLSGWWGHR APFAMQPAFE PDPGIARFLC GTQPIVSMSM VECGLDVFAQ 300
    TDMHAIRRKS LALTDAFVAL VESRCAGQPL KLVTPRAHHQ RGSQASFEHP 350
    HGYEVMQALI ARGVIGDYRE PRILRFGFTP LYTRFVDVWD AVETLRDILD 400
    TEAWRAPEFA TRAAVT 416
    Length:416
    Mass (Da):45,922
    Last modified:March 6, 2007 - v1
    Checksum:i35E6734AC426EE17
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000546 Genomic DNA. Translation: ABN01433.1.
    RefSeqiWP_004189663.1. NC_008836.1.
    YP_001028444.1. NC_008836.1.

    Genome annotation databases

    EnsemblBacteriaiABN01433; ABN01433; BMA10229_A2486.
    GeneIDi4791492.
    KEGGibml:BMA10229_A2486.
    PATRICi19135962. VBIBurMal46188_4684.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000546 Genomic DNA. Translation: ABN01433.1 .
    RefSeqi WP_004189663.1. NC_008836.1.
    YP_001028444.1. NC_008836.1.

    3D structure databases

    ProteinModelPortali A2S925.
    SMRi A2S925. Positions 3-404.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 412022.BMA10229_A2486.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN01433 ; ABN01433 ; BMA10229_A2486 .
    GeneIDi 4791492.
    KEGGi bml:BMA10229_A2486.
    PATRICi 19135962. VBIBurMal46188_4684.

    Phylogenomic databases

    eggNOGi COG3844.
    HOGENOMi HOG000242437.
    KOi K01556.
    OMAi VWDLAHS.
    OrthoDBi EOG6N67XP.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .
    BioCyci BMAL412022:GJI8-2486-MONOMER.

    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. DeShazer D., Woods D.E., Nierman W.C.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCTC 10229.

    Entry informationi

    Entry nameiKYNU_BURM9
    AccessioniPrimary (citable) accession number: A2S925
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 52 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

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

    External Data

    Dasty 3