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Q0CPB0

- KYNU1_ASPTN

UniProt

Q0CPB0 - KYNU1_ASPTN

Protein

Kynureninase 1

Gene

bna5-1

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (17 Oct 2006)
      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 sitei147 – 1471Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei148 – 1481Pyridoxal phosphateUniRule annotation
    Binding sitei232 – 2321Pyridoxal phosphateUniRule annotation
    Binding sitei261 – 2611Pyridoxal phosphateUniRule annotation
    Binding sitei264 – 2641Pyridoxal phosphateUniRule annotation
    Binding sitei286 – 2861Pyridoxal phosphateUniRule annotation
    Binding sitei326 – 3261Pyridoxal phosphateUniRule annotation
    Binding sitei354 – 3541Pyridoxal 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:
    Kynureninase 1UniRule annotation (EC:3.7.1.3UniRule annotation)
    Alternative name(s):
    Biosynthesis of nicotinic acid protein 5-1UniRule annotation
    L-kynurenine hydrolase 1UniRule annotation
    Gene namesi
    Name:bna5-1
    ORF Names:ATEG_04474
    OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
    Taxonomic identifieri341663 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000007963: 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 – 483483Kynureninase 1PRO_0000356971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei287 – 2871N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi33178.CADATEAP00009046.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0CPB0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni175 – 1784Pyridoxal phosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3844.
    HOGENOMiHOG000242438.
    OMAiGLMNDIV.
    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.

    Q0CPB0-1 [UniParc]FASTAAdd to Basket

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    MGSRLHLRDI KHGPPLPYHD DIRAFTKEYA ESLDAQDPLR KFRDEFIIPS    50
    KKDLKRTVLA ADENTDDSTD PRCIYLCGNS LGLQPRSTRK YIDRYLRTWA 100
    IKGVTGHFTP HDDQLLPPFV DVDVAGAKLM APVVGALESE VAVMDTLTTN 150
    LHLLMASFYR PTQERYKIII EGKAFPSDHY AVESQIRHHN REPSEAMVLI 200
    EPEDPKHPIL TTDQILRVID ENASSAALIL LSAIQFYTGQ YFDIKTITAH 250
    AQSKGIIVGW DCAHAAGNVD LQLHDWNVDF AAWCNYKYLN SGPGGMAGLF 300
    VHERHGHVES KNGAQNEGFR PRLSGWWGGD KETRFLMDNN FRPQVGAAGF 350
    QLSNPSVLDM NAVVASLEIF SRASMEKIRQ KSLHLTGYLE HLLVTYPLDA 400
    PPEEKPFTII TPSNPAERGA QLSLRLGPGL LEKVLEVLEE QGVIIDERKP 450
    DVIRVAPAPL YNTYAELSSS GIHIAYSSYN QYS 483
    Length:483
    Mass (Da):54,112
    Last modified:October 17, 2006 - v1
    Checksum:i6BCC62116EAB97BD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476599 Genomic DNA. Translation: EAU34921.1.
    RefSeqiXP_001213652.1. XM_001213652.1.

    Genome annotation databases

    EnsemblFungiiCADATEAT00009046; CADATEAP00009046; CADATEAG00009046.
    GeneIDi4320432.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476599 Genomic DNA. Translation: EAU34921.1 .
    RefSeqi XP_001213652.1. XM_001213652.1.

    3D structure databases

    ProteinModelPortali Q0CPB0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 33178.CADATEAP00009046.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADATEAT00009046 ; CADATEAP00009046 ; CADATEAG00009046 .
    GeneIDi 4320432.

    Phylogenomic databases

    eggNOGi COG3844.
    HOGENOMi HOG000242438.
    OMAi GLMNDIV.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NIH 2624 / FGSC A1156.

    Entry informationi

    Entry nameiKYNU1_ASPTN
    AccessioniPrimary (citable) accession number: Q0CPB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 45 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