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A4IT57

- KYNU_GEOTN

UniProt

A4IT57 - KYNU_GEOTN

Protein

Kynureninase

Gene

kynU

Organism
Geobacillus thermodenitrificans (strain NG80-2)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      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 sitei104 – 1041Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei105 – 1051Pyridoxal phosphateUniRule annotation
    Binding sitei213 – 2131Pyridoxal phosphateUniRule annotation
    Binding sitei216 – 2161Pyridoxal phosphateUniRule annotation
    Binding sitei238 – 2381Pyridoxal phosphateUniRule annotation
    Binding sitei267 – 2671Pyridoxal phosphateUniRule annotation
    Binding sitei295 – 2951Pyridoxal 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

    BioCyciGTHE420246:GIXT-3262-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:GTNG_3166
    OrganismiGeobacillus thermodenitrificans (strain NG80-2)
    Taxonomic identifieri420246 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
    ProteomesiUP000001578: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428KynureninasePRO_0000357007Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei239 – 2391N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi420246.GTNG_3166.

    Structurei

    3D structure databases

    ProteinModelPortaliA4IT57.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni132 – 1354Pyridoxal phosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3844.
    HOGENOMiHOG000242438.
    KOiK01556.
    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.

    A4IT57-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSTALEPTL EFARKLDQED PLRHFRDEFY LPPNSIYMDG NSLGLLSKRA    50
    EKTLFTILQD WKLLGIDGWT KGTYPWFDLS EKIGAMLAPL VGASPEEVIA 100
    TGSTTVNLHQ LVSTFYQPEG KRTKILADEL TFPSDIYALQ SQLRIHGYDP 150
    STHLIRVKSR DGRFLEEEDI IAAMSEDVAL VVLPTVLYRS GQILDIQLLT 200
    DEAHKRGILI GFDACHSIGA IPHSFSEWGV DFAFWCNYKY MNGGPGCVAG 250
    LYVHRKHFGS APGLAGWFGS KKDKQFDMEH TFTPSLTAGA YQIGTPHLLS 300
    LAPLIGSLEI FQEAGIERIR QKSLQLTNYF MYLIEQELSH FGFIIGNPKD 350
    DVRRGGHISL EHEEAARICK SLKENGVIPD FRAPNIIRLA PIALYTSYEE 400
    VWNVVQIMKK IMQEKQYKKF SNEREVVA 428
    Length:428
    Mass (Da):48,333
    Last modified:December 16, 2008 - v2
    Checksum:i19579C1F454D452B
    GO

    Sequence cautioni

    The sequence ABO68511.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000557 Genomic DNA. Translation: ABO68511.1. Different initiation.
    RefSeqiYP_001127256.1. NC_009328.1.

    Genome annotation databases

    EnsemblBacteriaiABO68511; ABO68511; GTNG_3166.
    GeneIDi4968092.
    KEGGigtn:GTNG_3166.
    PATRICi21982971. VBIGeoThe136879_3328.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000557 Genomic DNA. Translation: ABO68511.1 . Different initiation.
    RefSeqi YP_001127256.1. NC_009328.1.

    3D structure databases

    ProteinModelPortali A4IT57.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 420246.GTNG_3166.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO68511 ; ABO68511 ; GTNG_3166 .
    GeneIDi 4968092.
    KEGGi gtn:GTNG_3166.
    PATRICi 21982971. VBIGeoThe136879_3328.

    Phylogenomic databases

    eggNOGi COG3844.
    HOGENOMi HOG000242438.
    KOi K01556.
    OrthoDBi EOG6N67XP.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .
    BioCyci GTHE420246:GIXT-3262-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. "Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
      Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
      Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NG80-2.

    Entry informationi

    Entry nameiKYNU_GEOTN
    AccessioniPrimary (citable) accession number: A4IT57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 53 of the entry and version 2 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