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P83788

- KYNU_PSEFL

UniProt

P83788 - KYNU_PSEFL

Protein

Kynureninase

Gene

kynU

Organism
Pseudomonas fluorescens
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (15 Mar 2004)
      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.

    Catalytic activityi

    L-kynurenine + H2O = anthranilate + L-alanine.1 PublicationUniRule annotation
    L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.1 PublicationUniRule annotation

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei97 – 971Pyridoxal phosphate; via amide nitrogen1 PublicationUniRule annotation
    Binding sitei98 – 981Pyridoxal phosphate1 PublicationUniRule annotation
    Binding sitei172 – 1721Pyridoxal phosphate1 PublicationUniRule annotation
    Binding sitei201 – 2011Pyridoxal phosphate1 PublicationUniRule annotation
    Binding sitei204 – 2041Pyridoxal phosphate1 PublicationUniRule annotation
    Binding sitei226 – 2261Pyridoxal phosphate1 Publication
    Binding sitei256 – 2561Pyridoxal phosphate1 Publication
    Binding sitei282 – 2821Pyridoxal phosphate1 Publication

    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

    BioCyciMetaCyc:MONOMER-7065.
    SABIO-RKP83788.
    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
    OrganismiPseudomonas fluorescens
    Taxonomic identifieri294 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi132 – 1321D → A: Reduces binding to pyridoxal phosphate and strongly reduces catalytic activity. 1 Publication
    Mutagenesisi132 – 1321D → E: Enhances binding to pyridoxal phosphate. 1 Publication
    Mutagenesisi201 – 2011D → E: Enhances binding to pyridoxal phosphate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416KynureninasePRO_0000357010Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Subunit structurei

    Homodimer.1 PublicationUniRule annotation

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 129
    Helixi17 – 226
    Turni34 – 363
    Helixi44 – 5310
    Helixi54 – 596
    Helixi60 – 623
    Helixi63 – 664
    Helixi69 – 713
    Helixi72 – 8110
    Turni82 – 854
    Beta strandi90 – 934
    Helixi97 – 11519
    Beta strandi121 – 1255
    Helixi130 – 14314
    Beta strandi148 – 1547
    Helixi155 – 1573
    Helixi158 – 1614
    Beta strandi166 – 1749
    Turni176 – 1783
    Helixi184 – 19411
    Beta strandi197 – 2015
    Turni203 – 2086
    Helixi213 – 2164
    Beta strandi219 – 2235
    Beta strandi225 – 2273
    Beta strandi238 – 2414
    Turni243 – 2486
    Helixi256 – 2583
    Helixi275 – 2784
    Helixi285 – 29814
    Helixi303 – 32523
    Helixi338 – 3403
    Beta strandi343 – 3486
    Helixi352 – 3609
    Turni361 – 3633
    Beta strandi367 – 3693
    Turni370 – 3723
    Beta strandi373 – 3775
    Turni380 – 3823
    Helixi385 – 40117
    Turni402 – 4043

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QZ9X-ray1.85A1-416[»]
    ProteinModelPortaliP83788.
    SMRiP83788. Positions 2-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP83788.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    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.

    P83788-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTRNDCLAL DAQDSLAPLR QQFALPEGVI YLDGNSLGAR PVAALARAQA    50
    VIAEEWGNGL IRSWNSAGWR DLSERLGNRL ATLIGARDGE VVVTDTTSIN 100
    LFKVLSAALR VQATRSPERR VIVTETSNFP TDLYIAEGLA DMLQQGYTLR 150
    LVDSPEELPQ AIDQDTAVVM LTHVNYKTGY MHDMQALTAL SHECGALAIW 200
    DLAHSAGAVP VDLHQAGADY AIGCTYKYLN GGPGSQAFVW VSPQLCDLVP 250
    QPLSGWFGHS RQFAMEPRYE PSNGIARYLC GTQPITSLAM VECGLDVFAQ 300
    TDMASLRRKS LALTDLFIEL VEQRCAAHEL TLVTPREHAK RGSHVSFEHP 350
    EGYAVIQALI DRGVIGDYRE PRIMRFGFTP LYTTFTEVWD AVQILGEILD 400
    RKTWAQAQFQ VRHSVT 416
    Length:416
    Mass (Da):45,905
    Last modified:March 15, 2004 - v1
    Checksum:i50C3DE62A20C779D
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QZ9 X-ray 1.85 A 1-416 [» ]
    ProteinModelPortali P83788.
    SMRi P83788. Positions 2-405.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .
    BioCyci MetaCyc:MONOMER-7065.
    SABIO-RK P83788.

    Miscellaneous databases

    EvolutionaryTracei P83788.

    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. "Three-dimensional structure of kynureninase from Pseudomonas fluorescens."
      Momany C., Levdikov V., Blagova L., Lima S., Phillips R.S.
      Biochemistry 43:1193-1203(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, HOMODIMERIZATION, MUTAGENESIS OF ASP-132 AND ASP-201.

    Entry informationi

    Entry nameiKYNU_PSEFL
    AccessioniPrimary (citable) accession number: P83788
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: March 15, 2004
    Last modified: October 1, 2014
    This is version 50 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

    3D-structure

    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

    External Data

    Dasty 3