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Protein

Tryptophan 2,3-dioxygenase

Gene

kynA

Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring.UniRule annotation2 Publications

Catalytic activityi

L-tryptophan + O2 = N-formyl-L-kynurenine.UniRule annotation2 Publications

Cofactori

hemeNote: Binds 2 heme groups per tetramer.

Enzyme regulationi

Weakly inhibited by D-tryptophan.1 Publication

Kineticsi

  1. KM=114 µM for L-tryptophan2 Publications
  2. KM=100 µM for 5-fluoro-D/L-tryptophan2 Publications
  3. KM=186 µM for 6-fluoro-D/L-tryptophan2 Publications
  4. KM=357 µM for 5-methyl-D/L-tryptophan2 Publications
  5. KM=975 µM for 6-methyl-D/L-tryptophan2 Publications
  6. KM=119 µM for O22 Publications

    Pathwayi: L-tryptophan degradation via kynurenine pathway

    This protein is involved in step 1 of the subpathway that synthesizes L-kynurenine from L-tryptophan.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Tryptophan 2,3-dioxygenase (kynA)
    2. no protein annotated in this organism
    This subpathway is part of the pathway L-tryptophan degradation via kynurenine pathway, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-kynurenine from L-tryptophan, the pathway L-tryptophan degradation via kynurenine pathway and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei113Substrate1
    Binding sitei117Substrate1
    Binding sitei124HemeUniRule annotation2 Publications1
    Metal bindingi240Iron (heme axial ligand)1
    Binding sitei254Substrate1

    GO - Molecular functioni

    • heme binding Source: UniProtKB
    • metal ion binding Source: UniProtKB-KW
    • tryptophan 2,3-dioxygenase activity Source: UniProtKB

    GO - Biological processi

    • protein homotetramerization Source: UniProtKB
    • tryptophan catabolic process to acetyl-CoA Source: GO_Central
    • tryptophan catabolic process to kynurenine Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Tryptophan catabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.13.11.11. 6708.
    UniPathwayiUPA00333; UER00453.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptophan 2,3-dioxygenaseUniRule annotation (EC:1.13.11.11UniRule annotation)
    Short name:
    TDOUniRule annotation
    Alternative name(s):
    Tryptamin 2,3-dioxygenaseUniRule annotation
    Tryptophan oxygenaseUniRule annotation
    Short name:
    TOUniRule annotation
    Short name:
    TRPOUniRule annotation
    Tryptophan pyrrolaseUniRule annotation
    TryptophanaseUniRule annotation
    Gene namesi
    Name:kynAUniRule annotation
    Ordered Locus Names:XCC0432
    OrganismiXanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
    Taxonomic identifieri190485 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    Proteomesi
    • UP000001010 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi55H → A: Decrease in catalytic efficiency using L-tryptophan, 5-fluoro-D/L-tryptophan, 6-fluoro-D/L-tryptophan, 5-methyl-D/L-tryptophan and 6-methyl-D/L-tryptophan as substrate. 2 Publications1
    Mutagenesisi55H → S: Decrease in catalytic efficiency using L-tryptophan, 5-fluoro-D/L-tryptophan, 6-fluoro-D/L-tryptophan, 5-methyl-D/L-tryptophan and 6-methyl-D/L-tryptophan as substrate. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003601431 – 298Tryptophan 2,3-dioxygenaseAdd BLAST298

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation2 Publications

    Protein-protein interaction databases

    DIPiDIP-60795N.
    STRINGi190485.XCC0432.

    Structurei

    Secondary structure

    1298
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi24 – 27Combined sources4
    Helixi30 – 33Combined sources4
    Helixi48 – 77Combined sources30
    Helixi81 – 100Combined sources20
    Helixi102 – 105Combined sources4
    Helixi110 – 113Combined sources4
    Turni114 – 116Combined sources3
    Helixi117 – 119Combined sources3
    Helixi125 – 127Combined sources3
    Helixi129 – 138Combined sources10
    Helixi143 – 146Combined sources4
    Turni148 – 151Combined sources4
    Helixi153 – 163Combined sources11
    Helixi168 – 178Combined sources11
    Helixi185 – 188Combined sources4
    Helixi200 – 202Combined sources3
    Helixi203 – 211Combined sources9
    Turni213 – 216Combined sources4
    Helixi217 – 248Combined sources32
    Beta strandi254 – 257Combined sources4
    Helixi260 – 266Combined sources7
    Helixi273 – 277Combined sources5
    Helixi278 – 280Combined sources3
    Turni281 – 283Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1YW0X-ray2.70A/B/C/D23-298[»]
    2NW7X-ray2.70A/B/C/D1-298[»]
    2NW8X-ray1.60A/B1-298[»]
    2NW9X-ray1.80A/B1-298[»]
    3BK9X-ray2.15A/B/C/D/E/F/G/H1-298[»]
    3E08X-ray1.90A/B/C/D/E/F/G/H1-298[»]
    ProteinModelPortaliQ8PDA8.
    SMRiQ8PDA8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8PDA8.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni24 – 28Substrate binding5
    Regioni51 – 55Substrate binding5

    Sequence similaritiesi

    Belongs to the tryptophan 2,3-dioxygenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105HJ8. Bacteria.
    COG3483. LUCA.
    HOGENOMiHOG000221583.
    KOiK00453.
    OMAiYWDLYQL.

    Family and domain databases

    HAMAPiMF_01972. T23O. 1 hit.
    InterProiIPR004981. Trp_2_3_dOase.
    [Graphical view]
    PANTHERiPTHR10138. PTHR10138. 1 hit.
    PfamiPF03301. Trp_dioxygenase. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8PDA8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPVDKNLRDL EPGIHTDLEG RLTYGGYLRL DQLLSAQQPL SEPAHHDEML
    60 70 80 90 100
    FIIQHQTSEL WLKLLAHELR AAIVHLQRDE VWQCRKVLAR SKQVLRQLTE
    110 120 130 140 150
    QWSVLETLTP SEYMGFRDVL GPSSGFQSLQ YRYIEFLLGN KNPQMLQVFA
    160 170 180 190 200
    YDPAGQARLR EVLEAPSLYE EFLRYLARFG HAIPQQYQAR DWTAAHVADD
    210 220 230 240 250
    TLRPVFERIY ENTDRYWREY SLCEDLVDVE TQFQLWRFRH MRTVMRVIGF
    260 270 280 290
    KRGTGGSSGV GFLQQALALT FFPELFDVRT SVGVDNRPPQ GSADAGKR
    Length:298
    Mass (Da):34,617
    Last modified:October 1, 2002 - v1
    Checksum:i544600380EDD4A3D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE008922 Genomic DNA. Translation: AAM39750.1.
    RefSeqiNP_635826.1. NC_003902.1.
    WP_011035685.1. NC_003902.1.

    Genome annotation databases

    EnsemblBacteriaiAAM39750; AAM39750; XCC0432.
    GeneIDi1000901.
    KEGGixcc:XCC0432.
    PATRICi24071477. VBIXanCam115730_0475.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE008922 Genomic DNA. Translation: AAM39750.1.
    RefSeqiNP_635826.1. NC_003902.1.
    WP_011035685.1. NC_003902.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1YW0X-ray2.70A/B/C/D23-298[»]
    2NW7X-ray2.70A/B/C/D1-298[»]
    2NW8X-ray1.60A/B1-298[»]
    2NW9X-ray1.80A/B1-298[»]
    3BK9X-ray2.15A/B/C/D/E/F/G/H1-298[»]
    3E08X-ray1.90A/B/C/D/E/F/G/H1-298[»]
    ProteinModelPortaliQ8PDA8.
    SMRiQ8PDA8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-60795N.
    STRINGi190485.XCC0432.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAM39750; AAM39750; XCC0432.
    GeneIDi1000901.
    KEGGixcc:XCC0432.
    PATRICi24071477. VBIXanCam115730_0475.

    Phylogenomic databases

    eggNOGiENOG4105HJ8. Bacteria.
    COG3483. LUCA.
    HOGENOMiHOG000221583.
    KOiK00453.
    OMAiYWDLYQL.

    Enzyme and pathway databases

    UniPathwayiUPA00333; UER00453.
    BRENDAi1.13.11.11. 6708.

    Miscellaneous databases

    EvolutionaryTraceiQ8PDA8.

    Family and domain databases

    HAMAPiMF_01972. T23O. 1 hit.
    InterProiIPR004981. Trp_2_3_dOase.
    [Graphical view]
    PANTHERiPTHR10138. PTHR10138. 1 hit.
    PfamiPF03301. Trp_dioxygenase. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiT23O_XANCP
    AccessioniPrimary (citable) accession number: Q8PDA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 20, 2009
    Last sequence update: October 1, 2002
    Last modified: November 2, 2016
    This is version 83 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, Complete proteome, Reference proteome

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.