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Protein

1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase

Gene

qdo

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ring-cleaving dioxygenase involved in oxoquinoline degradation and utilization.1 Publication

Catalytic activityi

3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO.4 Publications

Cofactori

Note: None. Contrary to most other dioxygenases, this enzyme does not require a cofactor for catalysis.

Kineticsi

  1. KM=24 µM for 1H-3-hydroxy-4-oxoquinoline3 Publications

    pH dependencei

    Optimum pH is 8.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei153 – 1531SubstrateBy similarity
    Active sitei244 – 2441Proton donor/acceptorBy similarity

    GO - Molecular functioni

    • 3-hydroxy-4-oxoquinoline 2,4-dioxygenase activity Source: UniProtKB

    GO - Biological processi

    • aromatic compound catabolic process Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Enzyme and pathway databases

    BRENDAi1.13.11.47. 5092.

    Protein family/group databases

    ESTHERipsepu-QDO. HOD-cofactorfree-dioxygenase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (EC:1.13.11.47)
    Gene namesi
    Name:qdo
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi95 – 951S → A or C: Reduced affinity for substrate, and strongly reduced enzyme activity. 1 Publication
    Mutagenesisi120 – 1201D → A: Strongly reduced affinity for substrate. Strongly reduced enzyme activity. 2 Publications
    Mutagenesisi244 – 2441H → A: Abolishes enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2642641H-3-hydroxy-4-oxoquinoline 2,4-dioxygenasePRO_0000418916Add
    BLAST

    Structurei

    Secondary structure

    1
    264
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 175Combined sources
    Beta strandi19 – 213Combined sources
    Beta strandi23 – 275Combined sources
    Helixi34 – 374Combined sources
    Helixi40 – 445Combined sources
    Turni45 – 473Combined sources
    Beta strandi48 – 536Combined sources
    Helixi70 – 8314Combined sources
    Beta strandi88 – 947Combined sources
    Helixi97 – 10711Combined sources
    Turni110 – 1123Combined sources
    Beta strandi115 – 1206Combined sources
    Helixi127 – 1359Combined sources
    Turni139 – 1413Combined sources
    Helixi142 – 15413Combined sources
    Helixi160 – 1689Combined sources
    Helixi170 – 1723Combined sources
    Helixi175 – 19218Combined sources
    Helixi195 – 2006Combined sources
    Beta strandi207 – 2126Combined sources
    Helixi218 – 23013Combined sources
    Beta strandi234 – 2385Combined sources
    Beta strandi242 – 2443Combined sources
    Helixi246 – 2494Combined sources
    Helixi251 – 26111Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IBTX-ray2.60A1-264[»]
    ProteinModelPortaliO33472.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO33472.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 323Substrate bindingBy similarity
    Regioni94 – 952Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily.Curated

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O33472-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQSLNVNGTL MTYSESGDPH APTLFLLSGW CQDHRLFKNL APLLARDFHV
    60 70 80 90 100
    ICPDWRGHDA KQTDSGDFDS QTLAQDLLAF IDAKGIRDFQ MVSTSHGCWV
    110 120 130 140 150
    NIDVCEQLGA ARLPKTIVID WLLQPHPGFW QQLAEGQHPT EYVAGRQSFF
    160 170 180 190 200
    DEWAETTDNA DVLNHLRNEM PWFHGEMWQR ACREIEANYR TWGSPLDRME
    210 220 230 240 250
    SLPQKPEICH IYSQPLSQDY RQLQLDFAAG HSWFHPRHIP GRTHFPSLEN
    260
    PVAVAQAIRE FLQA
    Length:264
    Mass (Da):30,347
    Last modified:November 1, 1999 - v2
    Checksum:iDEBE92440554FA84
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y14779 Genomic DNA. Translation: CAA75082.2.
    PIRiS23121.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y14779 Genomic DNA. Translation: CAA75082.2.
    PIRiS23121.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IBTX-ray2.60A1-264[»]
    ProteinModelPortaliO33472.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    ESTHERipsepu-QDO. HOD-cofactorfree-dioxygenase.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi1.13.11.47. 5092.

    Miscellaneous databases

    EvolutionaryTraceiO33472.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiQDO_PSEPU
    AccessioniPrimary (citable) accession number: O33472
    Secondary accession number(s): Q9R5I6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: November 1, 1999
    Last modified: June 24, 2015
    This is version 40 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

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.