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Protein

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

Gene

hod

Organism
Arthrobacter nitroguajacolicus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO.4 Publications

Cofactori

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

Kineticsi

  1. KM=1.5 µM for 1H-3-hydroxy-4-oxoquinaldine3 Publications
  2. KM=180 µM for 1H-3-hydroxy-4-oxoquinoline3 Publications

    pH dependencei

    Optimum pH is 8-11.3 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei160Substrate1
    Active sitei251Proton donor/acceptor1 Publication1

    GO - Molecular functioni

    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. 8910.

    Protein family/group databases

    ESTHERiartsp-hod. HOD-cofactorfree-dioxygenase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (EC:1.13.11.48)
    Gene namesi
    Name:hod
    Synonyms:meqE
    ORF Names:ARUE_113p00080, pAL1.008
    Encoded oniPlasmid pAL10 Publication
    OrganismiArthrobacter nitroguajacolicus
    Taxonomic identifieri211146 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaePaenarthrobacter

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi38H → A: Strongly reduced affinity for substrate. Reduced enzyme activity. 1
    Mutagenesisi101S → A: Strongly reduced affinity for substrate. Strongly reduced enzyme activity. 2 Publications1
    Mutagenesisi102H → L: Strongly reduced enzyme activity. 1 Publication1
    Mutagenesisi102H → Q: Reduces enzyme activity by about half. 1 Publication1
    Mutagenesisi126D → A: Strongly reduced enzyme activity. 1
    Mutagenesisi196Y → A, K or R: Strongly reduced affinity for substrate. Strongly reduced enzyme activity. 1 Publication1
    Mutagenesisi233D → A: Reduces enzyme activity by about half. 1 Publication1
    Mutagenesisi251H → A: Abolishes enzyme activity. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004189151 – 2761H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenaseAdd BLAST276

    Expressioni

    Inductioni

    Expressed from a large linear plasmid that contains the operon for quinaldine degradation.1 Publication

    Structurei

    Secondary structure

    1276
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 5Combined sources3
    Beta strandi6 – 11Combined sources6
    Beta strandi14 – 20Combined sources7
    Beta strandi25 – 27Combined sources3
    Beta strandi29 – 33Combined sources5
    Helixi40 – 43Combined sources4
    Helixi44 – 50Combined sources7
    Turni51 – 53Combined sources3
    Beta strandi56 – 59Combined sources4
    Beta strandi65 – 67Combined sources3
    Helixi76 – 90Combined sources15
    Beta strandi94 – 100Combined sources7
    Helixi101 – 103Combined sources3
    Helixi104 – 118Combined sources15
    Beta strandi122 – 126Combined sources5
    Helixi134 – 144Combined sources11
    Turni146 – 148Combined sources3
    Helixi149 – 161Combined sources13
    Helixi167 – 174Combined sources8
    Turni175 – 179Combined sources5
    Helixi182 – 199Combined sources18
    Helixi202 – 207Combined sources6
    Beta strandi215 – 219Combined sources5
    Helixi225 – 237Combined sources13
    Beta strandi241 – 245Combined sources5
    Beta strandi249 – 251Combined sources3
    Helixi253 – 256Combined sources4
    Helixi258 – 273Combined sources16

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2WJ3X-ray2.09A/B/C/D1-276[»]
    2WJ4X-ray2.10A/B/C/D1-276[»]
    2WJ6X-ray2.00A/B/C/D1-276[»]
    2WM2X-ray2.70A/B/C/D1-276[»]
    4CFSX-ray1.94A/B/C/D3-275[»]
    ProteinModelPortaliO31266.
    SMRiO31266.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini28 – 150AB hydrolase-1Sequence analysisAdd BLAST123

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni36 – 38Substrate binding3
    Regioni100 – 101Substrate binding2

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily.Curated

    Phylogenomic databases

    OrthoDBiPOG091H0AXG.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O31266-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDTYLHETL VFDNKLSYID NQRDTDGPAI LLLPGWCHDH RVYKYLIQEL
    60 70 80 90 100
    DADFRVIVPN WRGHGLSPCE VPDFGYQEQV KDALEILDQL GVETFLPVSH
    110 120 130 140 150
    SHGGWVLVEL LEQAGPERAP RGIIMDWLMW APKPDFAKSL TLLKDPERWR
    160 170 180 190 200
    EGTHGLFDVW LDGHDEKRVR HHLLEEMADY GYDCWGRSGR VIEDAYGRNG
    210 220 230 240 250
    SPMQMMANLT KTRPIRHIFS QPTEPEYEKI NSDFAEQHPW FSYAKLGGPT
    260 270
    HFPAIDVPDR AAVHIREFAT AIRQGQ
    Length:276
    Mass (Da):31,858
    Last modified:January 1, 1998 - v1
    Checksum:i7153BCF652C653DB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y14778 Genomic DNA. Translation: CAA75080.1.
    CP003205 Genomic DNA. Translation: AFR34517.1.

    Genome annotation databases

    EnsemblBacteriaiAFR34517; AFR34517; ARUE_113p00080.
    KEGGiag:CAA75080.
    arr:ARUE_113p00080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y14778 Genomic DNA. Translation: CAA75080.1.
    CP003205 Genomic DNA. Translation: AFR34517.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2WJ3X-ray2.09A/B/C/D1-276[»]
    2WJ4X-ray2.10A/B/C/D1-276[»]
    2WJ6X-ray2.00A/B/C/D1-276[»]
    2WM2X-ray2.70A/B/C/D1-276[»]
    4CFSX-ray1.94A/B/C/D3-275[»]
    ProteinModelPortaliO31266.
    SMRiO31266.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    ESTHERiartsp-hod. HOD-cofactorfree-dioxygenase.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAFR34517; AFR34517; ARUE_113p00080.
    KEGGiag:CAA75080.
    arr:ARUE_113p00080.

    Phylogenomic databases

    OrthoDBiPOG091H0AXG.

    Enzyme and pathway databases

    BRENDAi1.13.11.47. 8910.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHOD_ARTNT
    AccessioniPrimary (citable) accession number: O31266
    Secondary accession number(s): A4V8M9, J7LVS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: January 1, 1998
    Last modified: November 2, 2016
    This is version 62 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, Plasmid

    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.