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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei160 – 1601Substrate
    Active sitei251 – 2511Proton donor/acceptor1 Publication

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381H → A: Strongly reduced affinity for substrate. Reduced enzyme activity.
    Mutagenesisi101 – 1011S → A: Strongly reduced affinity for substrate. Strongly reduced enzyme activity. 2 Publications
    Mutagenesisi102 – 1021H → L: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi102 – 1021H → Q: Reduces enzyme activity by about half. 1 Publication
    Mutagenesisi126 – 1261D → A: Strongly reduced enzyme activity.
    Mutagenesisi196 – 1961Y → A, K or R: Strongly reduced affinity for substrate. Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi233 – 2331D → A: Reduces enzyme activity by about half. 1 Publication
    Mutagenesisi251 – 2511H → A: Abolishes enzyme activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2762761H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenasePRO_0000418915Add
    BLAST

    Expressioni

    Inductioni

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

    Structurei

    Secondary structure

    1
    276
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53Combined sources
    Beta strandi6 – 116Combined sources
    Beta strandi14 – 207Combined sources
    Beta strandi25 – 273Combined sources
    Beta strandi29 – 335Combined sources
    Helixi40 – 434Combined sources
    Helixi44 – 507Combined sources
    Turni51 – 533Combined sources
    Beta strandi56 – 594Combined sources
    Beta strandi65 – 673Combined sources
    Helixi76 – 9015Combined sources
    Beta strandi94 – 1007Combined sources
    Helixi101 – 1033Combined sources
    Helixi104 – 11815Combined sources
    Beta strandi122 – 1265Combined sources
    Helixi134 – 14411Combined sources
    Turni146 – 1483Combined sources
    Helixi149 – 16113Combined sources
    Helixi167 – 1748Combined sources
    Turni175 – 1795Combined sources
    Helixi182 – 19918Combined sources
    Helixi202 – 2076Combined sources
    Beta strandi215 – 2195Combined sources
    Helixi225 – 23713Combined sources
    Beta strandi241 – 2455Combined sources
    Beta strandi249 – 2513Combined sources
    Helixi253 – 2564Combined sources
    Helixi258 – 27316Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni36 – 383Substrate binding
    Regioni100 – 1012Substrate binding

    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]
    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.
    KEGGiarr: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
    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.
    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.
    KEGGiarr:ARUE_113p00080.

    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...

    Publicationsi

    1. "Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter spec. Ru61a."
      Betz A., Facey S.J., Hauer B., Tshisuaka B., Lingens F.
      J. Basic Microbiol. 40:7-23(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF SER-101 AND ASP-233.
      Strain: Rue61a.
    2. "Complete nucleotide sequence of the 113-kilobase linear catabolic plasmid pAL1 of Arthrobacter nitroguajacolicus Ru61a and transcriptional analysis of genes involved in quinaldine degradation."
      Parschat K., Overhage J., Strittmatter A.W., Henne A., Gottschalk G., Fetzner S.
      J. Bacteriol. 189:3855-3867(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: Rue61a.
    3. "Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion."
      Frerichs-Deeken U., Ranguelova K., Kappl R., Huttermann J., Fetzner S.
      Biochemistry 43:14485-14499(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF SER-101; HIS-102 AND TYR-196, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: Rue61a.
    4. "Dioxygenases without requirement for cofactors: identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase."
      Frerichs-Deeken U., Fetzner S.
      Curr. Microbiol. 51:344-352(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-251, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Rue61a.
    5. "Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold."
      Steiner R.A., Janssen H.J., Roversi P., Oakley A.J., Fetzner S.
      Proc. Natl. Acad. Sci. U.S.A. 107:657-662(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH 2-(ACETYLAMINO)BENZOIC ACID AND 3-HYDROXY-2-METHYLQUINOLIN-4(1H)-ONE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, LACK OF COFACTOR, MUTAGENESIS OF HIS-251.

    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: May 11, 2016
    This is version 59 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.