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Protein

Hydroxyquinol 1,2-dioxygenase

Gene

chqB

Organism
Nocardioides simplex (Arthrobacter simplex)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ortho-cleavage of the aromatic ring of hydroxyquinol.1 Publication

Catalytic activityi

Benzene-1,2,4-triol + O2 = maleylacetate.

Cofactori

Fe3+Note: Binds 1 Fe3+ ion per subunit.

Enzyme regulationi

Inhibited by 3,5-dichlorocatechol, chlorohydroquinone and 4,5-dibromocatechol.

Kineticsi

5-chlorohydroxyquinols and 6-chloro-chlorohydroxyquinols are also substrates.

  1. KM=1.2 µM for hydroxyquinol1 Publication
  1. Vmax=55 µmol/min/mg enzyme with hydroxyquinol as substrate1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 50-55 degrees Celsius.1 Publication

Pathwayi: beta-ketoadipate pathway

This protein is involved in step 2 of the subpathway that synthesizes 3-oxoadipate from 3,4-dihydroxybenzoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Hydroxyquinol 1,2-dioxygenase (chqB)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway beta-ketoadipate pathway, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 3-oxoadipate from 3,4-dihydroxybenzoate, the pathway beta-ketoadipate pathway and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi164 – 1641Iron
Metal bindingi197 – 1971Iron
Metal bindingi221 – 2211Iron
Metal bindingi223 – 2231Iron

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.37. 456.
SABIO-RKQ5PXQ6.
UniPathwayiUPA00157; UER00268.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyquinol 1,2-dioxygenase (EC:1.13.11.37)
Alternative name(s):
1,2-HQD
Gene namesi
Name:chqB
OrganismiNocardioides simplex (Arthrobacter simplex)
Taxonomic identifieri2045 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesNocardioidaceaePimelobacter

Pathology & Biotechi

Chemistry

DrugBankiDB03793. Benzoic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293Hydroxyquinol 1,2-dioxygenasePRO_0000085086Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2317Combined sources
Turni24 – 263Combined sources
Helixi30 – 5021Combined sources
Helixi54 – 7017Combined sources
Helixi77 – 848Combined sources
Helixi87 – 959Combined sources
Beta strandi133 – 14210Combined sources
Beta strandi152 – 1565Combined sources
Helixi165 – 1673Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi175 – 1806Combined sources
Beta strandi185 – 1928Combined sources
Helixi204 – 2118Combined sources
Beta strandi221 – 2277Combined sources
Beta strandi234 – 2407Combined sources
Helixi244 – 2474Combined sources
Helixi256 – 2583Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi288 – 2903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TMXX-ray1.75A/B1-293[»]
ProteinModelPortaliQ5PXQ6.
SMRiQ5PXQ6. Positions 3-293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5PXQ6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK04098.

Family and domain databases

Gene3Di2.60.130.10. 1 hit.
InterProiIPR007535. Catechol_dOase_N.
IPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
[Graphical view]
PfamiPF00775. Dioxygenase_C. 1 hit.
PF04444. Dioxygenase_N. 1 hit.
[Graphical view]
SUPFAMiSSF49482. SSF49482. 1 hit.
PROSITEiPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5PXQ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPVSAEQQ AREQDLVERV LRSFDATADP RLKQVMQALT RHLHAFLREV
60 70 80 90 100
RLTEAEWETG IGFLTDAGHV TNERRQEFIL LSDVLGASMQ TIAMNNEAHG
110 120 130 140 150
DATEATVFGP FFVEGSPRIE SGGDIAGGAA GEPCWVEGTV TDTDGNPVPD
160 170 180 190 200
ARIEVWEADD DGFYDVQYDD DRTAARAHLL SGPDGGYAFW AITPTPYPIP
210 220 230 240 250
HDGPVGRMLA ATGRSPMRAS HLHFMVTAPG RRTLVTHIFV EGDELLDRDS
260 270 280 290
VFGVKDSLVK SFERQPAGAP TPGGREIDGP WSRVRFDIVL APA
Length:293
Mass (Da):31,967
Last modified:January 4, 2005 - v1
Checksum:iDEE403CF2AB8F5B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY822041 Genomic DNA. Translation: AAV71144.1.

Genome annotation databases

KEGGiag:AAV71144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY822041 Genomic DNA. Translation: AAV71144.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TMXX-ray1.75A/B1-293[»]
ProteinModelPortaliQ5PXQ6.
SMRiQ5PXQ6. Positions 3-293.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB03793. Benzoic Acid.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAV71144.

Phylogenomic databases

KOiK04098.

Enzyme and pathway databases

UniPathwayiUPA00157; UER00268.
BRENDAi1.13.11.37. 456.
SABIO-RKQ5PXQ6.

Miscellaneous databases

EvolutionaryTraceiQ5PXQ6.

Family and domain databases

Gene3Di2.60.130.10. 1 hit.
InterProiIPR007535. Catechol_dOase_N.
IPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
[Graphical view]
PfamiPF00775. Dioxygenase_C. 1 hit.
PF04444. Dioxygenase_N. 1 hit.
[Graphical view]
SUPFAMiSSF49482. SSF49482. 1 hit.
PROSITEiPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation."
    Ferraroni M., Seifert J., Travkin V.M., Thiel M., Kaschabek S., Scozzafava A., Golovleva L., Schloemann M., Briganti F.
    J. Biol. Chem. 280:21144-21154(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH FE(3+), CHARACTERIZATION.
    Strain: 3E.
  2. "Characterization of an intradiol dioxygenase involved in the biodegradation of the chlorophenoxy herbicides 2,4-D and 2,4,5-T."
    Travkin V.M., Jadan A.P., Briganti F., Scozzafava A., Golovleva L.A.
    FEBS Lett. 407:69-72(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: 3E.

Entry informationi

Entry nameiCHQB_NOCSI
AccessioniPrimary (citable) accession number: Q5PXQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: January 4, 2005
Last modified: May 11, 2016
This is version 54 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, Direct protein sequencing

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.