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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

Hydroxyquinol + O2 = maleylacetate.1 Publication

Cofactori

Fe3+1 PublicationNote: Binds 1 Fe3+ ion per subunit.1 Publication

Enzyme regulationi

Inhibited by 3,5-dichlorocatechol, chlorohydroquinone and 4,5-dibromocatechol.1 Publication

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)DescriptionActionsGraphical viewLength
Metal bindingi164Iron1 Publication1
Metal bindingi197Iron1 Publication1
Metal bindingi221Iron1 Publication1
Metal bindingi223Iron1 Publication1

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:1.13.11.371 Publication)
Alternative name(s):
1,2-HQD
Gene namesi
Name:chqB
OrganismiNocardioides simplex (Arthrobacter simplex)
Taxonomic identifieri2045 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesNocardioidaceaePimelobacter

Pathology & Biotechi

Chemistry databases

DrugBankiDB03793. Benzoic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000850861 – 293Hydroxyquinol 1,2-dioxygenaseAdd BLAST293

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 23Combined sources17
Turni24 – 26Combined sources3
Helixi30 – 50Combined sources21
Helixi54 – 70Combined sources17
Helixi77 – 84Combined sources8
Helixi87 – 95Combined sources9
Beta strandi133 – 142Combined sources10
Beta strandi152 – 156Combined sources5
Helixi165 – 167Combined sources3
Beta strandi168 – 170Combined sources3
Beta strandi175 – 180Combined sources6
Beta strandi185 – 192Combined sources8
Helixi204 – 211Combined sources8
Beta strandi221 – 227Combined sources7
Beta strandi234 – 240Combined sources7
Helixi244 – 247Combined sources4
Helixi256 – 258Combined sources3
Beta strandi282 – 285Combined sources4
Beta strandi288 – 290Combined sources3

3D structure databases

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

Chemistry databases

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...

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: November 2, 2016
This is version 56 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.