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Protein

Chlorocatechol 1,2-dioxygenase

Gene

clcA

Organism
Rhodococcus opacus (Nocardia opaca)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

4-chlorocatechol + O2 = 3-chloro-muconate.
3,5-dichlorocatechol + O2 = 2,4-dichloro -muconate.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi134 – 1341IronBy similarity
Metal bindingi169 – 1691IronBy similarity
Metal bindingi194 – 1941IronBy similarity
Metal bindingi196 – 1961IronBy similarity

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

BRENDAi1.13.11.1. 4353.

Names & Taxonomyi

Protein namesi
Recommended name:
Chlorocatechol 1,2-dioxygenase (EC:1.13.11.-)
Gene namesi
Name:clcA
OrganismiRhodococcus opacus (Nocardia opaca)
Taxonomic identifieri37919 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

Pathology & Biotechi

Chemistry

DrugBankiDB03793. Benzoic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257Chlorocatechol 1,2-dioxygenasePRO_0000085088Add
BLAST

Structurei

Secondary structure

1
257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2421Combined sources
Helixi28 – 4316Combined sources
Helixi47 – 6418Combined sources
Beta strandi67 – 693Combined sources
Beta strandi88 – 903Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi122 – 1265Combined sources
Turni135 – 1373Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi157 – 1648Combined sources
Helixi176 – 1827Combined sources
Turni183 – 1853Combined sources
Beta strandi195 – 2006Combined sources
Beta strandi207 – 2137Combined sources
Turni217 – 2204Combined sources
Helixi229 – 2313Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi243 – 25311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S9AX-ray2.47A/B1-257[»]
3O32X-ray2.85A/B1-257[»]
3O5UX-ray2.35A/B1-257[»]
3O6JX-ray2.90A/B1-257[»]
3O6RX-ray2.60A/B1-257[»]
ProteinModelPortaliO67987.
SMRiO67987. Positions 2-257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67987.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.130.10. 1 hit.
InterProiIPR007535. Catechol_dOase_N.
IPR012817. Chlorcchol_dOase.
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.
TIGRFAMsiTIGR02465. chlorocat_1_2. 1 hit.
PROSITEiPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O67987-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANTRVIELF DEFTDLIRDF IVRHEITTPE YETIMQYMIS VGEAGEWPLW
60 70 80 90 100
LDAFFETTVD SVSYGKGNWT SSAIQGPFFK EGAPLLTGKP ATLPMRADEP
110 120 130 140 150
GDRMRFTGSV RDTSGTPITG AVIDVWHSTN DGNYSFFSPA LPDQYLLRGR
160 170 180 190 200
VVPAEDGSIE FHSIRPVPYE IPKAGPTGQL MNSYLGRHSW RPAHIHIRIT
210 220 230 240 250
ADGYRPLITQ LYFEGDPYLD SDSCSAVKSE LVLPVNKIDI DGETWQLVDF

NFILQHN
Length:257
Mass (Da):28,953
Last modified:August 1, 1998 - v1
Checksum:iD834A96E85A15777
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003948 Genomic DNA. Translation: AAC38251.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003948 Genomic DNA. Translation: AAC38251.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S9AX-ray2.47A/B1-257[»]
3O32X-ray2.85A/B1-257[»]
3O5UX-ray2.35A/B1-257[»]
3O6JX-ray2.90A/B1-257[»]
3O6RX-ray2.60A/B1-257[»]
ProteinModelPortaliO67987.
SMRiO67987. Positions 2-257.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB03793. Benzoic Acid.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.13.11.1. 4353.

Miscellaneous databases

EvolutionaryTraceiO67987.

Family and domain databases

Gene3Di2.60.130.10. 1 hit.
InterProiIPR007535. Catechol_dOase_N.
IPR012817. Chlorcchol_dOase.
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.
TIGRFAMsiTIGR02465. chlorocat_1_2. 1 hit.
PROSITEiPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Evolutionary relationship between chlorocatechol catabolic enzymes from Rhodococcus opacus 1CP and their counterparts in proteobacteria: sequence divergence and functional convergence."
    Eulberg D., Kourbatova E.M., Golovleva L.A., Schloemann M.
    J. Bacteriol. 180:1082-1094(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 1CP.

Entry informationi

Entry nameiCLCA_RHOOP
AccessioniPrimary (citable) accession number: O67987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: January 20, 2016
This is version 74 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

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.