Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Catechol 1,2-dioxygenase

Gene

catA

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

Functioni

Catalytic activityi

Catechol + O2 = cis,cis-muconate.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi152IronBy similarity1
Metal bindingi186IronBy similarity1
Metal bindingi210IronBy similarity1
Metal bindingi212IronBy similarity1

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:
Catechol 1,2-dioxygenase (EC:1.13.11.1)
Alternative name(s):
1,2-CTD
Gene namesi
Name:catA
OrganismiRhodococcus opacus (Nocardia opaca)
Taxonomic identifieri37919 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000085084‹1 – 270Catechol 1,2-dioxygenaseAdd BLAST›270

Interactioni

Protein-protein interaction databases

STRINGi632772.ROP_20870.

Structurei

Secondary structure

1270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 42Combined sources22
Helixi46 – 61Combined sources16
Helixi65 – 72Combined sources8
Helixi74 – 83Combined sources10
Beta strandi106 – 109Combined sources4
Helixi116 – 118Combined sources3
Beta strandi121 – 129Combined sources9
Beta strandi131 – 133Combined sources3
Beta strandi140 – 144Combined sources5
Turni161 – 164Combined sources4
Beta strandi165 – 169Combined sources5
Beta strandi174 – 181Combined sources8
Helixi193 – 200Combined sources8
Beta strandi211 – 216Combined sources6
Beta strandi223 – 229Combined sources7
Turni233 – 236Combined sources4
Helixi245 – 247Combined sources3
Beta strandi259 – 262Combined sources4
Beta strandi265 – 267Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HGIX-ray1.94A1-270[»]
3HHXX-ray2.00A1-270[»]
3HHYX-ray1.55A1-270[»]
3HJ8X-ray2.40A1-270[»]
3HJQX-ray2.00A1-270[»]
3HJSX-ray1.80A1-270[»]
3HKPX-ray1.85A1-270[»]
3I4VX-ray2.00A1-270[»]
3I4YX-ray1.85A1-270[»]
3I51X-ray1.80A1-270[»]
ProteinModelPortaliP95607.
SMRiP95607.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP95607.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108QMY. Bacteria.
COG3485. LUCA.

Family and domain databases

CDDicd03462. 1_2-CCD. 1 hit.
Gene3Di2.60.130.10. 1 hit.
InterProiIPR007535. Catechol_dOase_N.
IPR012800. Cchol_dOase_actb.
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.
TIGRFAMsiTIGR02438. catachol_actin. 1 hit.
PROSITEiPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P95607-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GSGSAATDKF KAERATADTS PERLAAIAKD ALGALNDVIL KHGVTYPEYR
60 70 80 90 100
VFKQWLIDVG EGGEWPLFLD VFIEHSVEEV LARSRKGTMG SIEGPYYIEN
110 120 130 140 150
SPELPSKCTL PMREEDEKIT PLVFSGQVTD LDGNGLAGAK VELWHADNDG
160 170 180 190 200
YYSQFAPHLP EWNLRGTIIA DEEGRYEITT IQPAPYQIPT DGPTGQFIEA
210 220 230 240 250
QNGHPWRPAH LHLIVSAPGK ESVTTQLYFK GGEWIDSDVA SATKPELILD
260 270
PKTGDDGKNY VTYNFVLDPA
Length:270
Mass (Da):29,704
Last modified:May 1, 1997 - v1
Checksum:iBCD5BE5B8365115A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99622 Genomic DNA. Translation: CAA67941.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99622 Genomic DNA. Translation: CAA67941.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HGIX-ray1.94A1-270[»]
3HHXX-ray2.00A1-270[»]
3HHYX-ray1.55A1-270[»]
3HJ8X-ray2.40A1-270[»]
3HJQX-ray2.00A1-270[»]
3HJSX-ray1.80A1-270[»]
3HKPX-ray1.85A1-270[»]
3I4VX-ray2.00A1-270[»]
3I4YX-ray1.85A1-270[»]
3I51X-ray1.80A1-270[»]
ProteinModelPortaliP95607.
SMRiP95607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi632772.ROP_20870.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108QMY. Bacteria.
COG3485. LUCA.

Enzyme and pathway databases

BRENDAi1.13.11.1. 4353.

Miscellaneous databases

EvolutionaryTraceiP95607.

Family and domain databases

CDDicd03462. 1_2-CCD. 1 hit.
Gene3Di2.60.130.10. 1 hit.
InterProiIPR007535. Catechol_dOase_N.
IPR012800. Cchol_dOase_actb.
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.
TIGRFAMsiTIGR02438. catachol_actin. 1 hit.
PROSITEiPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATA_RHOOP
AccessioniPrimary (citable) accession number: P95607
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1997
Last modified: November 2, 2016
This is version 71 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. 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.