Reviewed, UniProtKB/Swiss-Prot Q43984 (CATA_ACIGB)

Names and origin

Protein names

Recommended name:
    Catechol 1,2-dioxygenase
    EC=1.13.11.1

Gene names

Name:

catA

Organism

Acinetobacter genomosp. 11

Taxonomic identifier

106649 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	Catechol + O(2) = cis,cis-muconate.
Cofactor	Binds 1 Fe(3+) ion per subunit By similarity.
Pathway	Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydrofuran-2-acetate from catechol: step 1/3.
Subunit structure	Homodimer By similarity.
Induction	By phenol and benzoate.
Sequence similarities	Belongs to the intradiol ring-cleavage dioxygenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW catechol catabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catechol 1,2-dioxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB ferric iron binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 305	305	Catechol 1,2-dioxygenase		PRO_0000085080
Sites
	Metal binding	163	1	Iron
	Metal binding	197	1	Iron
	Metal binding	221	1	Iron
	Metal binding	223	1	Iron

Sequences

	Sequence		Length	Mass (Da)
	Q43984-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E65143DFA0572937	FASTA	305	33,609
	10 20 30 40 50 60 MMMNRQQIDS LVQQMNVATA TGEVNLRVQQ IVVRLLGDLF QAIEDLNMSQ TELWKGLEYL 70 80 90 100 110 120 TDAGQANELG LLAAGLGLEH YLDLRADEAD AKAGITGGTP RTIEGPLYVA GAPESVGFAR 130 140 150 160 170 180 MDDGSESAHV DALIIEGNVT DTAGQIIPNA KVEIWHANSL GNYSFFDKSQ SAFNLRRSIF 190 200 210 220 230 240 TDTQGQYIAQ TTMPVGYGCP PEGTTQALLN LLGRHGNRPS HVHYFVSAPG YRKLTTQFNI 250 260 270 280 290 300 EGDKYLWDDF AFATRDGLIA TALDVTDLAK IKQYNLNKAF KHIKFNFQLV QDADQVPLQR LIVVE

References

[1]	"Genetic organization, nucleotide sequence and regulation of expression of genes encoding phenol hydroxylase and catechol 1,2-dioxygenase in Acinetobacter calcoacetious." Ehrt S., Schirmer F., Hillen W. Mol. Microbiol. 18:13-20(1995) [PubMed: 8596453] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY PHENOL. Strain: ATCC 11171 / NCIB 8250 / CIP 63.46 / B94.
[2]	"RpoN (sigma 54) is required for conversion of phenol to catechol in Acinetobacter calcoaceticus." Ehrt S., Ornston L.N., Hillen W. J. Bacteriol. 176:3493-3499(1994) [PubMed: 8206826] [Abstract] Cited for: INDUCTION BY PHENOL AND BENZOATE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z36909 Genomic DNA. Translation: CAA85386.1.
PIR	S47293.
3D structure databases
HSSP	HSSP built from PDB template 1DMH based on UniProtKB P07773.
ModBase	Search...
Family and domain databases
InterPro	IPR007535. Catechol_dOase_N. IPR012801. Cchol_dOase_prob. IPR000627. Intradiol_dOase_C. IPR015889. Intradiol_dOase_core. [Graphical view]
Gene3D	G3DSA:2.60.130.10. Intradiol_dOase_core. 1 hit.
Pfam	PF00775. Dioxygenase_C. 1 hit. PF04444. Dioxygenase_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR02439. catechol_proteo. 1 hit.
PROSITE	PS00083. INTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATA_ACIGB

Accession

Primary (citable) accession number: Q43984

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)