Reviewed, UniProtKB/Swiss-Prot P07773 (CATA_ACIAD)

Names and origin

Protein names

Recommended name:
    Catechol 1,2-dioxygenase
    EC=1.13.11.1
Alternative name(s):
    1,2-CTD

Gene names

Name:	catA
Ordered Locus Names:	ACIAD1442

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Catechol + O2 = cis,cis-muconate.
Cofactor	Binds 1 Fe3+ ion per subunit.
Pathway	Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydrofuran-2-acetate from catechol: step 1/3.
Subunit structure	Homodimer.
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
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW catechol catabolic process Ref.3 Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catechol 1,2-dioxygenase activity Ref.3 Inferred from direct assay. Source: UniProtKB ferric iron binding Ref.3 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 311

311

Catechol 1,2-dioxygenase

PRO_0000085078

Sites

Metal binding

164

1

Iron

Metal binding

200

1

Iron

Metal binding

224

1

Iron

Metal binding

226

1

Iron

Secondary structure

1

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311

Helix Strand Turn

Details...

Helix

9 – 18

10

Turn

19 – 22

4

Beta strand

24 – 26

3

Helix

28 – 47

20

Helix

52 – 67

16

Helix

71 – 77

7

Helix

80 – 94

15

Beta strand

116 – 122

7

Beta strand

133 – 141

9

Beta strand

152 – 156

5

Turn

175 – 178

4

Beta strand

179 – 183

5

Beta strand

188 – 195

8

Helix

207 – 214

8

Beta strand

223 – 230

8

Beta strand

237 – 243

7

Turn

247 – 250

4

Beta strand

266 – 268

3

Helix

271 – 276

6

Beta strand

283 – 287

5

Sequences

	Sequence		Length	Mass (Da)
	P07773-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 8999FDD3F783B4DB	FASTA	311	34,347
	10 20 30 40 50 60 MEVKIFNTQD VQDFLRVASG LEQEGGNPRV KQIIHRVLSD LYKAIEDLNI TSDEYWAGVA 70 80 90 100 110 120 YLNQLGANQE AGLLSPGLGF DHYLDMRMDA EDAALGIENA TPRTIEGPLY VAGAPESVGY 130 140 150 160 170 180 ARMDDGSDPN GHTLILHGTI FDADGKPLPN AKVEIWHANT KGFYSHFDPT GEQQAFNMRR 190 200 210 220 230 240 SIITDENGQY RVRTILPAGY GCPPEGPTQQ LLNQLGRHGN RPAHIHYFVS ADGHRKLTTQ 250 260 270 280 290 300 INVAGDPYTY DDFAYATREG LVVDAVEHTD PEAIKANDVE GPFAEMVFDL KLTRLVDGVD 310 NQVVDRPRLA V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence of the Acinetobacter calcoaceticus catechol 1,2-dioxygenase I structural gene catA: evidence for evolutionary divergence of intradiol dioxygenases by acquisition of DNA sequence repetitions." Neidle E.L., Hartnett C., Bonitz S., Ornston L.N. J. Bacteriol. 170:4874-4880(1988) [PubMed: 3170486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker." Vetting M.W., Ohlendorf D.H. Structure 8:429-440(2000) [PubMed: 10801478] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF009224 Genomic DNA. Translation: AAC46426.1.
CR543861 Genomic DNA. Translation: CAG68305.1.

RefSeq

YP_046127.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DLM	X-ray	2.00	A/B	1-311	[»]
1DLQ	X-ray	2.30	A/B	1-311	[»]
1DLT	X-ray	1.90	A/B	1-311	[»]
1DMH	X-ray	1.70	A/B	1-311	[»]

ModBase

Search...

Genome annotation databases

GeneID

2880527.

GenomeReviews

Gene locus ACIAD1442 in contig CR543861_GR.

KEGG

aci:ACIAD1442.

NMPDR

fig|62977.3.peg.799.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P07773.

OMA

P07773. NKLGQDG.

Enzyme and pathway databases

BioCyc

ASP62977:ACIAD1442-MON.

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_ACIAD

Accession

Primary (citable) accession number: P07773

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 75 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)