DB code: S00157

CATH domain 2.60.130.10 : Protocatechuate 3,4-Dioxygenase, subunit A Catalytic domain
E.C. 1.13.11.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P07773 Catechol 1,2-dioxygenase
EC 1.13.11.1
1,2-CTD
YP_046127.1 (Protein)
NC_005966.1 (DNA/RNA sequence)
PF00775 (Dioxygenase_C)
PF04444 (Dioxygenase_N)
[Graphical View]

KEGG enzyme name
catechol 1,2-dioxygenase
catechol-oxygen 1,2-oxidoreductase
1,2-pyrocatechase
catechase
catechol 1,2-oxygenase
catechol dioxygenase
pyrocatechase
pyrocatechol 1,2-dioxygenase
CD I
CD II

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P07773 CATA_ACIAD Catechol + O(2) = cis,cis-muconate. Homodimer. Binds 1 Fe(3+) ion per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00364 Fluorobenzoate degradation
MAP00622 Toluene and xylene degradation
MAP00627 1,4-Dichlorobenzene degradation
MAP00629 Carbazole degradation
MAP00361 gamma-Hexachlorocyclohexane degradation
MAP00362 Benzoate degradation via hydroxylation

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00023 C00090 C00007 C02480
E.C.
Compound Iron Catechol O2 cis,cis-Muconate
Type heavy metal aromatic ring (only carbon atom) others carboxyl group
ChEBI 18248
82664
18135
15379
26689
27140
16508
PubChem 23925
289
977
5280518
1dlmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Unbound Unbound Unbound
1dlmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Unbound Unbound Unbound
1dlqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Unbound Unbound Unbound
1dlqB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Unbound Unbound Unbound
1dltA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Bound:CAQ Unbound Unbound
1dltB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Bound:CAQ Unbound Unbound
1dmhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Analogue:MCT Unbound Unbound
1dmhB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Analogue:MCT Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [14]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dlmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dlmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dlqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dlqB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dltA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dltB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dmhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dmhB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.12, p.8471
[4]
Fig.7
[10]
Fig.3, Fig.4, p.95-96 6
[14]
Fig.6, p.436 1
[15]
p.3187-3189, Scheme 4
[17]
Scheme 1, p.8291-8293 1

References
[1]
Resource
Comments
Medline ID
PubMed ID 238971
Journal J Biol Chem
Year 1975
Volume 250
Pages 4848-55
Authors Fujiwara M, Golovleva LA, Saeki Y, Nozaki M, Hayaishi O
Title Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 6773944
Journal J Biol Chem
Year 1980
Volume 255
Pages 8465-71
Authors Saeki Y, Nozaki M, Senoh S
Title Cleavage of pyrogallol by non-heme iron-containing dioxygenases.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 3015028
Journal Arch Biochem Biophys
Year 1986
Volume 248
Pages 130-7
Authors Pascal RA Jr, Huang DS
Title Reactions of 3-ethylcatechol and 3-(methylthio)catechol with catechol dioxygenases.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 3365096
Journal Arch Microbiol
Year 1988
Volume 149
Pages 188-97
Authors Engesser KH, Cain RB, Knackmuss HJ
Title Bacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 2394680
Journal J Bacteriol
Year 1990
Volume 172
Pages 5119-29
Authors Schlomann M, Fischer P, Schmidt E, Knackmuss HJ
Title Enzymatic formation, stability, and spontaneous reactions of 4-fluoromuconolactone, a metabolite of the bacterial degradation of 4-fluorobenzoate.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 1649626
Journal Biochemistry
Year 1991
Volume 30
Pages 7349-58
Authors Broderick JB, O'Halloran TV
Title Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8107120
Journal J Mol Biol
Year 1994
Volume 236
Pages 377-8
Authors Earhart CA, Hall MD, Michaud-Soret I, Que L Jr, Ohlendorf DH
Title Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 9369233
Journal FEBS Lett
Year 1997
Volume 416
Pages 61-4
Authors Briganti F, Pessione E, Giunta C, Scozzafava A
Title Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 9677336
Journal Biochem J
Year 1998
Volume 333
Pages 741-7
Authors Strachan PD, Freer AA, Fewson CA
Title Purification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 9799107
Journal Eur J Biochem
Year 1998
Volume 257
Pages 92-100
Authors Ridder L, Briganti F, Boersma MG, Boeren S, Vis EH, Scozzafava A, Veeger C, Rietjens IM
Title Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 10515940
Journal J Bacteriol
Year 1999
Volume 181
Pages 6478-87
Authors D'Argenio DA, Vetting MW, Ohlendorf DH, Ornston LN
Title Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 10438749
Journal J Bacteriol
Year 1999
Volume 181
Pages 4812-7
Authors Riegert U, Heiss G, Kuhm AE, Muller C, Contzen M, Knackmuss HJ, Stolz A
Title Catalytic properties of the 3-chlorocatechol-oxidizing 2, 3-dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11307956
Journal J Protein Chem
Year 2000
Volume 19
Pages 709-16
Authors Briganti F, Pessione E, Giunta C, Mazzoli R, Scozzafava A
Title Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10801478
Journal Structure Fold Des
Year 2000
Volume 8
Pages 429-40
Authors Vetting MW, Ohlendorf DH
Title The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
Related PDB 1dlm 1dlq 1dlt 1dmh
Related UniProtKB P07773
[15]
Resource
Comments
Medline ID
PubMed ID 11399191
Journal Inorg Chem
Year 2001
Volume 40
Pages 3181-90
Authors Jo DH, Chiou YM, Que L Jr
Title Models for extradiol cleaving catechol dioxygenases: syntheses, structures, and reactivities of iron(II)-monoanionic catecholate complexes.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 12450835
Journal Appl Environ Microbiol
Year 2002
Volume 68
Pages 6114-20
Authors Haroune N, Combourieu B, Besse P, Sancelme M, Reemtsma T, Kloepfer A, Diab A, Knapp JS, Baumberg S, Delort AM
Title Benzothiazole degradation by Rhodococcus pyridinovorans strain PA: evidence of a catechol 1,2-dioxygenase activity.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 14658880
Journal Inorg Chem
Year 2003
Volume 42
Pages 8283-93
Authors Velusamy M, Palaniandavar M, Gopalan RS, Kulkarni GU
Title Novel iron(III) complexes of tripodal and linear tetradentate bis(phenolate) ligands: close relevance to intradiol-cleaving catechol dioxygenases.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-07-07 2009-03-19