S00157
type: Enzyme
cath: Protocatechuate 3,4-Dioxygenase, subunit A
ec: https://purl.uniprot.org/enzyme/1.13.11.1
uniprot: P07773
kegg enzyme: catechol 1,2-dioxygenase
kegg enzyme: catechol-oxygen 1,2-oxidoreductase
kegg enzyme: 1,2-pyrocatechase
kegg enzyme: catechase
kegg enzyme: catechol 1,2-oxygenase
kegg enzyme: catechol dioxygenase
kegg enzyme: pyrocatechase
kegg enzyme: pyrocatechol 1,2-dioxygenase
kegg enzyme: CD I
kegg enzyme: CD II
kegg pathway: gamma-Hexachlorocyclohexane degradation
kegg pathway: Benzoate degradation via hydroxylation
kegg pathway: Fluorobenzoate degradation
kegg pathway: Toluene and xylene degradation
kegg pathway: 1,4-Dichlorobenzene degradation
kegg pathway: Carbazole degradation
kegg cofactor: Iron
kegg substrate: Catechol
kegg substrate: O2
kegg product: cis,cis-Muconate
pdb: 1dlmA
pdb: 1dlmB
pdb: 1dlqA
pdb: 1dlqB
pdb: 1dltA
pdb: 1dltB
pdb: 1dmhA
pdb: 1dmhB
pdb bound state: Unbound
  compound: Catechol
  pdb: 1dlmA
pdb bound state: Unbound
  compound: Catechol
  pdb: 1dlmB
pdb bound state: Unbound
  compound: Catechol
  pdb: 1dlqA
pdb bound state: Unbound
  compound: Catechol
  pdb: 1dlqB
pdb bound state: Analogue
  compound: Catechol
  pdb: 1dmhA
  ligand het code: MCT
pdb bound state: Analogue
  compound: Catechol
  pdb: 1dmhB
  ligand het code: MCT
pdb bound state: Unbound
  compound: O2
  pdb: 1dlmA
pdb bound state: Unbound
  compound: O2
  pdb: 1dlmB
pdb bound state: Unbound
  compound: O2
  pdb: 1dlqA
pdb bound state: Unbound
  compound: O2
  pdb: 1dlqB
pdb bound state: Unbound
  compound: O2
  pdb: 1dltA
pdb bound state: Unbound
  compound: O2
  pdb: 1dltB
pdb bound state: Unbound
  compound: O2
  pdb: 1dmhA
pdb bound state: Unbound
  compound: O2
  pdb: 1dmhB
pdb bound state: Unbound
  compound: cis,cis-Muconate
  pdb: 1dlmA
pdb bound state: Unbound
  compound: cis,cis-Muconate
  pdb: 1dlmB
pdb bound state: Unbound
  compound: cis,cis-Muconate
  pdb: 1dlqA
pdb bound state: Unbound
  compound: cis,cis-Muconate
  pdb: 1dlqB
pdb bound state: Unbound
  compound: cis,cis-Muconate
  pdb: 1dltA
pdb bound state: Unbound
  compound: cis,cis-Muconate
  pdb: 1dltB
pdb bound state: Unbound
  compound: cis,cis-Muconate
  pdb: 1dmhA
pdb bound state: Unbound
  compound: cis,cis-Muconate
  pdb: 1dmhB
active site residues resources: Models for extradiol cleaving catechol dioxygenases: syntheses, structures, and reactivities of iron(II)-monoanionic catecholate complexes.
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 2
  reference section: Fig.12, p.8471
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 4
  reference section: Fig.7
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 10
  reference section: Fig.3, Fig.4, p.95-96
  reference step: 6
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 14
  reference section: Fig.6, p.436
  reference step: 1
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 15
  reference section: p.3187-3189, Scheme 4
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 17
  reference section: Scheme 1, p.8291-8293
  reference step: 1
references: Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad.
references: Cleavage of pyrogallol by non-heme iron-containing dioxygenases.
references: Reactions of 3-ethylcatechol and 3-(methylthio)catechol with catechol dioxygenases.
references: Bacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657.
references: Enzymatic formation, stability, and spontaneous reactions of 4-fluoromuconolactone, a metabolite of the bacterial degradation of 4-fluorobenzoate.
references: Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance.
references: Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1.
references: Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens.
references: Purification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene.
references: Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1.
references: Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases.
references: Catalytic properties of the 3-chlorocatechol-oxidizing 2, 3-dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6.
references: Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens.
references: The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
references: Models for extradiol cleaving catechol dioxygenases: syntheses, structures, and reactivities of iron(II)-monoanionic catecholate complexes.
references: Benzothiazole degradation by Rhodococcus pyridinovorans strain PA: evidence of a catechol 1,2-dioxygenase activity.
references: Novel iron(III) complexes of tripodal and linear tetradentate bis(phenolate) ligands: close relevance to intradiol-cleaving catechol dioxygenases.

Protocatechuate 3,4-Dioxygenase, subunit A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.130.10
catalytic domain: index.html

gamma-Hexachlorocyclohexane degradation
type: KeggPathway
references: KEGG:MAP00361

Benzoate degradation via hydroxylation
type: KeggPathway
references: KEGG:MAP00362

Fluorobenzoate degradation
type: KeggPathway
references: KEGG:MAP00364

Toluene and xylene degradation
type: KeggPathway
references: KEGG:MAP00622

1,4-Dichlorobenzene degradation
type: KeggPathway
references: KEGG:MAP00627

Carbazole degradation
type: KeggPathway
references: KEGG:MAP00629

Iron
type: KeggCofactor
references: KEGG:C00023
compound type: heavy metal
references: CHEBI:18248
references: CHEBI:82664
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Catechol
type: KeggSubstrate
references: KEGG:C00090
compound type: aromatic ring (only carbon atom)
references: CHEBI:18135
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

O2
type: KeggSubstrate
references: KEGG:C00007
compound type: others
references: CHEBI:15379
references: CHEBI:26689
references: CHEBI:27140
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

cis,cis-Muconate
type: KeggProduct
references: KEGG:C02480
compound type: carboxyl group
references: CHEBI:16508
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1dlmA
type: Pdb
references: 1dlm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dlm
catalytic residue: TYR 200;ARG 221
cofactor binding residue: TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

1dlmB
type: Pdb
references: 1dlm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dlm
catalytic residue: TYR 200;ARG 221
cofactor binding residue: TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

1dlqA
type: Pdb
references: 1dlq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dlq
catalytic residue: TYR 200;ARG 221
cofactor binding residue: TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

1dlqB
type: Pdb
references: 1dlq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dlq
catalytic residue: TYR 200;ARG 221
cofactor binding residue: TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

1dltA
type: Pdb
references: 1dlt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dlt
catalytic residue: TYR 200;ARG 221
cofactor binding residue: TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

1dltB
type: Pdb
references: 1dlt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dlt
catalytic residue: TYR 200;ARG 221
cofactor binding residue: TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

1dmhA
type: Pdb
references: 1dmh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dmh
catalytic residue: TYR 200;ARG 221
cofactor binding residue: TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

1dmhB
type: Pdb
references: 1dmh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dmh
catalytic residue: TYR 200;ARG 221
cofactor binding residue: TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/238971
journal: J Biol Chem
volume: 250
pages: 4848-55
published year: 1975
authors:
  item: Fujiwara M
  item: Golovleva LA
  item: Saeki Y
  item: Nozaki M
  item: Hayaishi O

Cleavage of pyrogallol by non-heme iron-containing dioxygenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6773944
journal: J Biol Chem
volume: 255
pages: 8465-71
published year: 1980
authors:
  item: Saeki Y
  item: Nozaki M
  item: Senoh S

Reactions of 3-ethylcatechol and 3-(methylthio)catechol with catechol dioxygenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3015028
journal: Arch Biochem Biophys
volume: 248
pages: 130-7
published year: 1986
authors:
  item: Pascal RA Jr
  item: Huang DS

Bacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3365096
journal: Arch Microbiol
volume: 149
pages: 188-97
published year: 1988
authors:
  item: Engesser KH
  item: Cain RB
  item: Knackmuss HJ

Enzymatic formation, stability, and spontaneous reactions of 4-fluoromuconolactone, a metabolite of the bacterial degradation of 4-fluorobenzoate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2394680
journal: J Bacteriol
volume: 172
pages: 5119-29
published year: 1990
authors:
  item: Schlomann M
  item: Fischer P
  item: Schmidt E
  item: Knackmuss HJ

Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1649626
journal: Biochemistry
volume: 30
pages: 7349-58
published year: 1991
authors:
  item: Broderick JB
  item: O'Halloran TV

Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8107120
journal: J Mol Biol
volume: 236
pages: 377-8
published year: 1994
authors:
  item: Earhart CA
  item: Hall MD
  item: Michaud-Soret I
  item: Que L Jr
  item: Ohlendorf DH

Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9369233
journal: FEBS Lett
volume: 416
pages: 61-4
published year: 1997
authors:
  item: Briganti F
  item: Pessione E
  item: Giunta C
  item: Scozzafava A

Purification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9677336
journal: Biochem J
volume: 333
pages: 741-7
published year: 1998
authors:
  item: Strachan PD
  item: Freer AA
  item: Fewson CA

Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9799107
journal: Eur J Biochem
volume: 257
pages: 92-100
published year: 1998
authors:
  item: Ridder L
  item: Briganti F
  item: Boersma MG
  item: Boeren S
  item: Vis EH
  item: Scozzafava A
  item: Veeger C
  item: Rietjens IM

Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10515940
journal: J Bacteriol
volume: 181
pages: 6478-87
published year: 1999
authors:
  item: D'Argenio DA
  item: Vetting MW
  item: Ohlendorf DH
  item: Ornston LN

Catalytic properties of the 3-chlorocatechol-oxidizing 2, 3-dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10438749
journal: J Bacteriol
volume: 181
pages: 4812-7
published year: 1999
authors:
  item: Riegert U
  item: Heiss G
  item: Kuhm AE
  item: Muller C
  item: Contzen M
  item: Knackmuss HJ
  item: Stolz A

Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11307956
journal: J Protein Chem
volume: 19
pages: 709-16
published year: 2000
authors:
  item: Briganti F
  item: Pessione E
  item: Giunta C
  item: Mazzoli R
  item: Scozzafava A

The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10801478
journal: Structure Fold Des
volume: 8
pages: 429-40
published year: 2000
authors:
  item: Vetting MW
  item: Ohlendorf DH
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07773

Models for extradiol cleaving catechol dioxygenases: syntheses, structures, and reactivities of iron(II)-monoanionic catecholate complexes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11399191
journal: Inorg Chem
volume: 40
pages: 3181-90
published year: 2001
authors:
  item: Jo DH
  item: Chiou YM
  item: Que L Jr

Benzothiazole degradation by Rhodococcus pyridinovorans strain PA: evidence of a catechol 1,2-dioxygenase activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12450835
journal: Appl Environ Microbiol
volume: 68
pages: 6114-20
published year: 2002
authors:
  item: Haroune N
  item: Combourieu B
  item: Besse P
  item: Sancelme M
  item: Reemtsma T
  item: Kloepfer A
  item: Diab A
  item: Knapp JS
  item: Baumberg S
  item: Delort AM

Novel iron(III) complexes of tripodal and linear tetradentate bis(phenolate) ligands: close relevance to intradiol-cleaving catechol dioxygenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14658880
journal: Inorg Chem
volume: 42
pages: 8283-93
published year: 2003
authors:
  item: Velusamy M
  item: Palaniandavar M
  item: Gopalan RS
  item: Kulkarni GU