EzCatDB: S00157
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DB codeS00157
CATH domainDomain 12.60.130.10 : Protocatechuate 3,4-Dioxygenase, subunit ACatalytic domain
E.C.1.13.11.1


Enzyme Name
UniProtKBKEGG

P07773
Protein nameCatechol 1,2-dioxygenasecatechol 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
SynonymsEC 1.13.11.1
1,2-CTD
RefSeqYP_046127.1 (Protein)
NC_005966.1 (DNA/RNA sequence)
PfamPF00775 (Dioxygenase_C)
PF04444 (Dioxygenase_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00361gamma-Hexachlorocyclohexane degradation
MAP00362Benzoate degradation via hydroxylation
MAP00364Fluorobenzoate degradation
MAP00622Toluene and xylene degradation
MAP006271,4-Dichlorobenzene degradation
MAP00629Carbazole degradation

UniProtKB:Accession NumberP07773
Entry nameCATA_ACIAD
ActivityCatechol + O(2) = cis,cis-muconate.
SubunitHomodimer.
Subcellular location
CofactorBinds 1 Fe(3+) ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00023C00090C00007C02480
CompoundIronCatecholO2cis,cis-Muconate
Typeheavy metalaromatic ring (only carbon atom)otherscarboxyl group
ChEBI18248
82664
18135
27140
26689
15379
16508
PubChem23925
289
977
5280518
            
1dlmABound:_FEUnboundUnboundUnbound
1dlmBBound:_FEUnboundUnboundUnbound
1dlqABound:_FEUnboundUnboundUnbound
1dlqBBound:_FEUnboundUnboundUnbound
1dltABound:_FEBound:CAQUnboundUnbound
1dltBBound:_FEBound:CAQUnboundUnbound
1dmhABound:_FEAnalogue:MCTUnboundUnbound
1dmhBBound:_FEAnalogue:MCTUnboundUnbound

Active-site residues
resource
literature [14]
pdbCatalytic residuesCofactor-binding residues
          
1dlmATYR 200;ARG 221
TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dlmBTYR 200;ARG 221
TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dlqATYR 200;ARG 221
TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dlqBTYR 200;ARG 221
TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dltATYR 200;ARG 221
TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dltBTYR 200;ARG 221
TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dmhATYR 200;ARG 221
TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dmhBTYR 200;ARG 221
TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.12, p.8471
[4]Fig.7
[10]Fig.3, Fig.4, p.95-966
[14]Fig.6, p.4361
[15]p.3187-3189, Scheme 4
[17]Scheme 1, p.8291-82931

references
[1]
PubMed ID238971
JournalJ Biol Chem
Year1975
Volume250
Pages4848-55
AuthorsFujiwara M, Golovleva LA, Saeki Y, Nozaki M, Hayaishi O
TitleExtradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad.
[2]
PubMed ID6773944
JournalJ Biol Chem
Year1980
Volume255
Pages8465-71
AuthorsSaeki Y, Nozaki M, Senoh S
TitleCleavage of pyrogallol by non-heme iron-containing dioxygenases.
[3]
PubMed ID3015028
JournalArch Biochem Biophys
Year1986
Volume248
Pages130-7
AuthorsPascal RA Jr, Huang DS
TitleReactions of 3-ethylcatechol and 3-(methylthio)catechol with catechol dioxygenases.
[4]
PubMed ID3365096
JournalArch Microbiol
Year1988
Volume149
Pages188-97
AuthorsEngesser KH, Cain RB, Knackmuss HJ
TitleBacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657.
[5]
PubMed ID2394680
JournalJ Bacteriol
Year1990
Volume172
Pages5119-29
AuthorsSchlomann M, Fischer P, Schmidt E, Knackmuss HJ
TitleEnzymatic formation, stability, and spontaneous reactions of 4-fluoromuconolactone, a metabolite of the bacterial degradation of 4-fluorobenzoate.
[6]
PubMed ID1649626
JournalBiochemistry
Year1991
Volume30
Pages7349-58
AuthorsBroderick JB, O'Halloran TV
TitleOverproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance.
[7]
PubMed ID8107120
JournalJ Mol Biol
Year1994
Volume236
Pages377-8
AuthorsEarhart CA, Hall MD, Michaud-Soret I, Que L Jr, Ohlendorf DH
TitleCrystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1.
[8]
PubMed ID9369233
JournalFEBS Lett
Year1997
Volume416
Pages61-4
AuthorsBriganti F, Pessione E, Giunta C, Scozzafava A
TitlePurification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens.
[9]
PubMed ID9677336
JournalBiochem J
Year1998
Volume333
Pages741-7
AuthorsStrachan PD, Freer AA, Fewson CA
TitlePurification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene.
[10]
PubMed ID9799107
JournalEur J Biochem
Year1998
Volume257
Pages92-100
AuthorsRidder L, Briganti F, Boersma MG, Boeren S, Vis EH, Scozzafava A, Veeger C, Rietjens IM
TitleQuantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1.
[11]
PubMed ID10515940
JournalJ Bacteriol
Year1999
Volume181
Pages6478-87
AuthorsD'Argenio DA, Vetting MW, Ohlendorf DH, Ornston LN
TitleSubstitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases.
[12]
PubMed ID10438749
JournalJ Bacteriol
Year1999
Volume181
Pages4812-7
AuthorsRiegert U, Heiss G, Kuhm AE, Muller C, Contzen M, Knackmuss HJ, Stolz A
TitleCatalytic properties of the 3-chlorocatechol-oxidizing 2, 3-dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6.
[13]
PubMed ID11307956
JournalJ Protein Chem
Year2000
Volume19
Pages709-16
AuthorsBriganti F, Pessione E, Giunta C, Mazzoli R, Scozzafava A
TitlePurification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens.
[14]
CommentsX-ray crystallography
PubMed ID10801478
JournalStructure Fold Des
Year2000
Volume8
Pages429-40
AuthorsVetting MW, Ohlendorf DH
TitleThe 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
Related PDB1dlm,1dlq,1dlt,1dmh
Related UniProtKBP07773
[15]
PubMed ID11399191
JournalInorg Chem
Year2001
Volume40
Pages3181-90
AuthorsJo DH, Chiou YM, Que L Jr
TitleModels for extradiol cleaving catechol dioxygenases: syntheses, structures, and reactivities of iron(II)-monoanionic catecholate complexes.
[16]
PubMed ID12450835
JournalAppl Environ Microbiol
Year2002
Volume68
Pages6114-20
AuthorsHaroune N, Combourieu B, Besse P, Sancelme M, Reemtsma T, Kloepfer A, Diab A, Knapp JS, Baumberg S, Delort AM
TitleBenzothiazole degradation by Rhodococcus pyridinovorans strain PA: evidence of a catechol 1,2-dioxygenase activity.
[17]
PubMed ID14658880
JournalInorg Chem
Year2003
Volume42
Pages8283-93
AuthorsVelusamy M, Palaniandavar M, Gopalan RS, Kulkarni GU
TitleNovel iron(III) complexes of tripodal and linear tetradentate bis(phenolate) ligands: close relevance to intradiol-cleaving catechol dioxygenases.


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2004-07-072009-03-19


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