EzCatDB: D00063
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DB codeD00063
CATH domainDomain 11.10.700.10 : Protocatechuate 4,5-dioxygenase; Chain A
Domain 23.40.830.10 : Protocatechuate 4,5-dioxygenase; Chain BCatalytic domain
E.C.1.13.11.8
CSA1bou


Enzyme Name
UniProtKBKEGG

P22635P22636
Protein nameProtocatechuate 4,5-dioxygenase alpha chainProtocatechuate 4,5-dioxygenase beta chainprotocatechuate 4,5-dioxygenase
protocatechuate 4,5-oxygenase
protocatechuic 4,5-dioxygenase
protocatechuic 4,5-oxygenase
SynonymsEC 1.13.11.8
4,5-PCD
EC 1.13.11.8
4,5-PCD
PfamPF07746 (LigA)
[Graphical view]
PF02900 (LigB)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00362Benzoate degradation via hydroxylation
MAP006232,4-Dichlorobenzoate degradation

UniProtKB:Accession NumberP22635P22636
Entry namePCYA_PSEPAPCYB_PSEPA
ActivityProtocatechuate + O(2) = 4-carboxy-2- hydroxymuconate semialdehyde.Protocatechuate + O(2) = 4-carboxy-2- hydroxymuconate semialdehyde.
SubunitComposed of two subunits (alpha and beta) in a 1:1 ratio.Composed of two subunits (alpha and beta) in a 1:1 ratio.
Subcellular location

CofactorFe(2+) ion.Fe(2+) ion.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00023C00230C00007C04484
CompoundIronProtocatechuateO24-Carboxy-2-hydroxymuconate semialdehyde
Typeheavy metalaromatic ring (only carbon atom),carboxyl groupotherscarbohydrate,carboxyl group
ChEBI18248
82664
36062
27140
26689
15379
18046
PubChem23925
72
977

            
1b4uAUnboundUnboundUnboundUnbound
1b4uCUnboundUnboundUnboundUnbound
1bouAUnboundUnboundUnboundUnbound
1bouCUnboundUnboundUnboundUnbound
1b4uBBound:_FEBound:DHBUnboundUnbound
1b4uDBound:_FEBound:DHBUnboundUnbound
1bouBBound:_FEUnboundUnboundUnbound
1bouDBound:_FEUnboundUnboundUnbound

Active-site residues
resource
literature [5]
pdbCatalytic residuesCofactor-binding residues
          
1b4uA 
 
1b4uC 
 
1bouA 
 
1bouC 
 
1b4uBHIS 127;HIS 195
HIS 12;HIS 61;GLU 242(Iron binding)
1b4uDHIS 127;HIS 195
HIS 12;HIS 61;GLU 242(Iron binding)
1bouBHIS 127;HIS 195
HIS 12;HIS 61;GLU 242(Iron binding)
1bouDHIS 127;HIS 195
HIS 12;HIS 61;GLU 242(Iron binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.14989
[3]Scheme 2, p.2177
[5]p.962-965

references
[1]
PubMed ID6317682
JournalJ Biol Chem
Year1983
Volume258
Pages14981-91
AuthorsArciero DM, Lipscomb JD, Huynh BH, Kent TA, Munck E
TitleEPR and Mossbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environment.
[2]
PubMed ID2997190
JournalJ Biol Chem
Year1985
Volume260
Pages14035-44
AuthorsArciero DM, Orville AM, Lipscomb JD
Title17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases.
[3]
PubMed ID3003098
JournalJ Biol Chem
Year1986
Volume261
Pages2170-8
AuthorsArciero DM, Lipscomb JD
TitleBinding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases.
[4]
PubMed ID2280721
JournalMethods Enzymol
Year1990
Volume188
Pages89-95
AuthorsArciero DM, Orville AM, Lipscomb JD
TitleProtocatechuate 4,5-dioxygenase from Pseudomonas testosteroni.
[5]
CommentsX-ray crystallography
PubMed ID10467151
JournalStructure Fold Des
Year1999
Volume7
Pages953-65
AuthorsSugimoto K, Senda T, Aoshima H, Masai E, Fukuda M, Mitsui Y
TitleCrystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions.
Related PDB1b4u,1bou

comments
The catalytic mechanism might be similar to Biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39, D00448 in EzCatDB), although the structure of this enzyme is not similar to that.
Physical and catalytic properties of the R. leguminosarum protocatechuate 4,5-dioxygenase were different from the characteristics of isofunctional enzymes from Pseudomonas paucimobilis and Comamonas testosteroni (Archives of Microbiology 161:191-195).

createdupdated
2004-05-122009-02-26


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