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P00436 (PCXA_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protocatechuate 3,4-dioxygenase alpha chain

EC=1.13.11.3
Alternative name(s):
3,4-PCD
Gene names
Name:pcaG
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.

Catalytic activity

3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate.

Cofactor

Binds Fe3+ ion per subunit.

Pathway

Aromatic compound metabolism; beta-ketoadipate pathway; 3-carboxy-cis,cis-muconate from 3,4-dihydroxybenzoate: step 1/1.

Subunit structure

The enzyme is an oligomer of 12 copies of the alpha and beta chains.

Sequence similarities

Belongs to the intradiol ring-cleavage dioxygenase family.

Caution

Strain ATCC 23975 was originally classified as being from Pseudomonas aeruginosa.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandIron
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processbeta-ketoadipate pathway

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

protocatechuate 3,4-dioxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 201200Protocatechuate 3,4-dioxygenase alpha chain
PRO_0000085095

Sites

Binding site1341Protocatechuate Potential

Experimental info

Sequence conflict601N → D AA sequence Ref.2
Sequence conflict771N → D AA sequence Ref.2

Secondary structure

................................. 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00436 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BF95DB892076FBAF

FASTA20122,387
        10         20         30         40         50         60 
MPIELLPETP SQTAGPYVHI GLALEAAGNP TRDQEIWNRL AKPDAPGEHI LLLGQVYDGN 

        70         80         90        100        110        120 
GHLVRDSFLE VWQADANGEY QDAYNLENAF NSFGRTATTF DAGEWTLHTV KPGVVNNAAG 

       130        140        150        160        170        180 
VPMAPHINIS LFARGINIHL HTRLYFDDEA QANAKCPVLN LIEQPQRRET LIAKRCEVDG 

       190        200 
KTAYRFDIRI QGEGETVFFD F 

« Hide

References

[1]"Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes."
Frazee R.W., Livingston D.M., Laporte D.C., Lipscomb J.D.
J. Bacteriol. 175:6194-6202(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
[2]"The primary structure of the alpha subunit of protocatechuate 3,4-dioxygenase. II. Isolation and sequence of overlap peptides and complete sequence."
Kohlmiller N.A., Howard J.B.
J. Biol. Chem. 254:7309-7315(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-201.
Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
[3]"Structure and assembly of protocatechuate 3,4-dioxygenase."
Ohlendorf D.H., Lipscomb J.D., Weber P.C.
Nature 336:403-405(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[4]"Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15-A resolution."
Ohlendorf D.H., Orville A.M., Lipscomb J.D.
J. Mol. Biol. 244:586-608(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
[5]"Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site."
Orville A.M., Elango N., Lipscomb J.D., Ohlendorf D.H.
Biochemistry 36:10039-10051(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
[6]"Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding."
Orville A.M., Lipscomb J.D., Ohlendorf D.H.
Biochemistry 36:10052-10066(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS).
Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
[7]"Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate."
Elgren T.E., Orville A.M., Kelly K.A., Lipscomb J.D., Ohlendorf D.H., Que L. Jr.
Biochemistry 36:11504-11513(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14836 Genomic DNA. Translation: AAB41025.1.
PIRDAPSAA. B36930.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YKKX-ray2.06A/C/E/G/I/K2-200[»]
1YKLX-ray2.25A/C/E/G/I/K2-200[»]
1YKMX-ray2.22A/C/E/G/I/K2-200[»]
1YKNX-ray2.06A/C/E/G/I/K2-200[»]
1YKOX-ray2.54A/C/E/G/I/K2-200[»]
1YKPX-ray2.41A/C/E/G/I/K2-200[»]
2PCDX-ray2.15A/B/C/D/E/F2-201[»]
3LKTX-ray1.65A/B/C/D/E/F2-201[»]
3LMXX-ray2.20A/B/C2-201[»]
3LXVX-ray1.90A/B/C2-201[»]
3MFLX-ray1.78A/B/C2-201[»]
3MI1X-ray1.74A/B/C2-201[»]
3MI5X-ray1.78A/B/C/D/E/F2-201[»]
3MV4X-ray1.59A/B/C2-201[»]
3MV6X-ray1.86A/B/C2-201[»]
3PCAX-ray2.20A/B/C/D/E/F2-201[»]
3PCBX-ray2.19A/B/C/D/E/F2-201[»]
3PCCX-ray1.98A/B/C/D/E/F2-201[»]
3PCDX-ray2.10A/B/C/D/E/F2-200[»]
3PCEX-ray2.06A/B/C/D/E/F2-201[»]
3PCFX-ray2.15A/B/C/D/E/F2-201[»]
3PCGX-ray1.96A/B/C/D/E/F2-201[»]
3PCHX-ray2.05A/B/C/D/E/F2-201[»]
3PCIX-ray2.21A/B/C/D/E/F2-201[»]
3PCJX-ray2.13A/B/C/D/E/F2-201[»]
3PCKX-ray2.13A/B/C/D/E/F2-201[»]
3PCLX-ray2.15A/B/C/D/E/F2-201[»]
3PCMX-ray2.25A/B/C/D/E/F2-201[»]
3PCNX-ray2.40A/B/C/D/E/F2-201[»]
3T63X-ray1.54A/B/C2-201[»]
3T67X-ray1.67A/B/C2-201[»]
ProteinModelPortalP00436.
SMRP00436. Positions 2-201.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00436. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3186.
UniPathwayUPA00157; UER00264.

Family and domain databases

Gene3D2.60.130.10. 1 hit.
InterProIPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
IPR012786. Protocat_dOase_a.
[Graphical view]
PfamPF00775. Dioxygenase_C. 1 hit.
[Graphical view]
SUPFAMSSF49482. SSF49482. 1 hit.
TIGRFAMsTIGR02423. protocat_alph. 1 hit.
PROSITEPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00436.

Entry information

Entry namePCXA_PSEPU
AccessionPrimary (citable) accession number: P00436
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways