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P00437 (PCXB_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. 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 beta chain

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

Protein attributes

Sequence length239 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 239238Protocatechuate 3,4-dioxygenase beta chain
PRO_0000085098

Sites

Metal binding1091Iron; catalytic Ref.4
Metal binding1481Iron; catalytic Ref.4
Metal binding1611Iron; catalytic Ref.4
Metal binding1631Iron; catalytic Ref.4

Experimental info

Sequence conflict621H → D AA sequence Ref.2
Sequence conflict701N → D AA sequence Ref.2
Sequence conflict721Missing AA sequence Ref.2
Sequence conflict2181D → N AA sequence Ref.2

Secondary structure

................................................... 239
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00437 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8F8CC293B6E434CE

FASTA23926,793
        10         20         30         40         50         60 
MPAQDNSRFV IRDRNWHPKA LTPDYKTSIA RSPRQALVSI PQSISETTGP NFSHLGFGAH 

        70         80         90        100        110        120 
DHDLLLNFNN GGLPIGERII VAGRVVDQYG KPVPNTLVEM WQANAGGRYR HKNDRYLAPL 

       130        140        150        160        170        180 
DPNFGGVGRC LTDSDGYYSF RTIKPGPYPW RNGPNDWRPA HIHFGISGPS IATKLITQLY 

       190        200        210        220        230 
FEGDPLIPMC PIVKSIANPE AVQQLIAKLD MNNANPMDCL AYRFDIVLRG QRKTHFENC 

« 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 complete amino acid sequence of the beta-subunit of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa."
Iwaki M., Kagamiyama H., Nozaki M.
J. Biochem. 86:1159-1162(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-239.
[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: AAB41024.1.
PIRDAPSBA. A36930.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YKKX-ray2.06B/D/F/H/J/L2-239[»]
1YKLX-ray2.25B/D/F/H/J/L2-239[»]
1YKMX-ray2.22B/D/F/H/J/L2-239[»]
1YKNX-ray2.06B/D/F/H/J/L2-239[»]
1YKOX-ray2.54B/D/F/H/J/L2-239[»]
1YKPX-ray2.41B/D/F/H/J/L2-239[»]
2PCDX-ray2.15M/N/O/P/Q/R2-239[»]
3LKTX-ray1.65M/N/O/P/Q/R2-239[»]
3LMXX-ray2.20M/N/O2-239[»]
3LXVX-ray1.90M/N/O2-239[»]
3MFLX-ray1.78M/N/O2-239[»]
3MI1X-ray1.74M/N/O2-239[»]
3MI5X-ray1.78M/N/O/P/Q/R2-239[»]
3MV4X-ray1.59M/N/O2-239[»]
3MV6X-ray1.86M/N/O2-239[»]
3PCAX-ray2.20M/N/O/P/Q/R2-239[»]
3PCBX-ray2.19M/N/O/P/Q/R2-239[»]
3PCCX-ray1.98M/N/O/P/Q/R2-239[»]
3PCDX-ray2.10M/N/O/P/Q/R2-239[»]
3PCEX-ray2.06M/N/O/P/Q/R2-239[»]
3PCFX-ray2.15M/N/O/P/Q/R2-239[»]
3PCGX-ray1.96M/N/O/P/Q/R2-239[»]
3PCHX-ray2.05M/N/O/P/Q/R2-239[»]
3PCIX-ray2.21M/N/O/P/Q/R2-239[»]
3PCJX-ray2.13M/N/O/P/Q/R2-239[»]
3PCKX-ray2.13M/N/O/P/Q/R2-239[»]
3PCLX-ray2.15M/N/O/P/Q/R2-239[»]
3PCMX-ray2.25M/N/O/P/Q/R2-239[»]
3PCNX-ray2.40M/N/O/P/Q/R2-239[»]
3T63X-ray1.54M/N/O2-239[»]
3T67X-ray1.67M/N/O2-239[»]
ProteinModelPortalP00437.
SMRP00437. Positions 2-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00437. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3185.
RETL1328306-WGS:GSTH-5905-MONOMER.
UniPathwayUPA00157; UER00264.

Family and domain databases

Gene3D2.60.130.10. 1 hit.
InterProIPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
IPR024756. PCDO_beta_N.
IPR012785. Protocat_dOase_b.
[Graphical view]
PfamPF00775. Dioxygenase_C. 1 hit.
PF12391. PCDO_beta_N. 1 hit.
[Graphical view]
SUPFAMSSF49482. SSF49482. 1 hit.
TIGRFAMsTIGR02422. protocat_beta. 1 hit.
PROSITEPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00437.

Entry information

Entry namePCXB_PSEPU
AccessionPrimary (citable) accession number: P00437
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 99 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