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P37334 (BPHE_BURXL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biphenyl dioxygenase subunit beta

EC=1.14.12.18
Alternative name(s):
Biphenyl 2,3-dioxygenase
Gene names
Name:bphE
Ordered Locus Names:Bxeno_C1130
ORF Names:Bxe_C1196
OrganismBurkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]
Taxonomic identifier266265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The beta subunit may be responsible for the substrate specificity of the enzyme.

Catalytic activity

Biphenyl + NADH + O2 = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+.

Pathway

Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl: step 1/4.

Subunit structure

Heterohexamer consisting of three BphA subunits and three BphE subunits. A ferredoxin (BphF) and a ferredoxin reductase (BphG) must be present to obtain activity.

Sequence similarities

Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.

Sequence caution

The sequence ABE37058.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 188187Biphenyl dioxygenase subunit beta
PRO_0000085068

Secondary structure

......................... 188
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37334 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 36DBE14E22FEA67B

FASTA18822,085
        10         20         30         40         50         60 
MTNPSPHFFK TFEWPSKAAG LELQNEIEQF YYREAQLLDH RAYEAWFALL DKDIHYFMPL 

        70         80         90        100        110        120 
RTNRMIREGE LEYSGDQDLA HFDETHETMY GRIRKVTSDV GWAENPPSRT RHLVSNVIVK 

       130        140        150        160        170        180 
ETATPDTFEV NSAFILYRNR LERQVDIFAG ERRDVLRRAD NNLGFSIAKR TILLDASTLL 


SNNLSMFF 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequencing and transcriptional mapping of the genes encoding biphenyl dioxygenase, a multicomponent polychlorinated-biphenyl-degrading enzyme in Pseudomonas strain LB400."
Erickson B.D., Mondello F.J.
J. Bacteriol. 174:2903-2912(1992) [PubMed: 1569021] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility."
Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J. expand/collapse author list , Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006) [PubMed: 17030797] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LB400.
[3]"Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400."
Haddock J.D., Gibson D.T.
J. Bacteriol. 177:5834-5839(1995) [PubMed: 7592331] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12, CHARACTERIZATION.
[4]Erratum
Haddock J.D., Gibson D.T.
J. Bacteriol. 178:258-258(1996)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86348 Genomic DNA. Translation: AAB63426.1.
CP000272 Genomic DNA. Translation: ABE37058.1. Different initiation.
RefSeqYP_556408.1. NC_007953.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XR8X-ray2.49B/D/F/H/J/L/N/P/R/T/V/X1-188[»]
2XRXX-ray2.42B/D/F/H/J/L/N/P/R/T/V/X1-188[»]
2XSHX-ray2.29B/D/F/H/J/L1-188[»]
2XSOX-ray2.20B/D/F/H/J/L/N/P/R/T/V/X1-188[»]
2YFIX-ray2.15B/D/F/H/J/L1-188[»]
2YFJX-ray2.15B/D/F/H/J/L1-188[»]
ProteinModelPortalP37334.
SMRP37334. Positions 10-188.
ModBaseSearch...

Protein-protein interaction databases

STRINGP37334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4010708.
GenomeReviewsGene locus Bxeno_C1130 in contig CP000272_GR.
KEGGbxe:Bxe_C1196.
PATRIC19343377. VBIBurXen52548_8946.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG582498.
OMADIFAGER.
ProtClustDBCLSK922463.

Enzyme and pathway databases

BioCycBXEN266265:BXE_C1196-MONOMER.

Family and domain databases

InterProIPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
KOK08689.
PfamPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBPHE_BURXL
AccessionPrimary (citable) accession number: P37334
Secondary accession number(s): Q13FT1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 75 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families