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P47228 (BPHC_BURXL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. 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-2,3-diol 1,2-dioxygenase
EC=1.13.11.39
Alternative name(s):
2,3-dihydroxybiphenyl dioxygenase
Short name=DHBD
23OHBP oxygenase
Gene names
Name:bphC
Ordered Locus Names:Bxeno_C1125
ORF Names:Bxe_C1191
OrganismBurkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]
Taxonomic identifier266265 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Shows a preference for catechols with groups immediately adjacent to the hydroxyl substituents.

Catalytic activity

Biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate.

Cofactor

Binds 1 Fe2+ ion per subunit.

Pathway

Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl: step 3/4.

Subunit structure

Homooctamer. The enzyme is composed of two planar tetramers rotated at 45 degrees relative to each other, with a channel in the middle. Ref.3

Sequence similarities

Belongs to the extradiol ring-cleavage dioxygenase family.

Biophysicochemical properties

Kinetic parameters:

Substrate inhibition occurs at 300 µM (+/- 20 µM).

KM=7 µM for biphenyl-2,3-diol

pH dependence:

Optimum pH is 8.0.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 298297Biphenyl-2,3-diol 1,2-dioxygenase
PRO_0000085033

Sites

Metal binding1461Iron
Metal binding2101Iron
Metal binding2601Iron

Secondary structure

1 .................................................. 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P47228 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: ADC0E4709E193FAB

FASTA29832,471
        10         20         30         40         50         60 
MSIRSLGYMG FAVSDVAAWR SFLTQKLGLM EAGTTDNGDL FRIDSRAWRI AVQQGEVDDL 

        70         80         90        100        110        120 
AFAGYEVADA AGLAQMADKL KQAGIAVTTG DASLARRRGV TGLITFADPF GLPLEIYYGA 

       130        140        150        160        170        180 
SEVFEKPFLP GAAVSGFLTG EQGLGHFVRC VPDSDKALAF YTDVLGFQLS DVIDMKMGPD 

       190        200        210        220        230        240 
VTVPAYFLHC NERHHTLAIA AFPLPKRIHH FMLEVASLDD VGFAFDRVDA DGLITSTLGR 

       250        260        270        280        290 
HTNDHMVSFY ASTPSGVEVE YGWSARTVDR SWVVVRHDSP SMWGHKSVRD KAAARNKA

« Hide

References

« Hide 'large scale' references
[1]"Genetic analysis of a Pseudomonas locus encoding a pathway for biphenyl/polychlorinated biphenyl degradation."
Hofer B., Eltis L.D., Dowling D.N., Timmis K.N.
Gene 130:47-55(1993) [PubMed: 8344527] [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 crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase."
Eltis L.D., Hofmann B., Hecht H.J., Luensdorf H., Timmis K.N.
J. Biol. Chem. 268:2727-2732(1993) [PubMed: 8428946] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-32, SUBSTRATE CHARACTERIZATION, PRELIMINARY CRYSTALLIZATION, SUBUNIT.
[4]"Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad."
Han S., Eltis L.D., Timmis K.N., Muchmore S.W., Bolin J.T.
Science 270:976-980(1995) [PubMed: 7481800] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[5]"Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol."
Vaillancourt F.H., Han S., Fortin P.D., Bolin J.T., Eltis L.D.
J. Biol. Chem. 273:34887-34895(1998) [PubMed: 9857017] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X66122 Genomic DNA. Translation: CAA46910.1.
CP000272 Genomic DNA. Translation: ABE37053.1.
PIRJN0815.
RefSeqYP_556403.1. NC_007953.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HANX-ray1.90A2-298[»]
1KMYX-ray2.00A2-298[»]
1KNDX-ray1.90A2-298[»]
1KNFX-ray1.90A2-298[»]
1LGTX-ray1.70A2-297[»]
1LKDX-ray1.70A2-297[»]
ProteinModelPortalP47228.
SMRP47228. Positions 2-289.
ModBaseSearch...

Protein-protein interaction databases

STRINGP47228.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4010703.
GenomeReviewsGene locus Bxeno_C1125 in contig CP000272_GR.
KEGGbxe:Bxe_C1191.
PATRIC19343367. VBIBurXen52548_8941.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG400175.
OMAIEYGWGG.
ProtClustDBCLSK826661.

Enzyme and pathway databases

BioCycBXEN266265:BXE_C1191-MONOMER.

Family and domain databases

InterProIPR017626. DiOHbiphenyl_dOase.
IPR004360. Glyas_Fos-R_dOase.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
KOK00462.
PfamPF00903. Glyoxalase. 1 hit.
[Graphical view]
TIGRFAMsTIGR03213. 23dbph12diox. 1 hit.
PROSITEPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBPHC_BURXL
AccessionPrimary (citable) accession number: P47228
Secondary accession number(s): Q13FT6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 93 of the entry and version 2 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

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