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P47227 (BPHB_BURXL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 104. 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:
Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase

EC=1.3.1.56
Alternative name(s):
2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase
2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase
Biphenyl-2,3-dihydro-2,3-diol dehydrogenase
Biphenyl-cis-diol dehydrogenase
Gene names
Name:bphB
Ordered Locus Names:Bxeno_C1126
ORF Names:Bxe_C1192
OrganismBurkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]
Taxonomic identifier266265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ = biphenyl-2,3-diol + NADH.

Pathway

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

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
PRO_0000054531

Regions

Nucleotide binding9 – 3628NAD

Sites

Active site1551Proton acceptor
Binding site591NAD
Binding site1421Substrate By similarity
Binding site1591NAD

Secondary structure

.................................................. 277
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P47227 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 00194120BD4E12D1

FASTA27728,901
        10         20         30         40         50         60 
MKLKGEAVLI TGGASGLGRA LVDRFVAEGA KVAVLDKSAE RLAELETDHG DNVLGIVGDV 

        70         80         90        100        110        120 
RSLEDQKQAA SRCVARFGKI DTLIPNAGIW DYSTALVDLP EESLDAAFDE VFHINVKGYI 

       130        140        150        160        170        180 
HAVKACLPAL VASRGNVIFT ISNAGFYPNG GGPLYTAAKH AIVGLVRELA FELAPYVRVN 

       190        200        210        220        230        240 
GVGSGGINSD LRGPSSLGMG SKAISTVPLA DMLKSVLPIG RMPEVEEYTG AYVFFATRGD 

       250        260        270 
AAPATGALLN YDGGLGVRGF FSGAGGNDLL EQLNIHP 

« 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LB400.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[4]"Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from a PCB degrader at 2.0-A resolution."
Huelsmeyer M., Hecht H.-J., Niefind K., Hofer B., Eltis L.D., Timmis K.N., Schomburg D.
Protein Sci. 7:1286-1293(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66122 Genomic DNA. Translation: CAA46909.1.
CP000272 Genomic DNA. Translation: ABE37054.1.
M86348 Genomic DNA. Translation: AAB63430.2.
PIRJN0814.
RefSeqYP_556404.1. NC_007953.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BDBX-ray2.00A1-277[»]
ProteinModelPortalP47227.
SMRP47227. Positions 1-276.
ModBaseSearch...

Protein-protein interaction databases

STRING266265.Bxe_C1192.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE37054; ABE37054; Bxe_C1192.
GeneID4010704.
KEGGbxe:Bxe_C1192.
PATRIC19343369. VBIBurXen52548_8942.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1028.
KOK08690.
OMAPNAGIWD.
ProtClustDBPRK06200.

Enzyme and pathway databases

BioCycBXEN266265:GJII-8844-MONOMER.
UniPathwayUPA00155; UER00251.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR017711. BphB_TodD.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsTIGR03325. BphB_TodD. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP47227.

Entry information

Entry nameBPHB_BURXL
AccessionPrimary (citable) accession number: P47227
Secondary accession number(s): Q13FT5, Q52435
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 29, 2013
This is version 104 of the entry and version 1 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