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Protein

Biphenyl dioxygenase subunit beta

Gene

bphE

Organism
Burkholderia xenovorans (strain LB400)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi: biphenyl degradation

This protein is involved in step 1 of the subpathway that synthesizes 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Biphenyl dioxygenase subunit alpha (bphA), Biphenyl dioxygenase subunit beta (bphE)
  2. Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (bphB)
  3. Biphenyl-2,3-diol 1,2-dioxygenase (bphC)
  4. 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (bphD)
This subpathway is part of the pathway biphenyl degradation, which is itself part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl, the pathway biphenyl degradation and in Xenobiotic degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciBXEN266265:GJII-8848-MONOMER.
BRENDAi1.14.12.18. 7691.
UniPathwayiUPA00155; UER00250.

Names & Taxonomyi

Protein namesi
Recommended name:
Biphenyl dioxygenase subunit beta (EC:1.14.12.18)
Alternative name(s):
Biphenyl 2,3-dioxygenase
Gene namesi
Name:bphE
Ordered Locus Names:Bxeno_C1130
ORF Names:Bxe_C1196
OrganismiBurkholderia xenovorans (strain LB400)
Taxonomic identifieri266265 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
Proteomesi
  • UP000001817 Componenti: Chromosome 3

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 188187Biphenyl dioxygenase subunit betaPRO_0000085068Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi266265.Bxe_C1196.

Structurei

Secondary structure

1
188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 3919Combined sources
Helixi43 – 475Combined sources
Beta strandi50 – 5910Combined sources
Helixi66 – 716Combined sources
Beta strandi80 – 845Combined sources
Helixi86 – 9611Combined sources
Helixi102 – 1043Combined sources
Beta strandi109 – 12113Combined sources
Beta strandi127 – 14014Combined sources
Turni141 – 1433Combined sources
Beta strandi144 – 15815Combined sources
Beta strandi160 – 17516Combined sources
Beta strandi177 – 1826Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
2YFLX-ray2.60B/D/F/H/J/L1-188[»]
ProteinModelPortaliP37334.
SMRiP37334. Positions 10-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37334.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4106DX9. Bacteria.
ENOG410YRH3. LUCA.
HOGENOMiHOG000106036.
KOiK15750.
OMAiFLVDEAY.
OrthoDBiEOG6M9DWF.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR032710. NTF2-like_dom.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamiPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37334-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNPSPHFFK TFEWPSKAAG LELQNEIEQF YYREAQLLDH RAYEAWFALL
60 70 80 90 100
DKDIHYFMPL RTNRMIREGE LEYSGDQDLA HFDETHETMY GRIRKVTSDV
110 120 130 140 150
GWAENPPSRT RHLVSNVIVK ETATPDTFEV NSAFILYRNR LERQVDIFAG
160 170 180
ERRDVLRRAD NNLGFSIAKR TILLDASTLL SNNLSMFF
Length:188
Mass (Da):22,085
Last modified:January 23, 2007 - v3
Checksum:i36DBE14E22FEA67B
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86348 Genomic DNA. Translation: AAB63426.1.
CP000272 Genomic DNA. Translation: ABE37058.1. Different initiation.
RefSeqiWP_040123616.1. NZ_CP008761.1.

Genome annotation databases

EnsemblBacteriaiABE37058; ABE37058; Bxe_C1196.
GeneIDi4010708.
KEGGibxb:DR64_8609.
bxe:Bxe_C1196.
PATRICi19343377. VBIBurXen52548_8946.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86348 Genomic DNA. Translation: AAB63426.1.
CP000272 Genomic DNA. Translation: ABE37058.1. Different initiation.
RefSeqiWP_040123616.1. NZ_CP008761.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
2YFLX-ray2.60B/D/F/H/J/L1-188[»]
ProteinModelPortaliP37334.
SMRiP37334. Positions 10-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266265.Bxe_C1196.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE37058; ABE37058; Bxe_C1196.
GeneIDi4010708.
KEGGibxb:DR64_8609.
bxe:Bxe_C1196.
PATRICi19343377. VBIBurXen52548_8946.

Phylogenomic databases

eggNOGiENOG4106DX9. Bacteria.
ENOG410YRH3. LUCA.
HOGENOMiHOG000106036.
KOiK15750.
OMAiFLVDEAY.
OrthoDBiEOG6M9DWF.

Enzyme and pathway databases

UniPathwayiUPA00155; UER00250.
BioCyciBXEN266265:GJII-8848-MONOMER.
BRENDAi1.14.12.18. 7691.

Miscellaneous databases

EvolutionaryTraceiP37334.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR032710. NTF2-like_dom.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamiPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12, CHARACTERIZATION.
  4. Erratum
    Haddock J.D., Gibson D.T.
    J. Bacteriol. 178:258-258(1996)

Entry informationi

Entry nameiBPHE_BURXL
AccessioniPrimary (citable) accession number: P37334
Secondary accession number(s): Q13FT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.