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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

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 lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeParaburkholderia
Proteomesi
  • UP000001817 Componenti: Chromosome 3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000850682 – 188Biphenyl dioxygenase subunit betaAdd BLAST187

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

1188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 12Combined sources4
Helixi21 – 39Combined sources19
Helixi43 – 47Combined sources5
Beta strandi50 – 59Combined sources10
Helixi66 – 71Combined sources6
Beta strandi80 – 84Combined sources5
Helixi86 – 97Combined sources12
Helixi102 – 104Combined sources3
Beta strandi109 – 121Combined sources13
Beta strandi127 – 140Combined sources14
Turni141 – 143Combined sources3
Beta strandi144 – 158Combined sources15
Beta strandi160 – 175Combined sources16
Beta strandi177 – 182Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5AEUX-ray2.49B/D/F/H1-188[»]
5AEWX-ray1.88B/D/F/H/J/L/N/P/R/T/V/X1-188[»]
ProteinModelPortaliP37334.
SMRiP37334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37334.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4106DX9. Bacteria.
ENOG410YRH3. LUCA.
HOGENOMiHOG000106036.
KOiK15750.
OMAiQRHFISN.
OrthoDBiPOG091H0C0Q.

Family and domain databases

CDDicd00667. ring_hydroxylating_dioxygenase. 1 hit.
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 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
PDB 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[»]
5AEUX-ray2.49B/D/F/H1-188[»]
5AEWX-ray1.88B/D/F/H/J/L/N/P/R/T/V/X1-188[»]
ProteinModelPortaliP37334.
SMRiP37334.
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.
OMAiQRHFISN.
OrthoDBiPOG091H0C0Q.

Enzyme and pathway databases

UniPathwayiUPA00155; UER00250.
BRENDAi1.14.12.18. 7691.

Miscellaneous databases

EvolutionaryTraceiP37334.

Family and domain databases

CDDicd00667. ring_hydroxylating_dioxygenase. 1 hit.
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...

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: November 2, 2016
This is version 102 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.