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P47243 (DBFB_PSEPA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
2,2',3-trihydroxybiphenyl dioxygenase

EC=1.13.11.-
Gene names
Name:dbfB
OrganismPseudomonas paucimobilis (Sphingomonas paucimobilis)
Taxonomic identifier13689 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingomonas

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for meta-cleavage of the first aromatic ring of 2,2',3-trihydroxybiphenyl and 2,3-dihydroxybiphenyl. 2,2',3-trihydroxydiphenyl ether, catechol, 3-methylcatechol, and 4-methylcatechol are oxidized less efficiently and 3,4-dihydroxybiphenyl is oxidized considerably less efficiently.

Cofactor

Fe2+ ion.

Pathway

Xenobiotic degradation; dibenzo-p-dioxin degradation; 2-hydroxymuconate and catechol from dibenzo-p-dioxin: step 2/3.

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

Subunit structure

Monomer.

Sequence similarities

Belongs to the extradiol ring-cleavage dioxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 2942932,2',3-trihydroxybiphenyl dioxygenase
PRO_0000085041

Sites

Metal binding1471Iron By similarity
Metal binding2091Iron By similarity
Metal binding2601Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
P47243 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 9315F5B922E1BF8D

FASTA29432,278
        10         20         30         40         50         60 
MSVKQLGYLI FECRADVLEQ MVVVYQDIIG AVVERDEGGR ALVRLDGRPF RIRLDPGPAN 

        70         80         90        100        110        120 
RLAAIGWNVD PSDLAAIAEQ VEKACYSVVT ADAELAADRA AAQVRQFADN DGFTHELYVE 

       130        140        150        160        170        180 
SSFPTDPVLE SLFVCGEEAN GIFGLGHLVV IVADRAKTQS FFTDVLGFGL SDRVTWPEAD 

       190        200        210        220        230        240 
IFFLHCNQRH HTVALSAPAL GLKPGMVHHL MLEAKSKEQV DRAFAAVKRL GYDVLMTIGQ 

       250        260        270        280        290 
HSNDKVYSFY MMAPAGFAVE LGFGGQVIGD LESWHVGFYD APSIWGHELQ LPAH 

« Hide

References

[1]"Characterization of 2,2',3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium Sphingomonas sp. strain RW1."
Happe B., Eltis L.D., Poth H., Hedderich R., Timmis K.N.
J. Bacteriol. 175:7313-7320(1993) [PubMed: 8226678] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-64.
Strain: RW1.
[2]Armengaud J.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72850 Genomic DNA. Translation: CAA51364.1.

3D structure databases

ProteinModelPortalP47243.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR004360. Glyas_Fos-R_dOase.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
PfamPF00903. Glyoxalase. 1 hit.
[Graphical view]
PROSITEPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDBFB_PSEPA
AccessionPrimary (citable) accession number: P47243
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: September 21, 2011
This is version 54 of the entry and version 4 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

SIMILARITY comments

Index of protein domains and families