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P17297 (BPHC_PSES1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismPseudomonas sp. (strain KKS102)
Taxonomic identifier307 [NCBI]
Taxonomic lineageBacteria › Proteobacteria ›

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Fe2+ ion.

Pathway

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

Subunit structure

Homooctamer.

Sequence similarities

Belongs to the extradiol ring-cleavage dioxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 293292Biphenyl-2,3-diol 1,2-dioxygenase
PRO_0000085035

Sites

Metal binding1461Iron
Metal binding2101Iron
Metal binding2611Iron

Secondary structure

1 .................................................... 293
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17297 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 53EF1B24502E3B24

FASTA29332,245
        10         20         30         40         50         60 
MSIERLGYLG FAVKDVPAWD HFLTKSVGLM AAGSAGDAAL YRADQRAWRI AVQPGELDDL 

        70         80         90        100        110        120 
AYAGLEVDDA AALERMADKL RQAGVAFTRG DEALMQQRKV MGLLCLQDPF GLPLEIYYGP 

       130        140        150        160        170        180 
AEIFHEPFLP SAPVSGFVTG DQGIGHFVRC VPDTAKAMAF YTEVLGFVLS DIIDIQMGPE 

       190        200        210        220        230        240 
TSVPAHFLHC NGRHHTIALA AFPIPKRIHH FMLQANTIDD VGYAFDRLDA AGRITSLLGR 

       250        260        270        280        290 
HTNDQTLSFY ADTPSPMIEV EFGWGPRTVD SSWTVARHSR TAMWGHKSVR GQR

« Hide

References

[1]"Cloning and sequencing of two tandem genes involved in degradation of 2,3-dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading soil bacterium Pseudomonas sp. strain KKS102."
Kimbara K., Hashimoto T., Fukuda M., Koana T., Takagi M., Oishi M., Yano K.
J. Bacteriol. 171:2740-2747(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Identification of the bphA and bphB genes of Pseudomonas sp. strains KKS102 involved in degradation of biphenyl and polychlorinated biphenyls."
Fukuda M., Yasukochi Y., Kikuchi Y., Nagata Y., Kimbara K., Horiuchi H., Takagi M., Yano K.
Biochem. Biophys. Res. Commun. 202:850-856(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[3]"Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102."
Senda T., Sugiyama K., Narita H., Yamamoto T., Kimbara K., Fukuda M., Sato M., Yano K., Mitsui Y.
J. Mol. Biol. 255:735-752(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[4]"Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase."
Uragami Y., Senda T., Sugimoto K., Sato N., Nagarajan V., Masai E., Fukuda M., Mitsui Y.
J. Inorg. Biochem. 83:269-279(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]"Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase."
Sato N., Uragami Y., Nishizaki T., Takahashi Y., Sazaki G., Sugimoto K., Nonaka T., Masai E., Fukuda M., Senda T.
J. Mol. Biol. 321:621-636(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF NATIVE ENZYME; SUBSTRATE COMPLEXES AND H145A MUTANT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M26433 Genomic DNA. Translation: AAA25750.1.
D17319 Genomic DNA. Translation: BAA04141.1.
PIRDAPSPC. A32312.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DHYX-ray2.30A2-293[»]
1EILX-ray2.00A2-293[»]
1EIQX-ray2.00A2-293[»]
1EIRX-ray2.00A2-293[»]
1KW3X-ray1.45B2-293[»]
1KW6X-ray1.45B2-293[»]
1KW8X-ray2.00B2-293[»]
1KW9X-ray1.95B2-293[»]
1KWBX-ray2.00B2-293[»]
1KWCX-ray2.10B2-293[»]
ProteinModelPortalP17297.
SMRP17297. Positions 2-290.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00155; UER00252.

Family and domain databases

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

Other

EvolutionaryTraceP17297.

Entry information

Entry nameBPHC_PSES1
AccessionPrimary (citable) accession number: P17297
Secondary accession number(s): Q52441
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 94 of the entry and version 3 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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