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P17297

- BPHC_PSES1

UniProt

P17297 - BPHC_PSES1

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Protein

Biphenyl-2,3-diol 1,2-dioxygenase

Gene
bphC
Organism
Pseudomonas sp. (strain KKS102)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Fe2+ ion.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi146 – 1461Iron
Metal bindingi210 – 2101Iron
Metal bindingi261 – 2611Iron

GO - Molecular functioni

  1. biphenyl-2,3-diol 1,2-dioxygenase activity Source: UniProtKB-EC
  2. ferrous iron binding Source: InterPro

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-KW
  2. xenobiotic catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00155; UER00252.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:bphC
OrganismiPseudomonas sp. (strain KKS102)
Taxonomic identifieri307 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 293292Biphenyl-2,3-diol 1,2-dioxygenasePRO_0000085035Add
BLAST

Interactioni

Subunit structurei

Homooctamer.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410
Helixi16 – 2510
Beta strandi30 – 356
Beta strandi38 – 4710
Beta strandi49 – 546
Beta strandi59 – 668
Helixi70 – 8314
Beta strandi87 – 893
Helixi92 – 987
Beta strandi101 – 1077
Helixi109 – 1113
Beta strandi113 – 1186
Beta strandi131 – 1333
Helixi140 – 1423
Beta strandi146 – 1505
Helixi154 – 16310
Beta strandi168 – 17811
Beta strandi181 – 19414
Beta strandi196 – 2005
Beta strandi205 – 21713
Helixi218 – 23013
Beta strandi238 – 2447
Beta strandi247 – 2526
Beta strandi259 – 2646
Beta strandi277 – 2793
Beta strandi281 – 2855

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP17297.
SMRiP17297. Positions 2-290.

Miscellaneous databases

EvolutionaryTraceiP17297.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR017626. DiOHbiphenyl_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 2 hits.
TIGRFAMsiTIGR03213. 23dbph12diox. 1 hit.
PROSITEiPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P17297-1 [UniParc]FASTAAdd to Basket

« Hide

MSIERLGYLG FAVKDVPAWD HFLTKSVGLM AAGSAGDAAL YRADQRAWRI    50
AVQPGELDDL AYAGLEVDDA AALERMADKL RQAGVAFTRG DEALMQQRKV 100
MGLLCLQDPF GLPLEIYYGP AEIFHEPFLP SAPVSGFVTG DQGIGHFVRC 150
VPDTAKAMAF YTEVLGFVLS DIIDIQMGPE TSVPAHFLHC NGRHHTIALA 200
AFPIPKRIHH FMLQANTIDD VGYAFDRLDA AGRITSLLGR HTNDQTLSFY 250
ADTPSPMIEV EFGWGPRTVD SSWTVARHSR TAMWGHKSVR GQR 293
Length:293
Mass (Da):32,245
Last modified:January 23, 2007 - v3
Checksum:i53EF1B24502E3B24
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26433 Genomic DNA. Translation: AAA25750.1.
D17319 Genomic DNA. Translation: BAA04141.1.
PIRiA32312. DAPSPC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26433 Genomic DNA. Translation: AAA25750.1 .
D17319 Genomic DNA. Translation: BAA04141.1 .
PIRi A32312. DAPSPC.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DHY X-ray 2.30 A 2-293 [» ]
1EIL X-ray 2.00 A 2-293 [» ]
1EIQ X-ray 2.00 A 2-293 [» ]
1EIR X-ray 2.00 A 2-293 [» ]
1KW3 X-ray 1.45 B 2-293 [» ]
1KW6 X-ray 1.45 B 2-293 [» ]
1KW8 X-ray 2.00 B 2-293 [» ]
1KW9 X-ray 1.95 B 2-293 [» ]
1KWB X-ray 2.00 B 2-293 [» ]
1KWC X-ray 2.10 B 2-293 [» ]
ProteinModelPortali P17297.
SMRi P17297. Positions 2-290.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00155 ; UER00252 .

Miscellaneous databases

EvolutionaryTracei P17297.

Family and domain databases

Gene3Di 3.10.180.10. 2 hits.
InterProi IPR017626. DiOHbiphenyl_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view ]
Pfami PF00903. Glyoxalase. 1 hit.
[Graphical view ]
SUPFAMi SSF54593. SSF54593. 2 hits.
TIGRFAMsi TIGR03213. 23dbph12diox. 1 hit.
PROSITEi PS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiBPHC_PSES1
AccessioniPrimary (citable) accession number: P17297
Secondary accession number(s): Q52441
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 96 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

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

External Data

Dasty 3

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