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Protein

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

Gene

bphC

Organism
Pseudomonas sp. (strain KKS102)
Status
Reviewed-Annotation score: 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

Pathwayi: biphenyl degradation

This protein is involved in step 3 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 (bphA1), Biphenyl dioxygenase subunit beta (bphA2)
  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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi146Iron1
Metal bindingi210Iron1
Metal bindingi261Iron1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000850352 – 293Biphenyl-2,3-diol 1,2-dioxygenaseAdd BLAST292

Interactioni

Subunit structurei

Homooctamer.

Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Helixi16 – 25Combined sources10
Beta strandi30 – 35Combined sources6
Beta strandi38 – 47Combined sources10
Beta strandi49 – 54Combined sources6
Beta strandi59 – 66Combined sources8
Helixi70 – 83Combined sources14
Beta strandi87 – 89Combined sources3
Helixi92 – 98Combined sources7
Beta strandi101 – 107Combined sources7
Helixi109 – 111Combined sources3
Beta strandi113 – 118Combined sources6
Beta strandi131 – 133Combined sources3
Helixi140 – 142Combined sources3
Beta strandi146 – 150Combined sources5
Helixi154 – 163Combined sources10
Beta strandi168 – 178Combined sources11
Beta strandi181 – 194Combined sources14
Beta strandi196 – 200Combined sources5
Beta strandi205 – 217Combined sources13
Helixi218 – 230Combined sources13
Beta strandi238 – 244Combined sources7
Beta strandi247 – 252Combined sources6
Beta strandi259 – 264Combined sources6
Beta strandi277 – 279Combined sources3
Beta strandi281 – 285Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MSIERLGYLG FAVKDVPAWD HFLTKSVGLM AAGSAGDAAL YRADQRAWRI
60 70 80 90 100
AVQPGELDDL AYAGLEVDDA AALERMADKL RQAGVAFTRG DEALMQQRKV
110 120 130 140 150
MGLLCLQDPF GLPLEIYYGP AEIFHEPFLP SAPVSGFVTG DQGIGHFVRC
160 170 180 190 200
VPDTAKAMAF YTEVLGFVLS DIIDIQMGPE TSVPAHFLHC NGRHHTIALA
210 220 230 240 250
AFPIPKRIHH FMLQANTIDD VGYAFDRLDA AGRITSLLGR HTNDQTLSFY
260 270 280 290
ADTPSPMIEV EFGWGPRTVD SSWTVARHSR TAMWGHKSVR GQR
Length:293
Mass (Da):32,245
Last modified:January 23, 2007 - v3
Checksum:i53EF1B24502E3B24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26433 Genomic DNA. Translation: AAA25750.1.
D17319 Genomic DNA. Translation: BAA04141.1.
PIRiA32312. DAPSPC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26433 Genomic DNA. Translation: AAA25750.1.
D17319 Genomic DNA. Translation: BAA04141.1.
PIRiA32312. DAPSPC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00155; UER00252.

Miscellaneous databases

EvolutionaryTraceiP17297.

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]
ProtoNetiSearch...

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: 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

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.