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

Details

Name
Biphenyl-2,3-diol 1,2-dioxygenase
Kind
protein
Synonyms
  • 1.13.11.39
  • 2,3-dihydroxybiphenyl dioxygenase
  • 23OHBP oxygenase
  • DHBD
Gene Name
bphC
UniProtKB Entry
P17297Swiss-Prot
Organism
Pseudomonas sp. (strain KKS102)
NCBI Taxonomy ID
307
Amino acid sequence
>lcl|BSEQ0011192|Biphenyl-2,3-diol 1,2-dioxygenase
MSIERLGYLGFAVKDVPAWDHFLTKSVGLMAAGSAGDAALYRADQRAWRIAVQPGELDDL
AYAGLEVDDAAALERMADKLRQAGVAFTRGDEALMQQRKVMGLLCLQDPFGLPLEIYYGP
AEIFHEPFLPSAPVSGFVTGDQGIGHFVRCVPDTAKAMAFYTEVLGFVLSDIIDIQMGPE
TSVPAHFLHCNGRHHTIALAAFPIPKRIHHFMLQANTIDDVGYAFDRLDAAGRITSLLGR
HTNDQTLSFYADTPSPMIEVEFGWGPRTVDSSWTVARHSRTAMWGHKSVRGQR
Number of residues
293
Molecular Weight
32244.46
Theoretical pI
6.23
GO Classification
Functions
biphenyl-2,3-diol 1,2-dioxygenase activity / ferrous iron binding
Processes
aromatic compound catabolic process / xenobiotic catabolic process
General Function
Not Available
Specific Function
biphenyl-2,3-diol 1,2-dioxygenase activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0003316|882 bp
ATGAGTATCGAACGTTTGGGCTACCTCGGCTTCGCCGTCAAGGATGTACCCGCCTGGGAC
CACTTTCTGACCAAGAGCGTGGGTTTGATGGCTGCGGGTTCGGCTGGCGACGCTGCGCTG
TACCGGGCCGATCAGCGTGCCTGGCGCATCGCCGTGCAGCCGGGCGAACTCGACGACCTG
GCCTACGCAGGCTTGGAAGTGGATGACGCCGCCGCGCTCGAGCGCATGGCCGACAAGCTG
CGCCAGGCAGGGGTGGCCTTCACCCGCGGTGACGAAGCGCTCATGCAGCAGCGCAAGGTC
ATGGGCCTGCTGTGTCTGCAAGATCCGTTCGGCCTGCCGCTCGAGATTTACTACGGCCCG
GCAGAAATCTTTCATGAGCCCTTCCTGCCTAGCGCCCCCGTGTCGGGCTTCGTCACGGGC
GACCAGGGCATCGGGCACTTCGTGCGCTGCGTGCCCGACACGGCGAAGGCGATGGCTTTC
TACACCGAGGTGCTTGGCTTTGTGCTGTCGGACATCATTGACATCCAGATGGGGCCGGAA
ACGAGCGTGCCCGCGCACTTTCTGCACTGCAATGGCCGTCACCACACGATCGCCCTGGCT
GCTTTCCCGATCCCGAAGCGCATCCACCACTTCATGCTGCAAGCCAACACCATCGACGAT
GTGGGCTACGCCTTCGATCGGCTGGACGCCGCCGGGCGCATCACCTCCCTGCTCGGGCGC
CACACCAACGACCAGACGCTCTCCTTCTATGCCGACACGCCGTCGCCCATGATCGAGGTC
GAGTTCGGCTGGGGGCCGCGCACAGTGGATTCCTCCTGGACGGTGGCGCGACACAGCCGC
ACGGCCATGTGGGGTCACAAGTCGGTACGCGGCCAGCGCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP17297
UniProtKB Entry NameBPHC_PSES1
GenBank Protein ID151099
GenBank Gene IDM26433
PDB ID(s)1DHY, 1EIL, 1EIQ, 1EIR, 1KW3, 1KW6, 1KW8, 1KW9, 1KWB, 1KWC
General References
  1. Kimbara K, Hashimoto T, Fukuda M, Koana T, Takagi M, Oishi M, Yano K: 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. J Bacteriol. 1989 May;171(5):2740-7. [Article]
  2. Fukuda M, Yasukochi Y, Kikuchi Y, Nagata Y, Kimbara K, Horiuchi H, Takagi M, Yano K: Identification of the bphA and bphB genes of Pseudomonas sp. strains KKS102 involved in degradation of biphenyl and polychlorinated biphenyls. Biochem Biophys Res Commun. 1994 Jul 29;202(2):850-6. [Article]
  3. Senda T, Sugiyama K, Narita H, Yamamoto T, Kimbara K, Fukuda M, Sato M, Yano K, Mitsui Y: 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. J Mol Biol. 1996 Feb 9;255(5):735-52. [Article]
  4. Uragami Y, Senda T, Sugimoto K, Sato N, Nagarajan V, Masai E, Fukuda M, Mitsu Y: Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase. J Inorg Biochem. 2001 Feb;83(4):269-79. [Article]
  5. Sato N, Uragami Y, Nishizaki T, Takahashi Y, Sazaki G, Sugimoto K, Nonaka T, Masai E, Fukuda M, Senda T: Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase. J Mol Biol. 2002 Aug 23;321(4):621-36. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Biphenyl-2,3-DiolexperimentalunknowntargetDetails