Biphenyl-2,3-diol 1,2-dioxygenase
Details
- Name
- Biphenyl-2,3-diol 1,2-dioxygenase
- Synonyms
- 1.13.11.39
- 2,3-dihydroxybiphenyl dioxygenase
- 23OHBP oxygenase
- DHBD
- Gene Name
- bphC
- Organism
- Pseudomonas sp. (strain KKS102)
- 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
- Functionsbiphenyl-2,3-diol 1,2-dioxygenase activity / ferrous iron bindingProcessesaromatic compound catabolic process / xenobiotic catabolic process
- General Function
- Ferrous iron binding
- Specific Function
- Not Available
- Pfam Domain Function
- Glyoxalase (PF00903)
- 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
Resource Link UniProtKB ID P17297 UniProtKB Entry Name BPHC_PSES1 GenBank Protein ID 151099 GenBank Gene ID M26433 - General References
- 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]
- 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]
- 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]
- 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]
- 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]