Haloalkane dehalogenase
Details
- Name
- Haloalkane dehalogenase
- Synonyms
- 1,3,4,6-tetrachloro-1,4-cyclohexadiene hydrolase
- 1,4-TCDN chlorohydrolase
- 3.8.1.5
- Gene Name
- linB
- Organism
- Sphingomonas paucimobilis
- Amino acid sequence
>lcl|BSEQ0019084|Haloalkane dehalogenase MSLGAKPFGEKKFIEIKGRRMAYIDEGTGDPILFQHGNPTSSYLWRNIMPHCAGLGRLIA CDLIGMGDSDKLDPSGPERYAYAEHRDYLDALWEALDLGDRVVLVVHDWGSALGFDWARR HRERVQGIAYMEAIAMPIEWADFPEQDRDLFQAFRSQAGEELVLQDNVFVEQVLPGLILR PLSEAEMAAYREPFLAAGEARRPTLSWPRQIPIAGTPADVVAIARDYAGWLSESPIPKLF INAEPGALTTGRMRDFCRTWPNQTEITVAGAHFIQEDSPDEIGAAIAAFVRRLRPA
- Number of residues
- 296
- Molecular Weight
- 33107.275
- Theoretical pI
- 4.8
- GO Classification
- Functionshaloalkane dehalogenase activityProcessesresponse to toxic substanceComponentsperiplasmic space
- General Function
- Haloalkane dehalogenase activity
- Specific Function
- Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic alcohols were good substrates. Shows almost no activity with 1,2-dichloroethane, but very high activity with the brominated analog. Is involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane (lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL).
- Pfam Domain Function
- Abhydrolase_1 (PF00561)
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0002456|891 bp ATGAGCCTCGGCGCAAAGCCATTTGGCGAGAAGAAATTCATTGAGATCAAGGGCCGGCGC ATGGCCTATATCGATGAAGGGACCGGCGATCCGATCCTCTTCCAGCACGGCAATCCGACG TCGTCCTATCTGTGGCGCAATATCATGCCGCATTGCGCCGGGCTGGGACGGCTGATCGCC TGTGACCTGATCGGCATGGGCGATTCGGACAAGCTCGATCCGTCGGGGCCCGAGCGTTAT GCCTATGCCGAGCATCGTGACTATCTCGACGCGCTGTGGGAGGCGCTCGATCTCGGGGAC AGGGTTGTTCTGGTCGTGCATGACTGGGGGTCCGCCCTCGGCTTCGACTGGGCCCGCCGC CACCGCGAGCGTGTACAGGGGATTGCCTATATGGAAGCGATCGCCATGCCGATCGAATGG GCGGATTTTCCCGAACAGGATCGCGATCTGTTTCAGGCCTTTCGCTCGCAGGCGGGCGAA GAATTGGTGTTGCAGGACAATGTTTTTGTCGAACAAGTTCTCCCCGGATTGATCCTGCGC CCCTTAAGCGAAGCGGAGATGGCCGCCTATCGCGAGCCCTTCCTCGCCGCCGGCGAAGCC CGTCGACCGACCCTGTCTTGGCCTCGCCAAATCCCGATCGCAGGCACCCCGGCCGACGTG GTCGCGATCGCCCGGGACTATGCCGGCTGGCTCAGCGAAAGCCCGATTCCGAAACTCTTC ATCAACGCCGAGCCGGGAGCCCTGACCACGGGCCGAATGCGCGACTTCTGCCGCACATGG CCAAACCAGACCGAAATCACGGTCGCAGGCGCCCATTTCATCCAGGAGGACAGTCCGGAC GAGATTGGCGCGGCGATTGCGGCGTTTGTCCGGCGATTGCGCCCAGCATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P51698 UniProtKB Entry Name LINB_SPHPI GenBank Protein ID 4521186 GenBank Gene ID D14594 - General References
- Nagata Y, Nariya T, Ohtomo R, Fukuda M, Yano K, Takagi M: Cloning and sequencing of a dehalogenase gene encoding an enzyme with hydrolase activity involved in the degradation of gamma-hexachlorocyclohexane in Pseudomonas paucimobilis. J Bacteriol. 1993 Oct;175(20):6403-10. [Article]
- Kumari R, Subudhi S, Suar M, Dhingra G, Raina V, Dogra C, Lal S, van der Meer JR, Holliger C, Lal R: Cloning and characterization of lin genes responsible for the degradation of Hexachlorocyclohexane isomers by Sphingomonas paucimobilis strain B90. Appl Environ Microbiol. 2002 Dec;68(12):6021-8. [Article]
- Nagata Y, Futamura A, Miyauchi K, Takagi M: Two different types of dehalogenases, LinA and LinB, involved in gamma-hexachlorocyclohexane degradation in Sphingomonas paucimobilis UT26 are localized in the periplasmic space without molecular processing. J Bacteriol. 1999 Sep;181(17):5409-13. [Article]
- Nagata Y, Miyauchi K, Damborsky J, Manova K, Ansorgova A, Takagi M: Purification and characterization of a haloalkane dehalogenase of a new substrate class from a gamma-hexachlorocyclohexane-degrading bacterium, Sphingomonas paucimobilis UT26. Appl Environ Microbiol. 1997 Sep;63(9):3707-10. [Article]
- Hynkova K, Nagata Y, Takagi M, Damborsky J: Identification of the catalytic triad in the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. FEBS Lett. 1999 Mar 5;446(1):177-81. [Article]
- Bohac M, Nagata Y, Prokop Z, Prokop M, Monincova M, Tsuda M, Koca J, Damborsky J: Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis. Biochemistry. 2002 Dec 3;41(48):14272-80. [Article]
- Smatanova I, Nagata Y, Svensson LA, Takagi M, Marek J: Crystallization and preliminary X-ray diffraction analysis of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26. Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1231-3. [Article]
- Marek J, Vevodova J, Smatanova IK, Nagata Y, Svensson LA, Newman J, Takagi M, Damborsky J: Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. Biochemistry. 2000 Nov 21;39(46):14082-6. [Article]
- Oakley AJ, Prokop Z, Bohac M, Kmunicek J, Jedlicka T, Monincova M, Kuta-Smatanova I, Nagata Y, Damborsky J, Wilce MC: Exploring the structure and activity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26: evidence for product- and water-mediated inhibition. Biochemistry. 2002 Apr 16;41(15):4847-55. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01701 1,2-Dichloro-Propane experimental unknown Details DB02145 Butyl alcohol experimental unknown Details DB02302 Symmetric dimethylarginine experimental unknown Details DB02774 1,3-Propanediol experimental unknown Details DB03335 (+)-1-bromo-2-propanol experimental unknown Details DB03733 Ethylene Dichloride experimental unknown Details DB04320 2-Bromo-2-Propene-1-Ol experimental unknown Details