Haloalkane dehalogenase

NameHaloalkane dehalogenase
Synonyms
  • 1,3,4,6-tetrachloro-1,4-cyclohexadiene hydrolase
  • 1,4-TCDN chlorohydrolase
  • 3.8.1.5
Gene NamelinB
OrganismPseudomonas paucimobilis
Amino acid sequence
>lcl|BSEQ0019084|Haloalkane dehalogenase
MSLGAKPFGEKKFIEIKGRRMAYIDEGTGDPILFQHGNPTSSYLWRNIMPHCAGLGRLIA
CDLIGMGDSDKLDPSGPERYAYAEHRDYLDALWEALDLGDRVVLVVHDWGSALGFDWARR
HRERVQGIAYMEAIAMPIEWADFPEQDRDLFQAFRSQAGEELVLQDNVFVEQVLPGLILR
PLSEAEMAAYREPFLAAGEARRPTLSWPRQIPIAGTPADVVAIARDYAGWLSESPIPKLF
INAEPGALTTGRMRDFCRTWPNQTEITVAGAHFIQEDSPDEIGAAIAAFVRRLRPA
Number of residuesNone
Molecular Weight33107.275
Theoretical pI4.8
GO Classification
Functions
  • haloalkane dehalogenase activity
Processes
  • response to toxic substance
Components
  • periplasmic space
General FunctionHaloalkane dehalogenase activity
Specific FunctionCatalyzes 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).
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP51698
UniProtKB Entry Name
Cellular LocationPeriplasm
Gene sequence
>lcl|BSEQ0002456|891 bp
ATGAGCCTCGGCGCAAAGCCATTTGGCGAGAAGAAATTCATTGAGATCAAGGGCCGGCGC
ATGGCCTATATCGATGAAGGGACCGGCGATCCGATCCTCTTCCAGCACGGCAATCCGACG
TCGTCCTATCTGTGGCGCAATATCATGCCGCATTGCGCCGGGCTGGGACGGCTGATCGCC
TGTGACCTGATCGGCATGGGCGATTCGGACAAGCTCGATCCGTCGGGGCCCGAGCGTTAT
GCCTATGCCGAGCATCGTGACTATCTCGACGCGCTGTGGGAGGCGCTCGATCTCGGGGAC
AGGGTTGTTCTGGTCGTGCATGACTGGGGGTCCGCCCTCGGCTTCGACTGGGCCCGCCGC
CACCGCGAGCGTGTACAGGGGATTGCCTATATGGAAGCGATCGCCATGCCGATCGAATGG
GCGGATTTTCCCGAACAGGATCGCGATCTGTTTCAGGCCTTTCGCTCGCAGGCGGGCGAA
GAATTGGTGTTGCAGGACAATGTTTTTGTCGAACAAGTTCTCCCCGGATTGATCCTGCGC
CCCTTAAGCGAAGCGGAGATGGCCGCCTATCGCGAGCCCTTCCTCGCCGCCGGCGAAGCC
CGTCGACCGACCCTGTCTTGGCCTCGCCAAATCCCGATCGCAGGCACCCCGGCCGACGTG
GTCGCGATCGCCCGGGACTATGCCGGCTGGCTCAGCGAAAGCCCGATTCCGAAACTCTTC
ATCAACGCCGAGCCGGGAGCCCTGACCACGGGCCGAATGCGCGACTTCTGCCGCACATGG
CCAAACCAGACCGAAATCACGGTCGCAGGCGCCCATTTCATCCAGGAGGACAGTCCGGAC
GAGATTGGCGCGGCGATTGCGGCGTTTGTCCGGCGATTGCGCCCAGCATAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. 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. [7691794 ]
  2. 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. [12450824 ]
  3. 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. [10464214 ]
  4. 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. [9293022 ]
  5. 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. [10100638 ]
  6. 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. [12450392 ]
  7. 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. [10329794 ]
  8. 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. [11087355 ]
  9. 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. [11939779 ]

From www.t3db.ca