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
Functions
haloalkane dehalogenase activity
Processes
response to toxic substance
Components
periplasmic 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
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
ResourceLink
UniProtKB IDP51698
UniProtKB Entry NameLINB_SPHPI
GenBank Protein ID4521186
GenBank Gene IDD14594
General 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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed:11939779]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB017011,2-Dichloro-PropaneexperimentalunknownDetails
DB01839Propylene glycolapproved, investigationalunknownDetails
DB02145Butyl alcoholexperimentalunknownDetails
DB02302N3, N4-DimethylarginineexperimentalunknownDetails
DB027741,3-PropandiolexperimentalunknownDetails
DB033351-Bromopropane-2-OlexperimentalunknownDetails
DB03733Ethylene DichlorideexperimentalunknownDetails
DB043202-Bromo-2-Propene-1-OlexperimentalunknownDetails