ID   DHAA_MYCSX              Reviewed;         307 AA.
AC   Q9ZER0;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Haloalkane dehalogenase;
DE            EC=3.8.1.5;
GN   Name=dhaAF;
OS   Mycobacterium sp. (strain GP1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=106323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10094681; DOI=10.1128/jb.181.7.2050-2058.1999;
RA   Poelarends G.J., van Hylckama Vlieg J.E.T., Marchesi J.R.,
RA   Freitas dos Santos L.M., Janssen D.B.;
RT   "Degradation of 1,2-dibromoethane by Mycobacterium sp. strain GP1.";
RL   J. Bacteriol. 181:2050-2058(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10735862; DOI=10.1128/jb.182.8.2191-2199.2000;
RA   Poelarends G.J., Kulakov L.A., Larkin M.J., van Hylckama Vlieg J.E.T.,
RA   Janssen D.B.;
RT   "Roles of horizontal gene transfer and gene integration in evolution of
RT   1,3-dichloropropene- and 1,2-dibromoethane-degradative pathways.";
RL   J. Bacteriol. 182:2191-2199(2000).
CC   -!- FUNCTION: Catalyzes hydrolytic cleavage of carbon-halogen bonds in
CC       halogenated aliphatic compounds, leading to the formation of the
CC       corresponding primary alcohols, halide ions and protons. Has a broad
CC       substrate specificity, which includes mono- and di-chlorinated and
CC       brominated alkanes. The highest activity was found with 1,2-
CC       dibromoethane, whereas low activity was measured with the analog 1,2-
CC       dichloroethane.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-haloalkane + H2O = a halide anion + a primary alcohol +
CC         H(+); Xref=Rhea:RHEA:19081, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15734, ChEBI:CHEBI:16042, ChEBI:CHEBI:18060; EC=3.8.1.5;
CC   -!- PATHWAY: Xenobiotic degradation; 1,2-dibromoethane degradation.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- INDUCTION: Constitutively expressed.
CC   -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ012627; CAA10076.1; -; Genomic_DNA.
DR   EMBL; AJ250372; CAB65289.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZER0; -.
DR   SMR; Q9ZER0; -.
DR   ESTHER; rhoso-halo1; Haloalkane_dehalogenase-HLD2.
DR   BRENDA; 3.8.1.5; 3490.
DR   UniPathway; UPA00006; -.
DR   GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01231; Haloalk_dehal_type2; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR023594; Haloalkane_dehalogenase_2.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Detoxification; Hydrolase.
FT   CHAIN           1..307
FT                   /note="Haloalkane dehalogenase"
FT                   /id="PRO_0000216773"
FT   DOMAIN          34..158
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   307 AA;  34726 MW;  A70801EF6FF831C0 CRC64;
     MSEIGTGFPF DPHYVEVLGE RMHYVDVGPR DGTPVLFLHG NPTSSYLWRN IIPHVAPSHR
     CIAPDLIGMG KSDKPDLDYF FDDHVRYLDA FIEALGLEEV VLVIHDWGSA LGFHWAKRNP
     ERVKGIACME FIRPIPTWDE WPEFARETFQ AFRTADVGRE LIIDQNAFIE GALPKFVVRP
     LTEVEMDHYR EPFLKPVDRE PLWRFPNELP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW
     GTPGVLISPA EAARLAESLP NCKTVDIGPG LHFLQEDNPD LIGSEIARWL PALIVGKSIE
     FDGGWAT