ID   DHLA_XANFL              Reviewed;         310 AA.
AC   Q6Q3H0;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Haloalkane dehalogenase;
DE            EC=3.8.1.5;
GN   Name=dhlA;
OS   Xanthobacter flavus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=281;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UE-15;
RA   Song J.-S., Kim C.-K.;
RT   "X. flavus UE-15 dhlA gene and insertion element.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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 terminally mono- and
CC       di- chlorinated and brominated alkanes (up to C4 only). The highest
CC       activity was found with 1,2-dichloroethane, 1,3-dichloropropane, and
CC       1,2-dibromoethane (By similarity). {ECO:0000250}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dichloroethane + H2O = 2-chloroethanol + chloride + H(+);
CC         Xref=Rhea:RHEA:25185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:27789, ChEBI:CHEBI:28200; EC=3.8.1.5;
CC   -!- ACTIVITY REGULATION: Inhibited by thiol reagents such as p-
CC       chloromercuribenzoate and iodoacetamide. {ECO:0000250}.
CC   -!- PATHWAY: Xenobiotic degradation; 1,2-dichloroethane degradation;
CC       glycolate from 1,2-dichloroethane: step 1/4.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY561847; AAS83192.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6Q3H0; -.
DR   SMR; Q6Q3H0; -.
DR   ESTHER; xanau-halo1; Haloalkane_dehalogenase-HLD1.
DR   UniPathway; UPA00265; UER00387.
DR   GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019260; P:1,2-dichloroethane catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01230; Haloalk_dehal_type1; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR023489; Haloalkane_dehalogenase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Detoxification; Hydrolase.
FT   CHAIN           1..310
FT                   /note="Haloalkane dehalogenase"
FT                   /id="PRO_0000216772"
FT   DOMAIN          49..295
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        124
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        260
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P22643"
FT   BINDING         175
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P22643"
SQ   SEQUENCE   310 AA;  35144 MW;  FB32C94BE5D8940C CRC64;
     MINAIRTPDQ RFSNLDQYPF SPNYLDDLPG YPGLRAHYLD EGNSDAEDVF LCLHGEPTWS
     YLYRKMIPVF AESGARVIAP DFFGFGKSDK PVDEEDYTFE FHRNFLLALI ERLDLRNITL
     VVQDWGGFLG LTLPMADPSR FKRLIIMNAC LMTDPVTQPA FSAFVTQPAD GFTAWKYDLV
     TPSDLRLDQF MKRWAPTLTE AEASAYAAPF PDTSYQAGVR KFPKMVAQRD QACIDISTEA
     ISFWQNDWNG QTFMAIGMKD KLLGPDVMYP MKALINGCPE PLEIADAGHF VQEFGEQVAR
     EALKHFAETE