ID   DHAA_MYCBO              Reviewed;         300 AA.
AC   Q9XB14; A0A1R3Y210; Q6EUU9; X2BL44;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2003, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Haloalkane dehalogenase {ECO:0000255|HAMAP-Rule:MF_01231};
DE            EC=3.8.1.5 {ECO:0000255|HAMAP-Rule:MF_01231};
GN   Name=dhaA {ECO:0000255|HAMAP-Rule:MF_01231}; Synonyms=dmbA;
GN   OrderedLocusNames=BQ2027_MB2610;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=5033/66, and MU11;
RA   Jesenska A., Strouhal M., Pavlova M., Tesinska I., Monincova M., Bartos M.,
RA   Pavlik I., Rychlik I., Nagata Y., Damborsky J.;
RT   "Mycobacterial haloalkane dehalogenases: cloning, biochemical properties
RT   and distribution.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01231}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01231};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01231}.
CC   -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01231}.
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DR   EMBL; AJ243259; CAB45532.2; -; Genomic_DNA.
DR   EMBL; AJ784272; CAH04659.1; -; Genomic_DNA.
DR   EMBL; LT708304; SIU01228.1; -; Genomic_DNA.
DR   RefSeq; NP_856256.1; NC_002945.3.
DR   RefSeq; WP_010950743.1; NC_002945.4.
DR   AlphaFoldDB; Q9XB14; -.
DR   SMR; Q9XB14; -.
DR   ESTHER; myctu-linb; Haloalkane_dehalogenase-HLD2.
DR   EnsemblBacteria; SIU01228; SIU01228; BQ2027_MB2610.
DR   PATRIC; fig|233413.5.peg.2871; -.
DR   OMA; TLEWPRQ; -.
DR   BRENDA; 3.8.1.5; 3494.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..300
FT                   /note="Haloalkane dehalogenase"
FT                   /id="PRO_0000216781"
FT   DOMAIN          32..155
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT   ACT_SITE        273
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT   CONFLICT        96
FT                   /note="T -> A (in Ref. 1; CAB45532/CAH04659)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   300 AA;  33730 MW;  BCFA71EC43529F7B CRC64;
     MTAFGVEPYG QPKYLEIAGK RMAYIDEGKG DAIVFQHGNP TSSYLWRNIM PHLEGLGRLV
     ACDLIGMGAS DKLSPSGPDR YSYGEQRDFL FALWDTLDLG DHVVLVLHDW GSALGFDWAN
     QHRDRVQGIA FMEAIVTPMT WADWPPAVRG VFQGFRSPQG EPMALEHNIF VERVLPGAIL
     RQLSDEEMNH YRRPFVNGGE DRRPTLSWPR NLPIDGEPAE VVALVNEYRS WLEETDMPKL
     FINAEPGAII TGRIRDYVRS WPNQTEITVP GVHFVQEDSP EEIGAAIAQF VRQLRSAAGV