ID   DHAA_MYCTO              Reviewed;         300 AA.
AC   P9WMR8; L0TA36; Q50642;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Haloalkane dehalogenase 3;
DE            EC=3.8.1.5;
GN   Name=dhaA; OrderedLocusNames=MT2656;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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. {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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46969.1; -; Genomic_DNA.
DR   PIR; B70725; B70725.
DR   RefSeq; WP_003413363.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMR8; -.
DR   SMR; P9WMR8; -.
DR   EnsemblBacteria; AAK46969; AAK46969; MT2656.
DR   GeneID; 45426581; -.
DR   KEGG; mtc:MT2656; -.
DR   PATRIC; fig|83331.31.peg.2863; -.
DR   HOGENOM; CLU_020336_13_3_11; -.
DR   Proteomes; UP000001020; 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 3"
FT                   /id="PRO_0000427254"
FT   DOMAIN          32..155
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        273
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  33728 MW;  E8F4854749F22562 CRC64;
     MTAFGVEPYG QPKYLEIAGK RMAYIDEGKG DAIVFQHGNP TSSYLWRNIM PHLEGLGRLV
     ACDLIGMGAS DKLSPSGPDR YSYGEQRDFL FALWDALDLG DHVVLVLHDW GSALGFDWAN
     QHRDRVQGIA FMEAIVTPMT WADWPPAVRG VFQGFRSPQG EPMALEHNIF VERVLPGAIL
     RQLSDEEMNH YRRPFVNGGE DRRPTLSWPR NLPIDGEPAE VVALVNEYRS WLEETDMPKL
     FINAEPGAII TGRIRDYVRS WPNQTEITVP GVHFVQEDSP EEIGAAIAQF VRRLRSAAGV