ID   DHMA1_MYCTO             Reviewed;         300 AA.
AC   P9WMS2; L0TAS4; P64301; Q50670;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Haloalkane dehalogenase 1;
DE            EC=3.8.1.5;
GN   Name=dhmA1; OrderedLocusNames=MT2353;
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 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46638.1; -; Genomic_DNA.
DR   PIR; D70733; D70733.
DR   RefSeq; WP_003411849.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMS2; -.
DR   SMR; P9WMS2; -.
DR   ESTHER; myctu-RV2296; Haloalkane_dehalogenase-HLD1.
DR   EnsemblBacteria; AAK46638; AAK46638; MT2353.
DR   GeneID; 45426276; -.
DR   KEGG; mtc:MT2353; -.
DR   PATRIC; fig|83331.31.peg.2533; -.
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_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   Hydrolase.
FT   CHAIN           1..300
FT                   /note="Haloalkane dehalogenase 1"
FT                   /id="PRO_0000427252"
FT   DOMAIN          47..176
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        123
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        250
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        279
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  33358 MW;  FFD750AB0E4B0A56 CRC64;
     MDVLRTPDSR FEHLVGYPFA PHYVDVTAGD TQPLRMHYVD EGPGDGPPIV LLHGEPTWSY
     LYRTMIPPLS AAGHRVLAPD LIGFGRSDKP TRIEDYTYLR HVEWVTSWFE NLDLHDVTLF
     VQDWGSLIGL RIAAEHGDRI ARLVVANGFL PAAQGRTPLP FYVWRAFARY SPVLPAGRLV
     NFGTVHRVPA GVRAGYDAPF PDKTYQAGAR AFPRLVPTSP DDPAVPANRA AWEALGRWDK
     PFLAIFGYRD PILGQADGPL IKHIPGAAGQ PHARIKASHF IQEDSGTELA ERMLSWQQAT