ID   DHAA_MYCS2              Reviewed;         311 AA.
AC   Q938B4; A0R7A4; I7GBR8;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 101.
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};
GN   OrderedLocusNames=MSMEG_6837, MSMEI_6656;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-280.
RA   Derbyshire K.M., Parsons L.M., DeVost J.;
RL   Submitted (AUG-2001) 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.
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; CP000480; ABK74278.1; -; Genomic_DNA.
DR   EMBL; AY054120; AAL17946.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP43082.1; -; Genomic_DNA.
DR   RefSeq; WP_011731575.1; NZ_SIJM01000001.1.
DR   RefSeq; YP_891042.1; NC_008596.1.
DR   AlphaFoldDB; Q938B4; -.
DR   SMR; Q938B4; -.
DR   STRING; 246196.MSMEI_6656; -.
DR   ESTHER; mycsm-Q938B4; Haloalkane_dehalogenase-HLD2.
DR   EnsemblBacteria; ABK74278; ABK74278; MSMEG_6837.
DR   EnsemblBacteria; AFP43082; AFP43082; MSMEI_6656.
DR   GeneID; 66738094; -.
DR   KEGG; msg:MSMEI_6656; -.
DR   KEGG; msm:MSMEG_6837; -.
DR   PATRIC; fig|246196.19.peg.6660; -.
DR   eggNOG; COG0596; Bacteria.
DR   OMA; TLEWPRQ; -.
DR   OrthoDB; 1890883at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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; IPR023594; Haloalkane_dehalogenase_2.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..311
FT                   /note="Haloalkane dehalogenase"
FT                   /id="PRO_0000216782"
FT   DOMAIN          30..148
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
SQ   SEQUENCE   311 AA;  34979 MW;  F52A9A4135B9C006 CRC64;
     MPGSEPYGRL QYREINGKRM AYIDEARGDA IVFQHGNPSS SYLWRNVLPH TEGLGRLVAC
     DLIGMGASDK LDGSGPDSYH YHENRDYLFA LWDALDLGDR VTLVLHDWGG ALGFDWANRH
     RDRVAGIVHM ETVSVPMEWD DFPDEVAQMF RGLRSPQGEE MVLENNAFIE GVLPSIVMRT
     LSEEEMIHYR RPFLNAGEDR RPTLSWPRDV PLAGEPAEVV AVIEDFGEWL ATSDIPKLFI
     RADPGVIQGK QRILDIVRSW PNQTEITVPG THFLQEDSAD QIGEAIASFV REIRAGDNLH
     REAAPEMNSA S