ID   DHMA2_MYCTU             Reviewed;         286 AA.
AC   P9WMS1; L0TAR1; P64303; Q50600;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Haloalkane dehalogenase 2;
DE            EC=3.8.1.5;
GN   Name=dhmA2; OrderedLocusNames=Rv1833c; ORFNames=MTCY1A11.10;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP44599.1; -; Genomic_DNA.
DR   PIR; B70722; B70722.
DR   RefSeq; NP_216349.1; NC_000962.3.
DR   RefSeq; WP_003409254.1; NZ_NVQJ01000013.1.
DR   AlphaFoldDB; P9WMS1; -.
DR   SMR; P9WMS1; -.
DR   STRING; 83332.Rv1833c; -.
DR   ESTHER; myctu-Rv1833c; Haloalkane_dehalogenase-HLD1.
DR   PaxDb; P9WMS1; -.
DR   DNASU; 885737; -.
DR   GeneID; 45425806; -.
DR   GeneID; 885737; -.
DR   KEGG; mtu:Rv1833c; -.
DR   TubercuList; Rv1833c; -.
DR   eggNOG; COG0596; Bacteria.
DR   OMA; HATVHEF; -.
DR   PhylomeDB; P9WMS1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..286
FT                   /note="Haloalkane dehalogenase 2"
FT                   /id="PRO_0000216769"
FT   DOMAIN          35..134
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        238
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  32151 MW;  A4080E76B3E7B37E CRC64;
     MSIDFTPDPQ LYPFESRWFD SSRGRIHYVD EGTGPPILLC HGNPTWSFLY RDIIVALRDR
     FRCVAPDYLG FGLSERPSGF GYQIDEHARV IGEFVDHLGL DRYLSMGQDW GGPISMAVAV
     ERADRVRGVV LGNTWFWPAD TLAMKAFSRV MSSPPVQYAI LRRNFFVERL IPAGTEHRPS
     SAVMAHYRAV QPNAAARRGV AEMPKQILAA RPLLARLARE VPATLGTKPT LLIWGMKDVA
     FRPKTIIPRL SATFPDHVLV ELPNAKHFIQ EDAPDRIAAA IIERFG