ID   DHAA_MYCBT              Reviewed;         300 AA.
AC   C1AF48;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 54.
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}; OrderedLocusNames=JTY_2596;
OS   Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=561275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX   PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA   Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT   "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT   Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL   Vaccine 27:1710-1716(2009).
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; AP010918; BAH26877.1; -; Genomic_DNA.
DR   RefSeq; WP_011799277.1; NZ_CP014566.1.
DR   AlphaFoldDB; C1AF48; -.
DR   SMR; C1AF48; -.
DR   ESTHER; myctu-linb; Haloalkane_dehalogenase-HLD2.
DR   KEGG; mbt:JTY_2596; -.
DR   HOGENOM; CLU_020336_13_3_11; -.
DR   OMA; TLEWPRQ; -.
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_1000164972"
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"
SQ   SEQUENCE   300 AA;  33700 MW;  47F4854749F22560 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 VRQLRSAAGV