ID   DHMA_MYCAV              Reviewed;         301 AA.
AC   Q93K00;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Haloalkane dehalogenase;
DE            EC=3.8.1.5;
GN   Name=dhmA;
OS   Mycobacterium avium.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N85;
RX   PubMed=12147465; DOI=10.1128/aem.68.8.3724-3730.2002;
RA   Jesenska A., Bartos M., Czernekova V., Rychlik I., Pavlik I., Damborsky J.;
RT   "Cloning and expression of the haloalkane dehalogenase gene dhmA from
RT   Mycobacterium avium N85 and preliminary characterization of DhmA.";
RL   Appl. Environ. Microbiol. 68:3724-3730(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. Has a broad
CC       substrate specificity, which includes mono- and di-chlorinated and
CC       brominated linear alkanes (up to at least C4). Shows good activity with
CC       the priority pollutant 1,2-dichloroethane.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.;
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.;
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; AJ314789; CAC41377.1; -; Genomic_DNA.
DR   RefSeq; WP_003872427.1; NZ_NSFF01000028.1.
DR   AlphaFoldDB; Q93K00; -.
DR   SMR; Q93K00; -.
DR   ESTHER; mycav-DHMA; Haloalkane_dehalogenase-HLD1.
DR   GeneID; 66693599; -.
DR   BRENDA; 3.8.1.5; 3492.
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.
FT   CHAIN           1..301
FT                   /note="Haloalkane dehalogenase"
FT                   /id="PRO_0000216766"
FT   DOMAIN          47..284
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   301 AA;  33842 MW;  AE2731C504BAAAE6 CRC64;
     MHVLRTPDSR FENLEDYPFV AHYLDVTARD TRPLRMHYLD EGPIDGPPIV LLHGEPTWSY
     LYRTMITPLT DAGNRVLAPD LIGFGRSDKP SRIEDYSYQR HVDWVVSWFE HLNLSDVTLF
     VQDWGSLIGL RIAAEQPDRV GRLVVANGFL PTAQRRTPPA FYAWRAFARY SPVLPAGRIV
     SVGTVRRVSS KVRAGYDAPF PDKTYQAGAR AFPQLVPTSP ADPAIPANRK AWEALGRWEK
     PFLAIFGARD PILGHADSPL IKHIPGAAGQ PHARINASHF IQEDRGPELA ERILSWQQAL
     L