DHMA_MYCMM
ID DHMA_MYCMM Reviewed; 297 AA.
AC B2HJU9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Haloalkane dehalogenase {ECO:0000255|HAMAP-Rule:MF_01230};
DE EC=3.8.1.5 {ECO:0000255|HAMAP-Rule:MF_01230};
GN Name=dhmA {ECO:0000255|HAMAP-Rule:MF_01230}; OrderedLocusNames=MMAR_3472;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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_01230}.
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_01230};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01230}.
CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01230}.
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DR EMBL; CP000854; ACC41891.1; -; Genomic_DNA.
DR RefSeq; WP_012395104.1; NC_010612.1.
DR AlphaFoldDB; B2HJU9; -.
DR SMR; B2HJU9; -.
DR STRING; 216594.MMAR_3472; -.
DR ESTHER; mycmm-dhma; Haloalkane_dehalogenase-HLD1.
DR EnsemblBacteria; ACC41891; ACC41891; MMAR_3472.
DR GeneID; 64262139; -.
DR KEGG; mmi:MMAR_3472; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_13_3_11; -.
DR OMA; IQEDSGP; -.
DR OrthoDB; 1890883at2; -.
DR Proteomes; UP000001190; 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; Reference proteome.
FT CHAIN 1..297
FT /note="Haloalkane dehalogenase"
FT /id="PRO_1000139631"
FT DOMAIN 47..148
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01230"
FT ACT_SITE 250
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01230"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01230"
SQ SEQUENCE 297 AA; 32818 MW; 89F44710E5DB7C6E CRC64;
MDVVRTPDAR FQNLVGYPFA AHYVDVAATD TPHLRMHYID EGPADGPPIV LLHGEPTWSY
LYRTMIPPLA AGGYRVLAPD LIGFGRSDKP TRIADYTYLR HVEWVKSWFE ELRLAEATLF
VQDWGSLIGL RVAAEHGDAI ARLVVANGFL PTARGRTPTA FHIWRAFARY SPVLPAGRLV
AAGTVRKVPP AVRAGYDAPF PDKSYQAGAR AFPQLVPISP DDPAVAANRA AWDALGRWEK
PFLAIFGERD PLLGRADRPL IKHIPGAAGQ PHARINANHF IQEDSGPELA ERIISWQ
