DHMA2_MYCTO
ID DHMA2_MYCTO Reviewed; 286 AA.
AC P9WMS0; 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 37.
DE RecName: Full=Haloalkane dehalogenase 2;
DE EC=3.8.1.5;
GN Name=dhmA2; OrderedLocusNames=MT1881;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(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. {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; AE000516; AAK46153.1; -; Genomic_DNA.
DR PIR; B70722; B70722.
DR RefSeq; WP_003409254.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMS0; -.
DR SMR; P9WMS0; -.
DR EnsemblBacteria; AAK46153; AAK46153; MT1881.
DR GeneID; 45425806; -.
DR KEGG; mtc:MT1881; -.
DR PATRIC; fig|83331.31.peg.2025; -.
DR HOGENOM; CLU_020336_13_3_11; -.
DR Proteomes; UP000001020; 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.
FT CHAIN 1..286
FT /note="Haloalkane dehalogenase 2"
FT /id="PRO_0000427253"
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