DHMA_MYCPA
ID DHMA_MYCPA Reviewed; 301 AA.
AC Q73Y99;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=MAP_2057;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS04374.1; -; Genomic_DNA.
DR RefSeq; WP_003872427.1; NC_002944.2.
DR AlphaFoldDB; Q73Y99; -.
DR SMR; Q73Y99; -.
DR STRING; 262316.MAP_2057; -.
DR ESTHER; mycav-DHMA; Haloalkane_dehalogenase-HLD1.
DR EnsemblBacteria; AAS04374; AAS04374; MAP_2057.
DR GeneID; 66693599; -.
DR KEGG; mpa:MAP_2057; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_13_3_11; -.
DR OMA; IQEDSGP; -.
DR BRENDA; 3.8.1.5; 3492.
DR Proteomes; UP000000580; 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..301
FT /note="Haloalkane dehalogenase"
FT /id="PRO_1000066841"
FT DOMAIN 47..284
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 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