ID A0A2R7L6H5_9CAUL Unreviewed; 301 AA.
AC A0A2R7L6H5;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Haloalkane dehalogenase {ECO:0000256|ARBA:ARBA00012065, ECO:0000256|HAMAP-Rule:MF_01230};
DE EC=3.8.1.5 {ECO:0000256|ARBA:ARBA00012065, ECO:0000256|HAMAP-Rule:MF_01230};
GN Name=dhmA {ECO:0000256|HAMAP-Rule:MF_01230};
GN ORFNames=DBR10_16665 {ECO:0000313|EMBL:PTT05194.1};
OS Caulobacter sp. HMWF025.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=2056860 {ECO:0000313|EMBL:PTT05194.1, ECO:0000313|Proteomes:UP000244835};
RN [1] {ECO:0000313|Proteomes:UP000244835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMWF025 {ECO:0000313|Proteomes:UP000244835};
RA Muscarella M.E.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001644, ECO:0000256|HAMAP-
CC Rule:MF_01230};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_01230}.
CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00008794, ECO:0000256|HAMAP-
CC Rule:MF_01230}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTT05194.1}.
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DR EMBL; QAII01000155; PTT05194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R7L6H5; -.
DR OrthoDB; 9804723at2; -.
DR Proteomes; UP000244835; Unassembled WGS sequence.
DR GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 PANTHER; PTHR42977:SF3; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42977; HYDROLASE-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01230, ECO:0000313|EMBL:PTT05194.1}.
FT DOMAIN 47..166
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01230"
FT ACT_SITE 249
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01230"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01230"
SQ SEQUENCE 301 AA; 32964 MW; 230076E0CBCA4222 CRC64;
MQVLRTPDER FEALADWPYA PHYATVTDAD GTVMRLHYVD EGPRDAPVVL LMHGEPSWAY
LYRKITAGLV AKGHRVIAPD LIGFGRSDKP TLRTDYTYER HVAWMSQWLT GLDLKDLTLF
CQDWGGLIGL RLVAAFPERF AAVTVGNTGL PIGTGWSEGF KAWLDFSQNT PTMPIGLIVN
MGTGRDLSAE EVAAYDAPFP DESFKEGARQ FPTLVPITPE HGSVAENKAA WEVLSAYDKP
FLTAFSDGDA VTRGGEAIFK ERVPGTAGQP HVILPGGHFL QEDCPDAIVE LLDGLVARAH
A
//
