ID Q11K15_CHESB Unreviewed; 220 AA.
AC Q11K15;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=(S)-2-haloacid dehalogenase {ECO:0000256|RuleBase:RU368077};
DE EC=3.8.1.2 {ECO:0000256|RuleBase:RU368077};
DE AltName: Full=2-haloalkanoic acid dehalogenase {ECO:0000256|RuleBase:RU368077};
DE AltName: Full=Halocarboxylic acid halidohydrolase {ECO:0000256|RuleBase:RU368077};
DE AltName: Full=L-2-haloacid dehalogenase {ECO:0000256|RuleBase:RU368077};
GN OrderedLocusNames=Meso_0860 {ECO:0000313|EMBL:ABG62260.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG62260.1};
RN [1] {ECO:0000313|EMBL:ABG62260.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG62260.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic dehalogenation of small (S)-2-
CC haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic
CC acids. {ECO:0000256|RuleBase:RU368077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (S)-2-haloacid + H2O = a (2R)-2-hydroxycarboxylate + a
CC halide anion + H(+); Xref=Rhea:RHEA:11192, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:58314,
CC ChEBI:CHEBI:137405; EC=3.8.1.2;
CC Evidence={ECO:0000256|RuleBase:RU368077};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. S-2-
CC haloalkanoic acid dehalogenase family. {ECO:0000256|ARBA:ARBA00008106,
CC ECO:0000256|RuleBase:RU368077}.
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DR EMBL; CP000390; ABG62260.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11K15; -.
DR STRING; 266779.Meso_0860; -.
DR KEGG; mes:Meso_0860; -.
DR eggNOG; COG1011; Bacteria.
DR HOGENOM; CLU_045011_3_1_5; -.
DR OrthoDB; 7989657at2; -.
DR GO; GO:0018784; F:(S)-2-haloacid dehalogenase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02588; HAD_L2-DEX; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006328; 2-HAD.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01493; HAD-SF-IA-v2; 1.
DR NCBIfam; TIGR01428; HAD_type_II; 1.
DR PANTHER; PTHR43316:SF3; HALOACID DEHALOGENASE, TYPE II (AFU_ORTHOLOGUE AFUA_2G07750)-RELATED; 1.
DR PANTHER; PTHR43316; HYDROLASE, HALOACID DELAHOGENASE-RELATED; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDF00045; 2-haloacid_dehalogenase; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368077}.
SQ SEQUENCE 220 AA; 24563 MW; 91A059E6AB89973F CRC64;
MRFSAFVFDA YGTVFDVHSA VRRHAGDIGP AGQTLSEIWR AKQLEYSWIG TLMDDYADFW
VLTERALDFA FKKVPSADPA LKQKLLEAYW RLDCYPEVPA VLSALKSSGA RISILSNGSP
EMLEAALRSS ALDTVVDDVF SADMVGKFKT HPAVYELVTT ALRVYPDAVS FQSANRWDVA
GAGSFGFRTV WINRSDQPDE YHEYPPQLIL PSLKGLLTDR
//
