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Database: UniProt
Entry: Q0B1K6_BURCM
LinkDB: Q0B1K6_BURCM
Original site: Q0B1K6_BURCM 
ID   Q0B1K6_BURCM            Unreviewed;       234 AA.
AC   Q0B1K6;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 86.
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=Bamb_6423 {ECO:0000313|EMBL:ABI91967.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI91967.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-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; CP000442; ABI91967.1; -; Genomic_DNA.
DR   RefSeq; WP_011661293.1; NZ_CP009800.1.
DR   AlphaFoldDB; Q0B1K6; -.
DR   GeneID; 69549379; -.
DR   KEGG; bam:Bamb_6423; -.
DR   PATRIC; fig|339670.21.peg.6314; -.
DR   eggNOG; COG1011; Bacteria.
DR   Proteomes; UP000000662; Chromosome 3.
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; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU368077}.
SQ   SEQUENCE   234 AA;  26622 MW;  4534B1CFABE4CA4E CRC64;
     MSNAEQLKSE IKVVMFDQYG TVVDMQRGLT EIAAPFLKEK GWTGNPNSFV TWWRRTHFEN
     SMIDALLHKE HTPYREIGHR AVAYTLERAG IQYTQEEVRY LVSCIERLKP FPDVPEALAR
     LQTRYKIVVL SNGDPDMLET AKEYHKIPFD NVISVKAAES FKPHVATYTK AAEIMGVKLS
     EVLFVANHAF DCIGAKSAGM RSAFIDRRKR PFGGTPHQPD IWVDDMSSLA DLMV
//
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