ID   Q12G50_POLSJ            Unreviewed;       229 AA.
AC   Q12G50;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=Bpro_0530 {ECO:0000313|EMBL:ABE42492.1};
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE42492.1, ECO:0000313|Proteomes:UP000001983};
RN   [1] {ECO:0000313|Proteomes:UP000001983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX   PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
RN   [2] {ECO:0007829|PDB:3UM9}
RP   X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS).
RA   Chan P.W.Y., To T.K.W., Petit P., Tran C., Waelti M., Savchenko A.,
RA   Yakunin A.F., Edwards E.A., Pai E.F.;
RT   "Structural adaptations of L-2-haloacid dehalogenases that enable
RT   hydrolytic defluorination.";
RL   Submitted (NOV-2011) to the PDB data bank.
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; CP000316; ABE42492.1; -; Genomic_DNA.
DR   RefSeq; WP_011481495.1; NC_007948.1.
DR   PDB; 3UM9; X-ray; 2.19 A; A/B=1-229.
DR   PDBsum; 3UM9; -.
DR   AlphaFoldDB; Q12G50; -.
DR   SMR; Q12G50; -.
DR   STRING; 296591.Bpro_0530; -.
DR   KEGG; pol:Bpro_0530; -.
DR   eggNOG; COG1011; Bacteria.
DR   HOGENOM; CLU_045011_3_1_4; -.
DR   OrthoDB; 264363at2; -.
DR   Proteomes; UP000001983; Chromosome.
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; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3UM9};
KW   Hydrolase {ECO:0000256|RuleBase:RU368077, ECO:0000313|EMBL:ABE42492.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001983}.
SQ   SEQUENCE   229 AA;  25447 MW;  21525491C306A94F CRC64;
     MHAIKAVVFD LYGTLYDVYS VRTSCERIFP GQGEMVSKMW RQKQLEYTWM RTLMGQYQDF
     ESATLDALRY TCGSLGLALD ADGEAHLCSE YLSLTPFADV PQALQQLRAA GLKTAILSNG
     SRHSIRQVVG NSGLTNSFDH LISVDEVRLF KPHQKVYELA MDTLHLGESE ILFVSCNSWD
     ATGAKYFGYP VCWINRSNGV FDQLGVVPDI VVSDVGVLAS RFSPVDEAA
//