ID   HAD_PSEFL               Reviewed;         227 AA.
AC   Q59666;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=(S)-2-haloacid dehalogenase {ECO:0000305};
DE            EC=3.8.1.2 {ECO:0000250|UniProtKB:Q53464};
DE   AltName: Full=2-haloalkanoic acid dehalogenase;
DE   AltName: Full=Halocarboxylic acid halidohydrolase;
DE   AltName: Full=L-2-haloacid dehalogenase;
GN   Name=dhl VII;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ABVII;
RA   Honnens E., Reiting R., Brokamp A., Schmidt F.J.R.;
RL   Submitted (DEC-1999) 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. Acts on acids of short chain lengths, C(2) to C(4), with
CC       inversion of configuration at C-2. Active with 2-halogenated carboxylic
CC       acids and converts only the S-isomer (or L-isomer) of 2-chloropropionic
CC       acid with inversion of configuration to produce R-lactate (or D-
CC       isomer). {ECO:0000250|UniProtKB:Q53464}.
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:0000250|UniProtKB:Q53464};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-chloropropanoate + H2O = (R)-lactate + chloride + H(+);
CC         Xref=Rhea:RHEA:67956, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16004, ChEBI:CHEBI:17996, ChEBI:CHEBI:73934;
CC         Evidence={ECO:0000250|UniProtKB:Q53464};
CC   -!- BIOTECHNOLOGY: (S)-2-haloacid dehalogenases may be used for the
CC       biodegradation of halogenated substances and their derivatives which
CC       are widely used as pesticides, herbicides and other industrial
CC       products. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. S-2-
CC       haloalkanoic acid dehalogenase family. {ECO:0000305}.
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DR   EMBL; X94147; CAA63861.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q59666; -.
DR   SMR; Q59666; -.
DR   GO; GO:0018784; F:(S)-2-haloacid dehalogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd02588; HAD_L2-DEX; 1.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR006328; 2-HAD.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   Pfam; PF13419; HAD_2; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01493; HAD-SF-IA-v2; 1.
DR   TIGRFAMs; TIGR01428; HAD_type_II; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..227
FT                   /note="(S)-2-haloacid dehalogenase"
FT                   /id="PRO_0000079165"
FT   REGION          175..180
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q53464"
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q53464"
FT   BINDING         11..12
FT                   /ligand="an (S)-2-haloacid"
FT                   /ligand_id="ChEBI:CHEBI:137405"
FT                   /evidence="ECO:0000250|UniProtKB:Q53464"
FT   BINDING         41
FT                   /ligand="an (S)-2-haloacid"
FT                   /ligand_id="ChEBI:CHEBI:137405"
FT                   /evidence="ECO:0000250|UniProtKB:Q53464"
FT   BINDING         118..119
FT                   /ligand="an (S)-2-haloacid"
FT                   /ligand_id="ChEBI:CHEBI:137405"
FT                   /evidence="ECO:0000250|UniProtKB:Q53464"
FT   SITE            14
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q53464"
FT   SITE            151
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q53464"
FT   SITE            157
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q53464"
SQ   SEQUENCE   227 AA;  25637 MW;  479D5C29FA91F234 CRC64;
     MKNIQGAVFD LYGTLYDVNS VAQVCEEVYS GHGDSISRLW RQKQLEYTWL RSLMGRYVNF
     EKATEDALRF TCTHLGLSLD DETHQRLSDA YLHLTPYADT ADALRRLKAA GLPVGIISNG
     SHCSIEQVVT NSEMNWAFDQ LISVEDVQVF KPDSRVYSLA EKRMGFPKEN ILFVSSNAWD
     ASAASNFGFP VCWINRQNGA FDELDAKPTH VVRNLAEMSN WLVNSLD