HAD9_PSEPU
ID HAD9_PSEPU Reviewed; 224 AA.
AC Q59728;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=(S)-2-haloacid dehalogenase H-109 {ECO:0000305};
DE EC=3.8.1.2 {ECO:0000250|UniProtKB:Q52087};
DE AltName: Full=2-haloalkanoic acid dehalogenase H-109;
DE AltName: Full=Halocarboxylic acid halidohydrolase H-109;
DE AltName: Full=L-2-haloacid dehalogenase H-109 {ECO:0000303|PubMed:7764511};
GN Name=dehH109 {ECO:0000303|PubMed:7764511};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid pUOH109.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=109;
RX PubMed=7764511; DOI=10.1271/bbb.58.160;
RA Kawasaki H., Toyama T., Maeda T., Nishino H., Tonomura K.;
RT "Cloning and sequence analysis of a plasmid-encoded 2-haloacid dehalogenase
RT gene from Pseudomonas putida No. 109.";
RL Biosci. Biotechnol. Biochem. 58:160-163(1994).
CC -!- FUNCTION: Catalyzes the hydrolytic dehalogenation of small (S)-2-
CC haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic
CC acids (By similarity). Acts on acids of short chain lengths, C(2) to
CC C(4), with inversion of configuration at C-2 (By similarity). Active
CC with 2-halogenated carboxylic acids and converts only the S-isomer (or
CC L-isomer) of 2-chloropropionic acid with inversion of configuration to
CC produce R-lactate (or D-isomer) (By similarity).
CC {ECO:0000250|UniProtKB:Q52087}.
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:Q52087};
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; D17523; BAA04474.1; -; Genomic_DNA.
DR PIR; JC2075; JC2075.
DR RefSeq; WP_021703071.1; NZ_RJAI01000086.1.
DR AlphaFoldDB; Q59728; -.
DR SMR; Q59728; -.
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; Plasmid.
FT CHAIN 1..224
FT /note="(S)-2-haloacid dehalogenase H-109"
FT /id="PRO_0000079164"
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 224 AA; 25231 MW; 2443D7EEEF7B6A8A CRC64;
MQPIEGIVFD LYGTLYDVHS VVQACESAYP GQGEAISRLW RQKQLEYTWL SSLMGRYASF
EQRTEEALRY TCKHLGLATD ETTLRQLGQA YLHLAPHPDT TAALRRLKAS GLPMAIASNG
SHHSIEQVVS HSDMGWAFDH LISVETVKVF KPDNRVYSLA EQTMAIPRDR LLFVSSNSWD
ATGARHFGFP VCWVNRQGAV FDELGATPTR EVRDLGEMSD WLLD