HAD1_PSEUC
ID HAD1_PSEUC Reviewed; 227 AA.
AC P24069;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=(S)-2-haloacid dehalogenase 1 {ECO:0000305};
DE EC=3.8.1.2 {ECO:0000250|UniProtKB:Q53464};
DE AltName: Full=2-haloalkanoic acid dehalogenase I {ECO:0000303|PubMed:1995594};
DE AltName: Full=DEHCI {ECO:0000303|PubMed:1995594};
DE AltName: Full=Halocarboxylic acid halidohydrolase I;
DE AltName: Full=L-2-haloacid dehalogenase I;
OS Pseudomonas sp. (strain CBS-3).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=72586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1995594; DOI=10.1128/jb.173.4.1530-1535.1991;
RA Schneider B., Mueller R., Frank R., Lingens F.;
RT "Complete nucleotide sequences and comparison of the structural genes of
RT two 2-haloalkanoic acid dehalogenases from Pseudomonas sp. strain CBS3.";
RL J. Bacteriol. 173:1530-1535(1991).
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; M62908; AAA63640.1; -; Genomic_DNA.
DR PIR; A38452; A38452.
DR AlphaFoldDB; P24069; -.
DR SMR; P24069; -.
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; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01493; HAD-SF-IA-v2; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 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 1"
FT /id="PRO_0000079160"
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; 25430 MW; 0D2002A0282C92EE CRC64;
MDPIRACVFD AYGTLLDVNT AVMKHAHDIG GCAEELSSLW RQRQLEYSWT RTLMGRYADF
WQLTTEALDF ALESFGLLER TDLKNRLLDA YHELSAYPDA VGTLGALKAA GFTTAILSNG
NNEMLRGALR AGNLTEALDQ CISVDEIKIY KPDPRVYQFA CDRLDVRPSE VCFVSSNAWD
IGGAGAFGFN TVRINRINKP QEYSFAPQRH QLSSLSELPQ LLLRLTQ