HAD_AGRTR
ID HAD_AGRTR Reviewed; 232 AA.
AC P60527;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=(S)-2-haloacid dehalogenase {ECO:0000305};
DE EC=3.8.1.2 {ECO:0000269|PubMed:9425247};
DE AltName: Full=2-haloalkanoic acid dehalogenase;
DE AltName: Full=Cryptic L-isomer-specific dehalogenase {ECO:0000303|PubMed:9425247};
DE AltName: Full=DhlS5I {ECO:0000303|PubMed:9425247};
DE AltName: Full=Halocarboxylic acid halidohydrolase;
DE AltName: Full=L-2-haloacid dehalogenase;
DE AltName: Full=L-DEX;
OS Agrobacterium tumefaciens (strain RS5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=260551;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9425247; DOI=10.1007/s002849900286;
RA Kohler R., Brokamp A., Schwarze R., Reiting R.H., Schmidt F.R.J.;
RT "Characteristics and DNA-sequence of a cryptic haloalkanoic acid
RT dehalogenase from Agrobacterium tumefaciens RS5.";
RL Curr. Microbiol. 36:96-101(1998).
CC -!- FUNCTION: Catalyzes the hydrolytic dehalogenation of small (S)-2-
CC haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic
CC acids (PubMed:9425247). Acts on acids of short chain lengths, C(2) to
CC C(4), with inversion of configuration at C-2 (PubMed:9425247). 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) (PubMed:9425247).
CC {ECO:0000269|PubMed:9425247}.
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:0000269|PubMed:9425247};
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:0000269|PubMed:9425247};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:9425247};
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 AlphaFoldDB; P60527; -.
DR SMR; P60527; -.
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; TIGR01428; HAD_type_II; 1.
PE 1: Evidence at protein level;
KW Hydrolase.
FT CHAIN 1..232
FT /note="(S)-2-haloacid dehalogenase"
FT /id="PRO_0000079168"
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 232 AA; 26164 MW; A618DD4ECF22DBC1 CRC64;
MKHIKAIAFD LYGTLFDVHS VIDQCEKRFP GRGREVSTLW RQKQLEYTWL RSLMNRYVTF
EQATEDALRY TCRHLGFALD DAACTVLCDA YLRLQAFPEV PPRLRELRNR GLQLAVLSNG
SPHSIGAVVG NAGIRDEFDH LISVDPVRVY KPHDRAYGLA EEAFGLARTS ILFVSSNGWD
ATGARYFGFP TCWINRGGNV FEEMGQTPDW DLLGIDEIVR LFDSAEGSAP SV