HADL_PSEPU
ID HADL_PSEPU Reviewed; 227 AA.
AC Q52087;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=(S)-2-haloacid dehalogenase {ECO:0000305};
DE EC=3.8.1.2 {ECO:0000269|PubMed:1588303};
DE AltName: Full=2-haloalkanoic acid dehalogenase;
DE AltName: Full=Halocarboxylic acid halidohydrolase {ECO:0000303|PubMed:1588303};
DE AltName: Full=L-2-haloacid dehalogenase;
GN Name=hadL {ECO:0000303|PubMed:1588303};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=AJ1;
RX PubMed=1588303; DOI=10.1099/00221287-138-4-675;
RA Jones D.H., Barth P.T., Byrom D., Thomas C.M.;
RT "Nucleotide sequence of the structural gene encoding a 2-haloalkanoic acid
RT dehalogenase of Pseudomonas putida strain AJ1 and purification of the
RT encoded protein.";
RL J. Gen. Microbiol. 138:675-683(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AJ1;
RX PubMed=1556080; DOI=10.1128/jb.174.8.2612-2619.1992;
RA Barth P.T., Bolton L., Thomson J.C.;
RT "Cloning and partial sequencing of an operon encoding two Pseudomonas
RT putida haloalkanoate dehalogenases of opposite stereospecificity.";
RL J. Bacteriol. 174:2612-2619(1992).
CC -!- FUNCTION: Catalyzes the hydrolytic dehalogenation of small (S)-2-
CC haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic
CC acids (PubMed:1588303). Acts on acids of short chain lengths, C(2) to
CC C(4), with inversion of configuration at C-2 (PubMed:1588303). 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:1588303).
CC {ECO:0000269|PubMed:1588303}.
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:1588303};
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:1588303};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 10 and 11. {ECO:0000269|PubMed:1588303};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1588303}.
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; M81841; AAA25832.1; -; Genomic_DNA.
DR PIR; A44830; A44830.
DR AlphaFoldDB; Q52087; -.
DR SMR; Q52087; -.
DR BRENDA; 3.8.1.2; 5092.
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 1: Evidence at protein level;
KW Hydrolase.
FT CHAIN 1..227
FT /note="(S)-2-haloacid dehalogenase"
FT /id="PRO_0000079163"
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; 25687 MW; DDDE58BDAEB46FAA CRC64;
MKNIQGIVFD LYGTLYDVHS VVQACEEVYP GQGDAISRLW RQKQLEYTWL RSLMGRYVNF
EKATEDALRF TCTHLGLSLD DETHQRLSDA YLHLTPYADT ADAVRRLKAA GLPLGIISNG
SHCSIEQVVT NSEMNWAFDQ LISVEDVQVF KPDSRVYSLA EKRMGFPKEN ILFVSSNAWD
ASAASNFGFP VCWINRQNGA FDELDAKPTH VVRNLAEMSN WLVNSLD
