HAD4_BURCE
ID HAD4_BURCE Reviewed; 231 AA.
AC Q51645;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=(S)-2-haloacid dehalogenase 4A {ECO:0000305};
DE EC=3.8.1.2 {ECO:0000269|PubMed:1376111};
DE AltName: Full=2-haloalkanoic acid dehalogenase IVA;
DE AltName: Full=Halocarboxylic acid halidohydrolase IVA {ECO:0000303|PubMed:1376111};
DE AltName: Full=L-2-haloacid dehalogenase IVA;
GN Name=hdl IVa {ECO:0000303|PubMed:1376111};
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=MBA4;
RX PubMed=1376111; DOI=10.1042/bj2840087;
RA Murdiyatmo U., Asmara W., Tsang J.S.H., Baines A.J., Bull A.T.,
RA Hardman D.J.;
RT "Molecular biology of the 2-haloacid halidohydrolase IVa from Pseudomonas
RT cepacia MBA4.";
RL Biochem. J. 284:87-93(1992).
RN [2] {ECO:0007744|PDB:2NO4, ECO:0007744|PDB:2NO5}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 2-231 IN COMPLEX WITH
RP (2S)-2-CHLOROPROPANOIC ACID, AND ACTIVE SITE.
RX PubMed=17368477; DOI=10.1016/j.jmb.2007.02.015;
RA Schmidberger J.W., Wilce J.A., Tsang J.S., Wilce M.C.;
RT "Crystal structures of the substrate free-enzyme, and reaction intermediate
RT of the HAD superfamily member, haloacid dehalogenase DehIVa from
RT Burkholderia cepacia MBA4.";
RL J. Mol. Biol. 368:706-717(2007).
CC -!- FUNCTION: Catalyzes the hydrolytic dehalogenation of small (S)-2-
CC haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic
CC acids (PubMed:1376111). Acts on acids of short chain lengths, C(2) to
CC C(4), with inversion of configuration at C-3 (PubMed:1376111). 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:1376111).
CC {ECO:0000269|PubMed:1376111}.
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:1376111};
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:1376111};
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; X66249; CAA46976.1; -; Genomic_DNA.
DR PIR; S29096; S29096.
DR PDB; 2NO4; X-ray; 1.93 A; A/B=2-231.
DR PDB; 2NO5; X-ray; 2.60 A; A/B=2-231.
DR PDBsum; 2NO4; -.
DR PDBsum; 2NO5; -.
DR AlphaFoldDB; Q51645; -.
DR SMR; Q51645; -.
DR BRENDA; 3.8.1.2; 1028.
DR EvolutionaryTrace; Q51645; -.
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; TIGR01549; HAD-SF-IA-v1; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1376111"
FT CHAIN 2..231
FT /note="(S)-2-haloacid dehalogenase 4A"
FT /id="PRO_0000079162"
FT REGION 176..181
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:17368477"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:17368477,
FT ECO:0007744|PDB:2NO5"
FT BINDING 12..13
FT /ligand="an (S)-2-haloacid"
FT /ligand_id="ChEBI:CHEBI:137405"
FT /evidence="ECO:0000269|PubMed:17368477,
FT ECO:0007744|PDB:2NO5"
FT BINDING 42
FT /ligand="an (S)-2-haloacid"
FT /ligand_id="ChEBI:CHEBI:137405"
FT /evidence="ECO:0000269|PubMed:17368477,
FT ECO:0007744|PDB:2NO5"
FT BINDING 119..120
FT /ligand="an (S)-2-haloacid"
FT /ligand_id="ChEBI:CHEBI:137405"
FT /evidence="ECO:0000269|PubMed:17368477,
FT ECO:0007744|PDB:2NO5"
FT SITE 15
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:17368477"
FT SITE 152
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:17368477"
FT SITE 158
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:17368477"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:2NO4"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 34..54
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 61..75
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:2NO4"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2NO4"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2NO4"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:2NO4"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:2NO4"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2NO4"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:2NO4"
SQ SEQUENCE 231 AA; 25995 MW; 75EBC85604B5F93C CRC64;
MVDSLRACVF DAYGTLLDVH SAVMRNADEV GASAEALSML WRQRQLEYSW TRTLMHQYAD
FWQLTDEALT FALRTYHLED RKGLKDRLMS AYKELSAYPD AAETLEKLKS AGYIVAILSN
GNDEMLQAAL KASKLDRVLD SCLSADDLKI YKPDPRIYQF ACDRLGVNPN EVCFVSSNAW
DLGGAGKFGF NTVRINRQGN PPEYEFAPLK HQVNSLSELW PLLAKNVTKA A
