HAD_XANAU
ID HAD_XANAU Reviewed; 253 AA.
AC Q60099; Q56757;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=(S)-2-haloacid dehalogenase {ECO:0000305};
DE EC=3.8.1.2 {ECO:0000269|PubMed:1744048};
DE AltName: Full=2-haloalkanoic acid dehalogenase {ECO:0000303|PubMed:7580000};
DE AltName: Full=Halocarboxylic acid halidohydrolase;
DE AltName: Full=L-2-haloacid dehalogenase {ECO:0000303|PubMed:1744048};
GN Name=dhlB {ECO:0000303|PubMed:1744048};
OS Xanthobacter autotrophicus.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=GJ10;
RX PubMed=1744048; DOI=10.1128/jb.173.24.7925-7933.1991;
RA van der Ploeg J., van Hall G., Janssen D.B.;
RT "Characterization of the haloacid dehalogenase from Xanthobacter
RT autotrophicus GJ10 and sequencing of the dhlB gene.";
RL J. Bacteriol. 173:7925-7933(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122.
RC STRAIN=GJ10;
RX PubMed=7580000; DOI=10.1007/bf00700465;
RA van der Ploeg J., Janssen D.B.;
RT "Sequence analysis of the upstream region of dhlB, the gene encoding
RT haloalkanoic acid dehalogenase of Xanthobacter autotrophicus GJ10.";
RL Biodegradation 6:257-263(1995).
RN [3] {ECO:0007744|PDB:1AQ6}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH FORMATE, SEQUENCE
RP REVISION TO 84, SUBUNIT, AND ACTIVE SITE.
RC STRAIN=GJ10;
RX PubMed=9407083; DOI=10.1074/jbc.272.52.33015;
RA Ridder I.S., Rozeboom H.J., Kalk K.H., Janssen D.B., Dijkstra B.W.;
RT "Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter
RT autotrophicus GJ10 complexed with the substrate-analogue formate.";
RL J. Biol. Chem. 272:33015-33022(1997).
RN [4] {ECO:0007744|PDB:1QQ5, ECO:0007744|PDB:1QQ6, ECO:0007744|PDB:1QQ7}
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) IN COMPLEX WITH FORMATE;
RP (S)-2-MONOCHLOROPROPIONATE AND MONOCHLOROACETATE, AND ACTIVE SITE.
RX PubMed=10521454; DOI=10.1074/jbc.274.43.30672;
RA Ridder I.S., Rozeboom H.J., Kalk K.H., Dijkstra B.W.;
RT "Crystal structures of intermediates in the dehalogenation of
RT haloalkanoates by L-2-haloacid dehalogenase.";
RL J. Biol. Chem. 274:30672-30678(1999).
CC -!- FUNCTION: Catalyzes the hydrolytic dehalogenation of small (S)-2-
CC haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic
CC acids (PubMed:1744048). Acts on acids of short chain lengths, C(2) to
CC C(4), with inversion of configuration at C-2 (PubMed:1744048). 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:1744048).
CC {ECO:0000269|PubMed:1744048}.
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:1744048};
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:1744048};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:1744048};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9407083}.
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; M81691; AAA27590.1; -; Genomic_DNA.
DR EMBL; X86084; CAA60039.1; -; Genomic_DNA.
DR PIR; S52840; S52840.
DR PDB; 1AQ6; X-ray; 1.95 A; A/B=1-253.
DR PDB; 1QQ5; X-ray; 1.52 A; A/B=1-253.
DR PDB; 1QQ6; X-ray; 2.10 A; A/B=1-253.
DR PDB; 1QQ7; X-ray; 1.70 A; A/B=1-253.
DR PDBsum; 1AQ6; -.
DR PDBsum; 1QQ5; -.
DR PDBsum; 1QQ6; -.
DR PDBsum; 1QQ7; -.
DR AlphaFoldDB; Q60099; -.
DR SMR; Q60099; -.
DR DrugBank; DB03522; Aspartic Acid-4-Carboxymethyl Ester.
DR DrugBank; DB01942; Formic acid.
DR BRENDA; 3.8.1.2; 1641.
DR EvolutionaryTrace; Q60099; -.
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; 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 CHAIN 1..253
FT /note="(S)-2-haloacid dehalogenase"
FT /id="PRO_0000079159"
FT REGION 171..176
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:10521454,
FT ECO:0000305|PubMed:9407083"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:10521454,
FT ECO:0000269|PubMed:9407083"
FT BINDING 9..10
FT /ligand="an (S)-2-haloacid"
FT /ligand_id="ChEBI:CHEBI:137405"
FT /evidence="ECO:0000269|PubMed:10521454,
FT ECO:0000269|PubMed:9407083, ECO:0007744|PDB:1AQ6,
FT ECO:0007744|PDB:1QQ5, ECO:0007744|PDB:1QQ6,
FT ECO:0007744|PDB:1QQ7"
FT BINDING 39
FT /ligand="an (S)-2-haloacid"
FT /ligand_id="ChEBI:CHEBI:137405"
FT /evidence="ECO:0000269|PubMed:10521454,
FT ECO:0007744|PDB:1QQ6, ECO:0007744|PDB:1QQ7"
FT BINDING 114..115
FT /ligand="an (S)-2-haloacid"
FT /ligand_id="ChEBI:CHEBI:137405"
FT /evidence="ECO:0000269|PubMed:10521454,
FT ECO:0000269|PubMed:9407083, ECO:0007744|PDB:1AQ6,
FT ECO:0007744|PDB:1QQ5, ECO:0007744|PDB:1QQ6,
FT ECO:0007744|PDB:1QQ7"
FT SITE 12
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:10521454,
FT ECO:0000305|PubMed:9407083"
FT SITE 147
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:10521454,
FT ECO:0000305|PubMed:9407083"
FT SITE 153
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:10521454,
FT ECO:0000305|PubMed:9407083"
FT CONFLICT 84
FT /note="D -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1QQ5"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1QQ5"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 31..52
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 58..72
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:1QQ5"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1QQ5"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1QQ5"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1QQ5"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:1QQ5"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:1QQ5"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1QQ5"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:1QQ5"
SQ SEQUENCE 253 AA; 27469 MW; E2AB8DEED37A5716 CRC64;
MIKAVVFDAY GTLFDVQSVA DATERAYPGR GEYITQVWRQ KQLEYSWLRA LMGRYADFWG
VTREALAYTL GTLGLEPDES FLADMAQAYN RLTPYPDAAQ CLAELAPLKR AILSNGAPDM
LQALVANAGL TDSFDAVISV DAKRVFKPHP DSYALVEEVL GVTPAEVLFV SSNGFDVGGA
KNFGFSVARV ARLSQEALAR ELVSGTIAPL TMFKALRMRE ETYAEAPDFV VPALGDLPRL
VRGMAGAHLA PAV
