HADD_PSEPU
ID HADD_PSEPU Reviewed; 301 AA.
AC Q52086;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=(R)-2-haloacid dehalogenase;
DE EC=3.8.1.9;
DE AltName: Full=D-2-haloacid dehalogenase;
DE AltName: Full=D-DEX;
GN Name=hadD;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10198020; DOI=10.1128/jb.181.8.2535-2547.1999;
RA Hill K.E., Marchesi J.R., Weightman A.J.;
RT "Investigation of two evolutionarily unrelated halocarboxylic acid
RT dehalogenase gene families.";
RL J. Bacteriol. 181:2535-2547(1999).
CC -!- FUNCTION: Catalyzes the hydrolytic dehalogenation of small (R)-2-
CC haloalkanoic acids to yield the corresponding (S)-2-hydroxyalkanoic
CC acids. Acts on acids of short chain lengths, C(2) to C(4), with
CC inversion of configuration at C-2.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (R)-2-haloacid + H2O = a (2S)-2-hydroxycarboxylate + a
CC halide anion + H(+); Xref=Rhea:RHEA:22188, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:58123,
CC ChEBI:CHEBI:137406; EC=3.8.1.9;
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. S-2-
CC haloalkanoic acid dehalogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25831.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M81841; AAA25831.1; ALT_FRAME; Genomic_DNA.
DR PIR; B41840; B41840.
DR PDB; 5GZX; X-ray; 2.35 A; A/B/C/D=1-301.
DR PDB; 5GZY; X-ray; 2.18 A; A/B/C/D=1-301.
DR PDB; 5H00; X-ray; 2.64 A; A/B/C/D=1-301.
DR PDB; 5H01; X-ray; 2.19 A; A/B/C/D=1-301.
DR PDBsum; 5GZX; -.
DR PDBsum; 5GZY; -.
DR PDBsum; 5H00; -.
DR PDBsum; 5H01; -.
DR AlphaFoldDB; Q52086; -.
DR SMR; Q52086; -.
DR BRENDA; 3.8.1.9; 5092.
DR GO; GO:0033975; F:(R)-2-haloacid dehalogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.1290.10; -; 2.
DR InterPro; IPR019714; 2-haloacid_dehalogenase_DehI.
DR InterPro; IPR029032; AhpD-like.
DR Pfam; PF10778; DehI; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase.
FT CHAIN 1..301
FT /note="(R)-2-haloacid dehalogenase"
FT /id="PRO_0000079169"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 77..97
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 114..147
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5GZY"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 230..248
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:5GZY"
FT HELIX 268..298
FT /evidence="ECO:0007829|PDB:5GZY"
SQ SEQUENCE 301 AA; 33977 MW; DA76926AFFFB7E51 CRC64;
MNLPDNSIHL QLPRPVCEAI IRPVPEHRAD QELSEIYRDL KATFGVPWVG VITQAVAYYR
PFFAEAWRRF APSAKTHFFE RASDDIRIRS WELMGQSFVI EGQTDRLREM GYSVREIGQI
RAVLDIFDYG NPKYLIFATA IKEGLLSGRT FGGAAGDARC HFPRSPICQI DPIPVMVEEH
HAGGTLSQVY ADIKQTLQLP FINSDYKAMA RWPSYLEQAW GALKPCIDTP AYQAGRFDIN
ARALAALDAL PTAYRMSRDD ALQAGLSEAQ TDELIQVISL FQWMLSGLVL NVTHFKQQAL
K