ID   DHAA_PSEPV              Reviewed;         293 AA.
AC   P0A3G4; Q53042;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Haloalkane dehalogenase;
DE            EC=3.8.1.5 {ECO:0000269|PubMed:9687453};
GN   Name=dhaA;
OS   Pseudomonas pavonaceae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=47881;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RC   STRAIN=170;
RX   PubMed=9687453; DOI=10.1128/aem.64.8.2931-2936.1998;
RA   Poelarends G.J., Wilkens M., Larkin M.J., van Elsas J.D., Janssen D.B.;
RT   "Degradation of 1,3-dichloropropene by Pseudomonas cichorii 170.";
RL   Appl. Environ. Microbiol. 64:2931-2936(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=170;
RX   PubMed=10735862; DOI=10.1128/jb.182.8.2191-2199.2000;
RA   Poelarends G.J., Kulakov L.A., Larkin M.J., van Hylckama Vlieg J.E.T.,
RA   Janssen D.B.;
RT   "Roles of horizontal gene transfer and gene integration in evolution of
RT   1,3-dichloropropene- and 1,2-dibromoethane-degradative pathways.";
RL   J. Bacteriol. 182:2191-2199(2000).
CC   -!- FUNCTION: Catalyzes hydrolytic cleavage of carbon-halogen bonds in
CC       halogenated aliphatic compounds, leading to the formation of the
CC       corresponding primary alcohols, halide ions and protons. Has a broad
CC       substrate specificity, as it is able to dehalogenate mono- and
CC       di- chlorinated and brominated alkanes (up to at least C10), and the
CC       two isomers of 1,3-dichloropropene to 3-chloroallyl alcohol; the
CC       highest activity was found with 1,2-dibromoethane, while no activity
CC       was observed with the analog 1,2-dichloroethane.
CC       {ECO:0000269|PubMed:9687453}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-haloalkane + H2O = a halide anion + a primary alcohol +
CC         H(+); Xref=Rhea:RHEA:19081, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15734, ChEBI:CHEBI:16042, ChEBI:CHEBI:18060; EC=3.8.1.5;
CC         Evidence={ECO:0000269|PubMed:9687453};
CC   -!- PATHWAY: Xenobiotic degradation; haloalkane degradation.
CC   -!- PATHWAY: Xenobiotic degradation; 1,3-dichloropropene degradation.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- INDUCTION: Constitutively expressed.
CC   -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ250371; CAB65362.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0A3G4; -.
DR   SMR; P0A3G4; -.
DR   ESTHER; rhoso-halo1; Haloalkane_dehalogenase-HLD2.
DR   UniPathway; UPA00005; -.
DR   UniPathway; UPA00007; -.
DR   GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01231; Haloalk_dehal_type2; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR023594; Haloalkane_dehalogenase_2.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Detoxification; Direct protein sequencing; Hydrolase.
FT   CHAIN           1..293
FT                   /note="Haloalkane dehalogenase"
FT                   /id="PRO_0000216774"
FT   DOMAIN          34..158
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  33246 MW;  2B637C53E36BE9F3 CRC64;
     MSEIGTGFPF DPHYVEVLGE RMHYVDVGPR DGTPVLFLHG NPTSSYLWRN IIPHVAPSHR
     CIAPDLIGMG KSDKPDLDYF FDDHVRYLDA FIEALGLEEV VLVIHDWGSA LGFHWAKRNP
     ERVKGIACME FIRPIPTWDE WPEFARETFQ AFRTADVGRE LIIDQNAFIE GALPKCVVRP
     LTEVEMDHYR EPFLKPVDRE PLWRFPNELP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW
     GTPGVLIPPA EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PAL