ID   DHMA_PHEZH              Reviewed;         301 AA.
AC   B4RF90;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Haloalkane dehalogenase {ECO:0000255|HAMAP-Rule:MF_01230};
DE            EC=3.8.1.5 {ECO:0000255|HAMAP-Rule:MF_01230};
GN   Name=dhmA {ECO:0000255|HAMAP-Rule:MF_01230}; OrderedLocusNames=PHZ_c2250;
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1;
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01230}.
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:0000255|HAMAP-Rule:MF_01230};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01230}.
CC   -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01230}.
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DR   EMBL; CP000747; ACG78660.1; -; Genomic_DNA.
DR   RefSeq; WP_012522801.1; NC_011144.1.
DR   AlphaFoldDB; B4RF90; -.
DR   SMR; B4RF90; -.
DR   STRING; 450851.PHZ_c2250; -.
DR   ESTHER; phezh-dhma; Haloalkane_dehalogenase-HLD1.
DR   PRIDE; B4RF90; -.
DR   EnsemblBacteria; ACG78660; ACG78660; PHZ_c2250.
DR   KEGG; pzu:PHZ_c2250; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_13_3_5; -.
DR   OMA; TLFCQDW; -.
DR   OrthoDB; 1890883at2; -.
DR   Proteomes; UP000001868; Chromosome.
DR   GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01230; Haloalk_dehal_type1; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR023489; Haloalkane_dehalogenase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..301
FT                   /note="Haloalkane dehalogenase"
FT                   /id="PRO_1000139632"
FT   ACT_SITE        123
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01230"
FT   ACT_SITE        250
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01230"
FT   ACT_SITE        279
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01230"
SQ   SEQUENCE   301 AA;  32843 MW;  33F97C4356DFEDFB CRC64;
     MQVLRTPDER FEGLADWPFA PKYVQVKDAD GTLLRIHHVD EGPRDGAPVL LMHGEPSWAY
     LYRHIIPRLV AAGHRAIAPD LVGFGRSDKP ADRGDYTYAR HVAWMSAWLE AVDLRGAYLF
     CQDWGGLIGL RLVAAYPERF AGVVVSNTGL PVGGGAMTDG FKAWLQFSQT VPELPIGFLL
     NGGSVRELSA AEMAAYDAPF PDESYKEGAR QFPALVPVTS EHAGVAENQA AWKVLEAWDK
     PLVTAFSDGD PITKGGEVPF RERVPGARGQ PHVTLHGGHF VQEDSPAEIA GLLDGLIRRS
     R