ID DHAA_RHORH Reviewed; 293 AA. AC P0A3G2; Q53042; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 71. DE RecName: Full=Haloalkane dehalogenase; DE EC=3.8.1.5; GN Name=dhaA; OS Rhodococcus rhodochrous. OG Plasmid pRTL1. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=1829; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NCIMB 13064; RX PubMed=9025284; DOI=10.1099/00221287-143-1-109; RA Kulakova A.N., Larkin M.J., Kulakov L.A.; RT "The plasmid-located haloalkane dehalogenase gene from Rhodococcus RT rhodochrous NCIMB 13064."; RL Microbiology 143:109-115(1997). 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. Expresses CC halogenase activity against 1-chloroalkanes of chain length C3 to C10, CC and also shows a very weak activity with 1,2-dichloroethane. 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 -!- PATHWAY: Xenobiotic degradation; haloalkane degradation. CC -!- SUBUNIT: Monomer. CC -!- INDUCTION: By 1-haloalkanes. CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF060871; AAC15838.1; -; Genomic_DNA. DR PDB; 2V9Z; X-ray; 3.00 A; A=1-293. DR PDB; 3FBW; X-ray; 1.23 A; A=1-293. DR PDB; 3RK4; X-ray; 1.31 A; A=1-293. DR PDB; 3SK0; X-ray; 1.78 A; A=1-293. DR PDB; 4E46; X-ray; 1.26 A; A=1-293. DR PDB; 4F5Z; X-ray; 1.20 A; A=1-293. DR PDB; 4F60; X-ray; 1.45 A; A=1-293. DR PDB; 4FWB; X-ray; 1.26 A; A=4-293. DR PDB; 4WCV; X-ray; 1.69 A; A=1-293. DR PDB; 5FLK; X-ray; 0.99 A; A=1-293. DR PDB; 5UXZ; X-ray; 1.92 A; A/B=4-290. DR PDB; 5UY1; X-ray; 1.35 A; A/B=4-290. DR PDB; 5VNP; X-ray; 2.23 A; A/B=4-293. DR PDB; 6SP5; X-ray; 1.60 A; A/B=3-293. DR PDB; 6SP8; X-ray; 1.55 A; A/B=3-293. DR PDB; 6TY7; X-ray; 1.50 A; A/B=1-293. DR PDB; 6XT8; X-ray; 1.70 A; A/B/C/D=1-293. DR PDB; 6XTC; X-ray; 2.54 A; A/B/C/D=1-293. DR PDB; 7O3O; X-ray; 1.25 A; A=1-293. DR PDB; 7O8B; X-ray; 1.75 A; A=4-293. DR PDBsum; 2V9Z; -. DR PDBsum; 3FBW; -. DR PDBsum; 3RK4; -. DR PDBsum; 3SK0; -. DR PDBsum; 4E46; -. DR PDBsum; 4F5Z; -. DR PDBsum; 4F60; -. DR PDBsum; 4FWB; -. DR PDBsum; 4WCV; -. DR PDBsum; 5FLK; -. DR PDBsum; 5UXZ; -. DR PDBsum; 5UY1; -. DR PDBsum; 5VNP; -. DR PDBsum; 6SP5; -. DR PDBsum; 6SP8; -. DR PDBsum; 6TY7; -. DR PDBsum; 6XT8; -. DR PDBsum; 6XTC; -. DR PDBsum; 7O3O; -. DR PDBsum; 7O8B; -. DR AlphaFoldDB; P0A3G2; -. DR SMR; P0A3G2; -. DR ESTHER; rhoso-halo1; Haloalkane_dehalogenase-HLD2. DR BRENDA; 3.8.1.5; 5395. DR SABIO-RK; P0A3G2; -. DR UniPathway; UPA00007; -. DR EvolutionaryTrace; P0A3G2; -. 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; alpha/beta hydrolase; 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 PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1. DR PANTHER; PTHR43329:SF74; HALOALKANE DEHALOGENASE; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PRINTS; PR00412; EPOXHYDRLASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure; Detoxification; Hydrolase; Plasmid. FT CHAIN 1..293 FT /note="Haloalkane dehalogenase" FT /id="PRO_0000216775" 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" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 20..28 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 30..32 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 45..48 FT /evidence="ECO:0007829|PDB:5FLK" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 52..55 FT /evidence="ECO:0007829|PDB:5FLK" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 81..94 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 99..105 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 106..118 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 123..130 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:3RK4" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 146..152 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 154..156 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 157..162 FT /evidence="ECO:0007829|PDB:5FLK" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:6XTC" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 183..190 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 200..208 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 216..231 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 236..243 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 249..258 FT /evidence="ECO:0007829|PDB:5FLK" FT STRAND 262..272 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 274..277 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 279..289 FT /evidence="ECO:0007829|PDB:5FLK" FT HELIX 291..293 FT /evidence="ECO:0007829|PDB:5FLK" 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 //