ID DHAA_RHOSD Reviewed; 294 AA. AC P59336; DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 22-FEB-2003, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Haloalkane dehalogenase; DE EC=3.8.1.5; GN Name=dhaA; OS Rhodococcus sp. (strain TDTM0003). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=269091; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.5 RP ANGSTROMS) IN COMPLEX WITH IODIDE. RX PubMed=10587433; DOI=10.1021/bi9913855; RA Newman J., Peat T.S., Richard R., Kan L., Swanson P.E., Affholter J.A., RA Holmes I.H., Schindler J.F., Unkefer C.J., Terwilliger T.C.; RT "Haloalkane dehalogenases: structure of a Rhodococcus enzyme."; RL Biochemistry 38:16105-16114(1999). 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, which includes primary, secondary and cyclic CC haloalkanes (chain length > C4). 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 -!- SUBUNIT: Monomer. {ECO:0000250}. 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 PDB; 1BN6; X-ray; 1.50 A; A=1-293. DR PDB; 1BN7; X-ray; 1.50 A; A=1-293. DR PDB; 1CQW; X-ray; 1.50 A; A=4-293. DR PDBsum; 1BN6; -. DR PDBsum; 1BN7; -. DR PDBsum; 1CQW; -. DR AlphaFoldDB; P59336; -. DR PCDDB; P59336; -. DR SMR; P59336; -. DR ESTHER; rhoso-halo1; Haloalkane_dehalogenase-HLD2. DR EvolutionaryTrace; P59336; -. DR GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule. 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; Hydrolase. FT CHAIN 1..294 FT /note="Haloalkane dehalogenase" FT /id="PRO_0000216777" FT DOMAIN 34..158 FT /note="AB hydrolase-1" FT /evidence="ECO:0000255" FT ACT_SITE 106 FT /note="Nucleophile" FT ACT_SITE 130 FT /note="Proton donor" FT ACT_SITE 272 FT /note="Proton acceptor" FT BINDING 41 FT /ligand="iodide" FT /ligand_id="ChEBI:CHEBI:16382" FT /evidence="ECO:0000269|PubMed:10587433" FT BINDING 107 FT /ligand="iodide" FT /ligand_id="ChEBI:CHEBI:16382" FT /evidence="ECO:0000269|PubMed:10587433" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 20..28 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 30..33 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 45..48 FT /evidence="ECO:0007829|PDB:1BN6" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 52..55 FT /evidence="ECO:0007829|PDB:1BN6" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 81..94 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 99..105 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 107..118 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 123..130 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 143..152 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 157..162 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 183..190 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 200..208 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 216..231 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 236..243 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 249..258 FT /evidence="ECO:0007829|PDB:1BN6" FT STRAND 262..272 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 279..289 FT /evidence="ECO:0007829|PDB:1BN6" FT HELIX 290..293 FT /evidence="ECO:0007829|PDB:1BN6" SQ SEQUENCE 294 AA; 33331 MW; 190E6B9944E5DBEF CRC64; MSEIGTGFPF DPHYVEVLGE RMHYVDVGPR DGTPVLFLHG NPTSSYLWRN IIPHVAPSHR CIAPDLIGMG KSDKPDLDYF FDDHVRYLDA FIEALGLEEV VLVIHDWGSA LGFHWAKRNP ERVKGIACME FIRPIPTWDE WPEFARETFQ AFRTADVGRE LIIDQNAFIE GVLPKCVVRP LTEVEMDHYR EPFLKPVDRE PLWRFPNEIP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW GTPGVLIPPA EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PGLA //