ID DHLA_XANAU Reviewed; 310 AA. AC P22643; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 27-MAR-2024, entry version 121. DE RecName: Full=Haloalkane dehalogenase; DE EC=3.8.1.5; GN Name=dhlA; OS Xanthobacter autotrophicus. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Xanthobacteraceae; Xanthobacter. OX NCBI_TaxID=280; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=GJ10; RX PubMed=2687254; DOI=10.1128/jb.171.12.6791-6799.1989; RA Janssen D.B., Pries F., van der Ploeg J., Kazemier B., Terpstra P., RA Witholt B.; RT "Cloning of 1,2-dichloroethane degradation genes of Xanthobacter RT autotrophicus GJ10 and expression and sequencing of the dhlA gene."; RL J. Bacteriol. 171:6791-6799(1989). RN [2] RP PROTEIN SEQUENCE OF 1-10. RX PubMed=4019411; DOI=10.1128/jb.163.2.635-639.1985; RA Keuning S., Janssen D.B., Witholt B.; RT "Purification and characterization of hydrolytic haloalkane dehalogenase RT from Xanthobacter autotrophicus GJ10."; RL J. Bacteriol. 163:635-639(1985). RN [3] RP CRYSTALLIZATION. RC STRAIN=GJ10; RX PubMed=3398051; DOI=10.1016/0022-2836(88)90548-7; RA Rozeboom H.J., Kingma J., Janssen D.B., Dijkstra B.W.; RT "Crystallization of haloalkane dehalogenase from Xanthobacter autotrophicus RT GJ10."; RL J. Mol. Biol. 200:611-612(1988). RN [4] {ECO:0007744|PDB:2HAD} RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SEQUENCE REVISION TO 120. RC STRAIN=GJ10; RX PubMed=2026135; DOI=10.1002/j.1460-2075.1991.tb07647.x; RA Franken S.M., Rozeboom H.J., Kalk K.H., Dijkstra B.W.; RT "Crystal structure of haloalkane dehalogenase: an enzyme to detoxify RT halogenated alkanes."; RL EMBO J. 10:1297-1302(1991). RN [5] {ECO:0007744|PDB:1EDE} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=8355275; DOI=10.1006/jmbi.1993.1436; RA Verschueren K.H.G., Franken S.M., Rozeboom H.J., Kalk K.H., Dijkstra B.W.; RT "Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 RT and implications for the reaction mechanism."; RL J. Mol. Biol. 232:856-872(1993). RN [6] {ECO:0007744|PDB:2DHC, ECO:0007744|PDB:2DHD, ECO:0007744|PDB:2DHE} RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) IN COMPLEXES WITH 1,2-DICHLOROETHANE RP AND CHLORIDE. RC STRAIN=GJ10; RX PubMed=8515812; DOI=10.1038/363693a0; RA Verschueren K.H.G., Seljee F., Rozeboom H.J., Kalk K.H., Dijkstra B.W.; RT "Crystallographic analysis of the catalytic mechanism of haloalkane RT dehalogenase."; RL Nature 363:693-698(1993). RN [7] {ECO:0007744|PDB:1BE0, ECO:0007744|PDB:1BEE, ECO:0007744|PDB:1BEZ} RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS). RX PubMed=9790663; DOI=10.1021/bi9815187; RA Krooshof G.H., Ridder I.S., Tepper A.W.J.W., Vos G.J., Rozeboom H.J., RA Kalk K.H., Dijkstra B.W., Janssen D.B.; RT "Kinetic analysis and X-ray structure of haloalkane dehalogenase with a RT modified halide-binding site."; RL Biochemistry 37:15013-15023(1998). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=10508409; DOI=10.1021/bi990849w; RA Pikkemaat M.G., Ridder I.S., Rozeboom H.J., Kalk K.H., Dijkstra B.W., RA Janssen D.B.; RT "Crystallographic and kinetic evidence of a collision complex formed during RT halide import in haloalkane dehalogenase."; RL Biochemistry 38:12052-12061(1999). RN [9] {ECO:0007744|PDB:1B6G} RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH CHLORIDE. RC STRAIN=GJ10; RX PubMed=10393294; DOI=10.1107/s090744499900534x; RA Ridder I.S., Rozeboom H.J., Dijkstra B.W.; RT "Haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 refined at RT 1.15 A resolution."; RL Acta Crystallogr. D 55:1273-1290(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 terminally mono- and CC di- chlorinated and brominated alkanes (up to C4 only). The highest CC activity was found with 1,2-dichloroethane, 1,3-dichloropropane, and CC 1,2-dibromoethane. 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 -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dichloroethane + H2O = 2-chloroethanol + chloride + H(+); CC Xref=Rhea:RHEA:25185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17996, ChEBI:CHEBI:27789, ChEBI:CHEBI:28200; EC=3.8.1.5; CC -!- ACTIVITY REGULATION: Inhibited by thiol reagents such as p- CC chloromercuribenzoate and iodoacetamide. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.2.; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius.; CC -!- PATHWAY: Xenobiotic degradation; 1,2-dichloroethane degradation; CC glycolate from 1,2-dichloroethane: step 1/4. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 1 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; M26950; AAA88691.1; -; Genomic_DNA. DR PIR; B43718; B43718. DR PDB; 1B6G; X-ray; 1.15 A; A=3-310. DR PDB; 1BE0; X-ray; 1.96 A; A=3-310. DR PDB; 1BEE; X-ray; 2.60 A; A=3-310. DR PDB; 1BEZ; X-ray; 2.10 A; A=3-310. DR PDB; 1CIJ; X-ray; 2.30 A; A=3-310. DR PDB; 1EDB; X-ray; 2.01 A; A=1-310. DR PDB; 1EDD; X-ray; 2.19 A; A=1-310. DR PDB; 1EDE; X-ray; 1.90 A; A=1-310. DR PDB; 1HDE; X-ray; 2.70 A; A/B=1-310. DR PDB; 2DHC; X-ray; 2.30 A; A=1-310. DR PDB; 2DHD; X-ray; 2.13 A; A=1-310. DR PDB; 2DHE; X-ray; 2.13 A; A=1-310. DR PDB; 2EDA; X-ray; 2.19 A; A=1-310. DR PDB; 2EDC; X-ray; 2.30 A; A=1-310. DR PDB; 2HAD; X-ray; 1.90 A; A=1-310. DR PDB; 2PKY; X-ray; 1.55 A; X=1-310. DR PDB; 2YXP; X-ray; 1.53 A; X=1-310. DR PDBsum; 1B6G; -. DR PDBsum; 1BE0; -. DR PDBsum; 1BEE; -. DR PDBsum; 1BEZ; -. DR PDBsum; 1CIJ; -. DR PDBsum; 1EDB; -. DR PDBsum; 1EDD; -. DR PDBsum; 1EDE; -. DR PDBsum; 1HDE; -. DR PDBsum; 2DHC; -. DR PDBsum; 2DHD; -. DR PDBsum; 2DHE; -. DR PDBsum; 2EDA; -. DR PDBsum; 2EDC; -. DR PDBsum; 2HAD; -. DR PDBsum; 2PKY; -. DR PDBsum; 2YXP; -. DR AlphaFoldDB; P22643; -. DR SMR; P22643; -. DR ESTHER; xanau-halo1; Haloalkane_dehalogenase-HLD1. DR MEROPS; S33.990; -. DR KEGG; ag:AAA88691; -. DR BioCyc; MetaCyc:DHLAXANAU-MONOMER; -. DR BRENDA; 3.8.1.5; 1641. DR UniPathway; UPA00265; UER00387. DR EvolutionaryTrace; P22643; -. DR GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019260; P:1,2-dichloroethane catabolic process; IEA:UniProtKB-UniPathway. 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_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 PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1. DR PANTHER; PTHR43329:SF74; HALOALKANE DEHALOGENASE; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PRINTS; PR00111; ABHYDROLASE. DR PRINTS; PR00412; EPOXHYDRLASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure; Detoxification; Direct protein sequencing; Hydrolase. FT CHAIN 1..310 FT /note="Haloalkane dehalogenase" FT /id="PRO_0000216771" FT DOMAIN 49..295 FT /note="AB hydrolase-1" FT /evidence="ECO:0000255" FT ACT_SITE 124 FT /note="Nucleophile" FT ACT_SITE 260 FT /note="Proton donor" FT ACT_SITE 289 FT /note="Proton acceptor" FT BINDING 125 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000269|PubMed:10393294, FT ECO:0000269|PubMed:8515812" FT BINDING 175 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000269|PubMed:10393294, FT ECO:0000269|PubMed:8515812, ECO:0007744|PDB:2DHD, FT ECO:0007744|PDB:2DHE" FT HELIX 9..12 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 23..27 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 35..42 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 60..63 FT /evidence="ECO:0007829|PDB:1B6G" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 67..72 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 99..113 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 117..122 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 125..130 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 141..148 FT /evidence="ECO:0007829|PDB:1B6G" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 160..163 FT /evidence="ECO:0007829|PDB:1B6G" FT TURN 164..166 FT /evidence="ECO:0007829|PDB:1B6G" FT TURN 169..171 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 172..180 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 187..194 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 200..207 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 217..227 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 231..246 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 250..257 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 265..274 FT /evidence="ECO:0007829|PDB:1B6G" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 291..294 FT /evidence="ECO:0007829|PDB:1B6G" FT HELIX 295..308 FT /evidence="ECO:0007829|PDB:1B6G" SQ SEQUENCE 310 AA; 35144 MW; FB32C94BE5D8940C CRC64; MINAIRTPDQ RFSNLDQYPF SPNYLDDLPG YPGLRAHYLD EGNSDAEDVF LCLHGEPTWS YLYRKMIPVF AESGARVIAP DFFGFGKSDK PVDEEDYTFE FHRNFLLALI ERLDLRNITL VVQDWGGFLG LTLPMADPSR FKRLIIMNAC LMTDPVTQPA FSAFVTQPAD GFTAWKYDLV TPSDLRLDQF MKRWAPTLTE AEASAYAAPF PDTSYQAGVR KFPKMVAQRD QACIDISTEA ISFWQNDWNG QTFMAIGMKD KLLGPDVMYP MKALINGCPE PLEIADAGHF VQEFGEQVAR EALKHFAETE //