DHLA_XANAU
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 03-AUG-2022, entry version 116.
DE RecName: Full=Haloalkane dehalogenase;
DE EC=3.8.1.5;
GN Name=dhlA;
OS Xanthobacter autotrophicus.
OC Bacteria; Proteobacteria; 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}.
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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-MON; -.
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; -; 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; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 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
