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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
 
 
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