DHAA_RHOSO
ID DHAA_RHOSO Reviewed; 293 AA.
AC P0A3G3; Q53042;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Haloalkane dehalogenase;
DE EC=3.8.1.5;
GN Name=dhaA;
OS Rhodococcus sp.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=1831;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF CYS-176 AND TYR-273.
RC STRAIN=m15-3;
RX PubMed=12089046; DOI=10.1128/aem.68.7.3582-3587.2002;
RA Bosma T., Damborsky J., Stucki G., Janssen D.B.;
RT "Biodegradation of 1,2,3-trichloropropane through directed evolution and
RT heterologous expression of a haloalkane dehalogenase gene.";
RL Appl. Environ. Microbiol. 68:3582-3587(2002).
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.
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. {ECO:0000250}.
CC -!- BIOTECHNOLOGY: The recombinant strain obtained by expression of the
CC Tyr-176/Phe-273 mutant in the 2,3-dichloro-1-propanol-utilizing
CC bacterium Agrobacterium radiobacter AD1 is able to utilize the
CC environmental pollutant 1,2,3-trichloropropane (TCP) as the sole carbon
CC and energy source.
CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC subfamily. {ECO:0000305}.
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DR PDB; 3FWH; X-ray; 1.22 A; A=1-293.
DR PDB; 3G9X; X-ray; 0.95 A; A=1-293.
DR PDB; 4HZG; X-ray; 1.95 A; A=1-293.
DR PDB; 4KAA; X-ray; 2.28 A; A/B=2-291.
DR PDB; 4KAC; X-ray; 2.22 A; A/B=2-291.
DR PDB; 4KAF; X-ray; 1.50 A; A/B=3-293.
DR PDB; 4KAJ; X-ray; 1.95 A; A=3-293.
DR PDB; 5Y2X; X-ray; 2.02 A; A=2-293.
DR PDB; 5Y2Y; X-ray; 2.27 A; A/B=2-293.
DR PDB; 6Y7A; X-ray; 1.40 A; A=4-293.
DR PDB; 6Y7B; X-ray; 3.10 A; A/B/C/D/E=4-293.
DR PDB; 6ZCC; X-ray; 1.52 A; A=4-293.
DR PDB; 6ZVU; X-ray; 1.40 A; A=4-293.
DR PDB; 6ZVV; X-ray; 1.40 A; A/B/C/D=4-293.
DR PDB; 6ZVW; X-ray; 1.60 A; A/B=4-293.
DR PDB; 6ZVX; X-ray; 1.40 A; A=4-293.
DR PDB; 6ZVY; X-ray; 1.40 A; A/B=4-293.
DR PDB; 7PCW; X-ray; 2.30 A; A/B/C/D=4-293.
DR PDB; 7PCX; X-ray; 1.40 A; A/B/C/D/E/F=4-293.
DR PDB; 7WAM; X-ray; 1.49 A; A=2-293.
DR PDB; 7WAN; X-ray; 2.28 A; A=2-293.
DR PDBsum; 3FWH; -.
DR PDBsum; 3G9X; -.
DR PDBsum; 4HZG; -.
DR PDBsum; 4KAA; -.
DR PDBsum; 4KAC; -.
DR PDBsum; 4KAF; -.
DR PDBsum; 4KAJ; -.
DR PDBsum; 5Y2X; -.
DR PDBsum; 5Y2Y; -.
DR PDBsum; 6Y7A; -.
DR PDBsum; 6Y7B; -.
DR PDBsum; 6ZCC; -.
DR PDBsum; 6ZVU; -.
DR PDBsum; 6ZVV; -.
DR PDBsum; 6ZVW; -.
DR PDBsum; 6ZVX; -.
DR PDBsum; 6ZVY; -.
DR PDBsum; 7PCW; -.
DR PDBsum; 7PCX; -.
DR PDBsum; 7WAM; -.
DR PDBsum; 7WAN; -.
DR AlphaFoldDB; P0A3G3; -.
DR SMR; P0A3G3; -.
DR ESTHER; rhoso-halo1; Haloalkane_dehalogenase-HLD2.
DR BRENDA; 3.8.1.5; 5397.
DR UniPathway; UPA00007; -.
DR EvolutionaryTrace; P0A3G3; -.
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; -; 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 Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Detoxification; Hydrolase.
FT CHAIN 1..293
FT /note="Haloalkane dehalogenase"
FT /id="PRO_0000216776"
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 MUTAGEN 176
FT /note="C->Y: 3-fold increase in catalytic efficiency for
FT TCP dehalogenation. 8-fold increase in catalytic efficiency
FT for TCP dehalogenation; when associated with F-273."
FT /evidence="ECO:0000269|PubMed:12089046"
FT MUTAGEN 273
FT /note="Y->F: 8-fold increase in catalytic efficiency for
FT TCP dehalogenation; when associated with Y-176."
FT /evidence="ECO:0000269|PubMed:12089046"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:3G9X"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:3G9X"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4HZG"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 216..231
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:3G9X"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:3G9X"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3G9X"
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
