DHAA_RHOSD
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 03-AUG-2022, entry version 72.
DE RecName: Full=Haloalkane dehalogenase;
DE EC=3.8.1.5;
GN Name=dhaA;
OS Rhodococcus sp. (strain TDTM0003).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; 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}.
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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; -; 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; 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
