LIMA_RHOER
ID LIMA_RHOER Reviewed; 149 AA.
AC Q9ZAG3;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Limonene-1,2-epoxide hydrolase;
DE EC=3.3.2.8;
GN Name=limA;
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DCL 14;
RX PubMed=9827564; DOI=10.1016/s0014-5793(98)01322-2;
RA Barbirato F., Verdoes J.C., de Bont J.A.M., van der Werf M.J.;
RT "The Rhodococcus erythropolis DCL14 limonene-1,2-epoxide hydrolase gene
RT encodes an enzyme belonging to a novel class of epoxide hydrolases.";
RL FEBS Lett. 438:293-296(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DCL 14;
RA Van der Vlugt-Bergmans C.J.B., van der Werf M.J.;
RT "Genetic analysis of the lim operon of Rhodococcus erythropolis DCL14.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-51, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=9748436; DOI=10.1128/jb.180.19.5052-5057.1998;
RA van der Werf M.J., Overkamp K.M., de Bont J.A.M.;
RT "Limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14 belongs
RT to a novel class of epoxide hydrolases.";
RL J. Bacteriol. 180:5052-5057(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH INHIBITOR,
RP MUTAGENESIS OF TYR-53; ASN-55; ARG-99; ASP-101 AND ASP-132, AND PUTATIVE
RP REACTION MECHANISM.
RX PubMed=12773375; DOI=10.1093/emboj/cdg275;
RA Arand M., Hallberg B.M., Zou J., Bergfors T., Oesch F., van der Werf M.J.,
RA de Bont J.A., Jones T.A., Mowbray S.L.;
RT "Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase
RT reveals a novel active site.";
RL EMBO J. 22:2583-2592(2003).
CC -!- FUNCTION: Catalyzes the conversion of limonene-1,2-epoxide to limonene-
CC 1,2-diol. Can use both the (-) and (+) isomers of limonene-1,2-epoxide
CC as substrates and also has some activity with 1-methylcyclohexene
CC oxide, cyclohexene oxide and indene oxide as substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + limonene 1,2-epoxide = limonene-1,2-diol;
CC Xref=Rhea:RHEA:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:16431,
CC ChEBI:CHEBI:17219; EC=3.3.2.8; Evidence={ECO:0000269|PubMed:9748436};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:9748436};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:9748436};
CC -!- PATHWAY: Terpene metabolism; (4R)-limonene degradation; (1S,4R)-1-
CC hydroxylimonen-2-one from (4R)-limonene: step 2/3.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12773375,
CC ECO:0000269|PubMed:9748436}.
CC -!- INDUCTION: By growth on monoterpenes.
CC -!- SIMILARITY: Belongs to the limonene-1,2-epoxide hydrolase family.
CC {ECO:0000305}.
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DR EMBL; Y18005; CAA77012.1; -; Genomic_DNA.
DR EMBL; AJ272366; CAC20854.1; -; Genomic_DNA.
DR PDB; 1NU3; X-ray; 1.75 A; A/B=1-149.
DR PDB; 1NWW; X-ray; 1.20 A; A/B=1-149.
DR PDB; 4R9K; X-ray; 1.50 A; A/B/C=3-149.
DR PDB; 4R9L; X-ray; 1.80 A; A/B/C=3-149.
DR PDB; 4XBT; X-ray; 1.70 A; A/B/C/D=2-149.
DR PDB; 4XBX; X-ray; 1.53 A; A/B/C/D=2-149.
DR PDB; 4XBY; X-ray; 2.30 A; A/B/C/D/E/F/G/H=5-149.
DR PDB; 4XDV; X-ray; 2.25 A; A/B/C/D/E/F/G/H=5-149.
DR PDB; 4XDW; X-ray; 2.05 A; A/B/C/D/E/F/G/H=5-149.
DR PDB; 5CF1; X-ray; 2.24 A; A/B/C/D/E/F/G/H=2-149.
DR PDB; 5CF2; X-ray; 3.00 A; A/B/C/D=2-149.
DR PDB; 5CK6; X-ray; 2.50 A; A/B=2-149.
DR PDB; 5CLK; X-ray; 2.70 A; A/B=2-149.
DR PDB; 5GKW; X-ray; 2.01 A; A/B=2-149.
DR PDB; 5JPP; X-ray; 2.50 A; A/B=2-149.
DR PDB; 5JPU; X-ray; 1.50 A; A/B=2-149.
DR PDB; 5YAO; X-ray; 2.61 A; A/B=2-149.
DR PDB; 5YNG; X-ray; 2.50 A; A/B=2-149.
DR PDB; 5YQT; X-ray; 2.30 A; A/B/C/D/E/F/G/H=5-149.
DR PDBsum; 1NU3; -.
DR PDBsum; 1NWW; -.
DR PDBsum; 4R9K; -.
DR PDBsum; 4R9L; -.
DR PDBsum; 4XBT; -.
DR PDBsum; 4XBX; -.
DR PDBsum; 4XBY; -.
DR PDBsum; 4XDV; -.
DR PDBsum; 4XDW; -.
DR PDBsum; 5CF1; -.
DR PDBsum; 5CF2; -.
DR PDBsum; 5CK6; -.
DR PDBsum; 5CLK; -.
DR PDBsum; 5GKW; -.
DR PDBsum; 5JPP; -.
DR PDBsum; 5JPU; -.
DR PDBsum; 5YAO; -.
DR PDBsum; 5YNG; -.
DR PDBsum; 5YQT; -.
DR AlphaFoldDB; Q9ZAG3; -.
DR SMR; Q9ZAG3; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB02641; Heptanamide.
DR DrugBank; DB04165; Valpromide.
DR KEGG; ag:CAA77012; -.
DR BioCyc; MetaCyc:MON-13975; -.
DR BRENDA; 3.3.2.8; 5389.
DR SABIO-RK; Q9ZAG3; -.
DR UniPathway; UPA00987; UER00865.
DR EvolutionaryTrace; Q9ZAG3; -.
DR GO; GO:0018744; F:limonene-1,2-epoxide hydrolase activity; IEA:UniProtKB-EC.
DR InterPro; IPR013100; LEH.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR Pfam; PF07858; LEH; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9748436"
FT CHAIN 2..149
FT /note="Limonene-1,2-epoxide hydrolase"
FT /id="PRO_0000084422"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT MUTAGEN 53
FT /note="Y->F: 15% of wild-type catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:12773375"
FT MUTAGEN 55
FT /note="N->A: Almost no activity."
FT /evidence="ECO:0000269|PubMed:12773375"
FT MUTAGEN 55
FT /note="N->D: No activity."
FT /evidence="ECO:0000269|PubMed:12773375"
FT MUTAGEN 99
FT /note="R->A,H,K,Q: Impaired protein folding and no
FT activity."
FT /evidence="ECO:0000269|PubMed:12773375"
FT MUTAGEN 101
FT /note="D->A,N: No activity."
FT /evidence="ECO:0000269|PubMed:12773375"
FT MUTAGEN 132
FT /note="D->A,N: No activity."
FT /evidence="ECO:0000269|PubMed:12773375"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:5CF2"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:1NWW"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:1NWW"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1NWW"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:1NWW"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1NWW"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1NWW"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:1NWW"
FT STRAND 78..91
FT /evidence="ECO:0007829|PDB:1NWW"
FT STRAND 94..105
FT /evidence="ECO:0007829|PDB:1NWW"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1NWW"
FT STRAND 111..123
FT /evidence="ECO:0007829|PDB:1NWW"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:1NWW"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1NWW"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4R9L"
SQ SEQUENCE 149 AA; 16521 MW; 1A8602D20793A1B9 CRC64;
MTSKIEQPRW ASKDSAAGAA STPDEKIVLE FMDALTSNDA AKLIEYFAED TMYQNMPLPP
AYGRDAVEQT LAGLFTVMSI DAVETFHIGS SNGLVYTERV DVLRALPTGK SYNLSILGVF
QLTEGKITGW RDYFDLREFE EAVDLPLRG
