ID   MLHB_RHOER              Reviewed;         297 AA.
AC   Q9EX73;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Monoterpene epsilon-lactone hydrolase {ECO:0000303|PubMed:11157238};
DE            EC=3.1.1.83 {ECO:0000269|PubMed:11157238};
GN   Name=mlhB {ECO:0000312|EMBL:CAC17806.1};
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAC17806.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-46, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=DCL 14 {ECO:0000312|EMBL:CAC17806.1};
RX   PubMed=11157238; DOI=10.1128/aem.67.2.733-741.2001;
RA   van der Vlugt-Bergmans C.J., van der Werf M.J.;
RT   "Genetic and biochemical characterization of a novel monoterpene epsilon-
RT   lactone hydrolase from Rhodococcus erythropolis DCL14.";
RL   Appl. Environ. Microbiol. 67:733-741(2001).
CC   -!- FUNCTION: Lactone hydrolase that is required for the degradation of
CC       monocyclic monoterpenes such as menthol and carvone. Catalyzes the ring
CC       opening of lactones formed during degradation of monocyclic
CC       monoterpenes. Can hydrolyze epsilon-caprolactone, the lactone
CC       derivatives of dihydrocarvone (4R)-4-isopropenyl-7-methyl-2-oxo-
CC       oxepanone and (6R)-6-isopropenyl-3-methyl-2-oxo-oxepanone, and ethyl
CC       caproate. {ECO:0000269|PubMed:11157238}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-isopropenyl-7-methyloxepan-2-one + H2O = 6-hydroxy-3-
CC         isopropenylheptanoate + H(+); Xref=Rhea:RHEA:32507,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:50238,
CC         ChEBI:CHEBI:64224; EC=3.1.1.83;
CC         Evidence={ECO:0000269|PubMed:11157238};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-isopropyl-4-methyloxepan-2-one + H2O = 6-hydroxy-3,7-
CC         dimethyloctanoate + H(+); Xref=Rhea:RHEA:32595, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:50243, ChEBI:CHEBI:64223; EC=3.1.1.83;
CC         Evidence={ECO:0000269|PubMed:11157238};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by the imidazole-modifying
CC       compound 2-bromo-4'-nitroacetophenone, by HgCl(2) and CoCl(2). Not
CC       inhibited by the thiol reagents iodoacetate and dithiothreitol.
CC       {ECO:0000269|PubMed:11157238}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:11157238};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius. Inactivated above 40
CC         degrees Celsius. {ECO:0000269|PubMed:11157238};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11157238}.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000255}.
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DR   EMBL; AJ292535; CAC17806.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9EX73; -.
DR   SMR; Q9EX73; -.
DR   ESTHER; rhoer-MLHB; Hormone-sensitive_lipase_like.
DR   KEGG; ag:CAC17806; -.
DR   BioCyc; MetaCyc:MON-13966; -.
DR   GO; GO:0046573; F:lactonohydrolase activity; IDA:CACAO.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11157238"
FT   CHAIN           2..297
FT                   /note="Monoterpene epsilon-lactone hydrolase"
FT                   /evidence="ECO:0000269|PubMed:11157238"
FT                   /id="PRO_0000402576"
FT   MOTIF           74..76
FT                   /note="Involved in the stabilization of the negatively
FT                   charged intermediate by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000250|UniProtKB:O06350"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000250|UniProtKB:O06350"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000250|UniProtKB:O06350"
SQ   SEQUENCE   297 AA;  31134 MW;  07B1617C5D6EBBEE CRC64;
     MSATDTARAK ELLASLVSMP DATIDDFRAL YEQVCATFEL PDDAQVEPVD ANGADALWVS
     APGVSADTVA VVVHGGGFTM GSAHGYRELG YRLSKSGNLR ALVVDYRLAP ESPFPAPVDD
     VVAAYRYARS LDGVENVFLV GDSAGGGIAM SALITLRDAG EQLPDAAVVL SPLVDLAGES
     PSLVDRAHLD PLPAAVLVNG MGGLYLNGLD VRHPVASPMH GDLTGLPATL VLVGTDEGLH
     DDSTRLVDKL KAADVEVQLE IGEGLPHIWP IFSFHPDAVA ATDRIGEFLR SHVAAPR