ID   LIHY_GEOSE              Reviewed;         543 AA.
AC   O85057;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Limonene hydroxylase;
DE   AltName: Full=(S)-limonene 6-monooxygenase;
DE            EC=1.14.14.51 {ECO:0000269|PubMed:10849845};
DE   AltName: Full=(S)-limonene 7-monooxygenase;
DE            EC=1.14.14.52 {ECO:0000269|PubMed:10849845};
DE   AltName: Full=Carveol dehydrogenase;
DE            EC=1.1.1.243 {ECO:0000269|PubMed:10849845};
DE   AltName: Full=Perillyl-alcohol dehydrogenase;
DE            EC=1.1.1.144 {ECO:0000269|PubMed:10849845};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=BR388;
RX   PubMed=10849845; DOI=10.1385/abab:84-86:1-9:903;
RA   Cheong T.K., Oriel P.J.;
RT   "Cloning and expression of the limonene hydroxylase of Bacillus
RT   stearothermophilus BR388 and utilization in two-phase limonene
RT   conversions.";
RL   Appl. Biochem. Biotechnol. 84:903-915(2000).
CC   -!- FUNCTION: Involved in limonene hydroxylation to a mixture of carveol
CC       and perillyl alcohol as well as in dehydrogenation of these products to
CC       carvone and perillyl aldehyde. Aromatic alcohols containing an
CC       isopropyl or isopropenyl group at ring position 4 also served as
CC       substrates for the dehydrogenase activity.
CC       {ECO:0000269|PubMed:10849845}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4S)-limonene + O2 + reduced [NADPH--hemoprotein reductase] =
CC         (1S,5R)-carveol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17945, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15383, ChEBI:CHEBI:15389, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.51;
CC         Evidence={ECO:0000269|PubMed:10849845};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4S)-limonene + O2 + reduced [NADPH--hemoprotein reductase] =
CC         (4S)-perillyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:23432, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:10782, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15383, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.52;
CC         Evidence={ECO:0000269|PubMed:10849845};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + perillyl alcohol = H(+) + NADH + perillyl aldehyde;
CC         Xref=Rhea:RHEA:10664, ChEBI:CHEBI:15378, ChEBI:CHEBI:15420,
CC         ChEBI:CHEBI:15421, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.144; Evidence={ECO:0000269|PubMed:10849845};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,5R)-carveol + NADP(+) = (R)-carvone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:13629, ChEBI:CHEBI:15378, ChEBI:CHEBI:15389,
CC         ChEBI:CHEBI:15400, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.243; Evidence={ECO:0000269|PubMed:10849845};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.7. {ECO:0000269|PubMed:10849845};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:10849845};
CC   -!- MISCELLANEOUS: Oxygen, FAD, and NADH stimulate the hydroxylation
CC       reaction, while NAD(+) stimulates the dehydrogenase reaction.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF039527; AAC25032.1; -; Genomic_DNA.
DR   AlphaFoldDB; O85057; -.
DR   SMR; O85057; -.
DR   KEGG; ag:AAC25032; -.
DR   BioCyc; MetaCyc:MON-15696; -.
DR   BRENDA; 1.14.14.51; 623.
DR   GO; GO:0018675; F:(S)-limonene 6-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018676; F:(S)-limonene 7-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0018459; F:carveol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018457; F:perillyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; FAD; Flavoprotein; NAD; NADP; Nucleotide-binding;
KW   Oxidoreductase; Transcription; Transcription regulation.
FT   CHAIN           1..543
FT                   /note="Limonene hydroxylase"
FT                   /id="PRO_0000389504"
FT   DOMAIN          232..464
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         260..267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         324..333
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
SQ   SEQUENCE   543 AA;  61569 MW;  FC7A0863239D4A44 CRC64;
     MGSKYAAGHY SCSSYFQSLD IPENRQFVQG MKKRYGQDTV ISSVMANTYS GIQMILEAIV
     HLRSTDRKKI LNYLYNKTFP SPSGNITIES NHHLSREVRI GQANLDGQFD IVWSSEQPIP
     AKPLMTNTII DSANEEQIWK YVVESMGEET ADGVLVLDQD QTILYANSAA YSFLRVKQGD
     ILKEEQLREI SHQLIKKETS KYGVQLFIFK RAKRGPLLVT KPDKEPYRFG RVVTYNPSFE
     KELRTASIAS QSDANVLILG ETGSGKEVLA RTIHEQSPRR NGPFVALNAG AIPRELIASE
     LFGYVEGAFT GARKGGRPGK FEVADGGTLF LDEIGDMPLE LQVNLLRVLE ERKVIRIGDH
     KERPINVRVI AATNRNLKEE IAYRGSFRSD LYYRLNVFTI HIPPLRDRKE DIETLSLQFL
     KNFHQHYCGK GTCHLSNSAL QLLQSYNWPG NIRELRNVIE RAFLLAIDEP EILPIHLPEE
     IQNANCAIPP SSVNNLKDVE KKMIEQALKE SKSLTEAAKK LGITRSTLYR KIKQWKIHKT
     TFS