ID   ISPD_MENPI              Reviewed;         265 AA.
AC   Q5C9I9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=(-)-isopiperitenol/(-)-carveol dehydrogenase, mitochondrial;
DE            EC=1.1.1.223;
DE            EC=1.1.1.243;
DE   Flags: Precursor;
OS   Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Menthinae;
OC   Mentha.
OX   NCBI_TaxID=34256;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   TISSUE=Oil gland;
RX   PubMed=15734920; DOI=10.1104/pp.104.053298;
RA   Ringer K.L., Davis E.M., Croteau R.;
RT   "Monoterpene metabolism. Cloning, expression, and characterization of (-)-
RT   isopiperitenol/(-)-carveol dehydrogenase of peppermint and spearmint.";
RL   Plant Physiol. 137:863-872(2005).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15542490; DOI=10.1104/pp.104.050229;
RA   Turner G.W., Croteau R.;
RT   "Organization of monoterpene biosynthesis in Mentha. Immunocytochemical
RT   localizations of geranyl diphosphate synthase, limonene-6-hydroxylase,
RT   isopiperitenol dehydrogenase, and pulegone reductase.";
RL   Plant Physiol. 136:4215-4227(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of menthol and related
CC       monoterpenes in leaves. Can use (-)-trans-carveol and, with a lower
CC       relative velocity, (-)-trans-isopiperitenol, (+)-neomenthol, (+)-
CC       neoisomenthol and (-)-cis-isopiperitenol as substrates, but not (-)-
CC       cis-carvenol, (-)-menthol, (+)-isomenthol, 7-hydroxy-limonene, (-)-
CC       isopiperitenone or (-)-carvone.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,6R)-isopiperitenol + NAD(+) = (6R)-isopiperitenone + H(+)
CC         + NADH; Xref=Rhea:RHEA:20860, ChEBI:CHEBI:15378, ChEBI:CHEBI:15406,
CC         ChEBI:CHEBI:15408, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.223; Evidence={ECO:0000269|PubMed:15734920};
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:15734920};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.8 uM for (-)-trans-carveol (at pH 7.5)
CC         {ECO:0000269|PubMed:15734920};
CC         KM=72 uM for (-)-trans-isopiperitenol (at pH 7.5)
CC         {ECO:0000269|PubMed:15734920};
CC         KM=410 uM for NAD(+) (at pH 7.5) {ECO:0000269|PubMed:15734920};
CC         Note=kcat is 0.02 sec(-1) with (-)-trans-carveol as substrate (at pH
CC         7.5), kcat is 0.06 sec(-1) with (-)-trans-carveol as substrate (at pH
CC         10), kcat is 0.002 sec(-1) with (-)-trans-isopiperitenol as substrate
CC         (at pH 7.5).;
CC       pH dependence:
CC         Optimum pH is 10. {ECO:0000269|PubMed:15734920};
CC   -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000305|PubMed:15734920}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15542490}.
CC   -!- TISSUE SPECIFICITY: Peltate glandular trichomes.
CC   -!- MISCELLANEOUS: Can use both NAD(+) or NADP(+) as cofactor.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AY641428; AAU20370.1; -; mRNA.
DR   AlphaFoldDB; Q5C9I9; -.
DR   SMR; Q5C9I9; -.
DR   KEGG; ag:AAU20370; -.
DR   BRENDA; 1.1.1.223; 3222.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0018459; F:carveol dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0018458; F:isopiperitenol dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR   GO; GO:0031525; P:menthol biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Mitochondrion; NAD; NADP; Oxidoreductase; Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..265
FT                   /note="(-)-isopiperitenol/(-)-carveol dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000418415"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   265 AA;  27191 MW;  8BE61C0865A5BA75 CRC64;
     MASVKKLAGK VAIVTGGASG IGEVTARLFA ERGARAVVIA DMQPEKGGTV AESIGGRRCS
     YVHCDITDEQ QVRSVVDWTA ATYGGVDVMF CNAGTASATA QTVLDLDLAQ FDRVMRVNAR
     GTAACVKQAA RKMVELGRGG AIICTASATV HHAGPNLTDY IMSKCGVLGL VRSASLQLGV
     HGIRVNSVSP TALATPLTAT IGLRTAADVE SFYGQVTSLK GVAITAEHVA EAVAFLASDE
     AAFVTGHDLA VDGGLQCLPF VAVAK