IPIPR_MENPI
ID IPIPR_MENPI Reviewed; 314 AA.
AC Q6WAU1; B0F4G7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=(-)-isopiperitenone reductase;
DE EC=1.3.1.82;
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, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Black Mitcham; TISSUE=Peltate glandular trichome;
RX PubMed=13679086; DOI=10.1016/s0003-9861(03)00390-4;
RA Ringer K.L., McConkey M.E., Davis E.M., Rushing G.W., Croteau R.;
RT "Monoterpene double-bond reductases of the (-)-menthol biosynthetic
RT pathway: isolation and characterization of cDNAs encoding (-)-
RT isopiperitenone reductase and (+)-pulegone reductase of peppermint.";
RL Arch. Biochem. Biophys. 418:80-92(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gupta M.K., Gupta S., Shasany A.K., Khanuja S.P.S.;
RT "Isolation of full-length genes of menthol biosynthesis pathway from Mentha
RT x piperita cv. Madhuras.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Monoterpene synthase that catalyzes the specific reduction of
CC the 1(2)-double bond of (-)-isopiperitenone to produce (+)-cis-
CC isopulegone. Does not catalyze the reverse reaction. Unable to reduce
CC (+)-pulegone, (+)-cis-isopulegone, (-)-menthone or the 1,2-double bond
CC of (-)-carvone. Able to utilize NADH with 20% the efficiency of NADPH.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,5R)-isopulegone + NADP(+) = (6R)-isopiperitenone + H(+) +
CC NADPH; Xref=Rhea:RHEA:25649, ChEBI:CHEBI:15378, ChEBI:CHEBI:15408,
CC ChEBI:CHEBI:37047, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.82;
CC Evidence={ECO:0000269|PubMed:13679086};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 uM for (-)-isopiperitenone {ECO:0000269|PubMed:13679086};
CC KM=2.2 uM for NADPH {ECO:0000269|PubMed:13679086};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:13679086};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AY300162; AAQ75422.1; -; mRNA.
DR EMBL; EU108700; ABW86884.1; -; mRNA.
DR PDB; 5L4S; X-ray; 1.41 A; A=1-314.
DR PDB; 5LCX; X-ray; 1.71 A; A=1-314.
DR PDB; 5LDG; X-ray; 1.30 A; A=1-314.
DR PDBsum; 5L4S; -.
DR PDBsum; 5LCX; -.
DR PDBsum; 5LDG; -.
DR AlphaFoldDB; Q6WAU1; -.
DR SMR; Q6WAU1; -.
DR KEGG; ag:AAQ75422; -.
DR BioCyc; MetaCyc:MON-6684; -.
DR BRENDA; 1.3.1.82; 3222.
DR UniPathway; UPA00213; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052581; F:(-)-isopiperitenone reductase activity; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0031525; P:menthol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042214; P:terpene metabolic process; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NADP; Oxidoreductase.
FT CHAIN 1..314
FT /note="(-)-isopiperitenone reductase"
FT /id="PRO_0000398336"
FT BINDING 10..33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 17
FT /note="I -> V (in Ref. 2; ABW86884)"
FT /evidence="ECO:0000305"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:5LDG"
FT TURN 226..230
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 236..255
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5LDG"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:5LDG"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:5LDG"
SQ SEQUENCE 314 AA; 34410 MW; A4170D1B149BD52A CRC64;
MAEVQRYALV TGANKGIGFE ICRQLAEKGI IVILTSRNEK RGLEARQKLL KELNVSENRL
VFHQLDVTDL ASVAAVAVFI KSKFGKLDIL VNNAGVSGVE MVGDVSVFNE YIEADFKALQ
ALEAGAKEEP PFKPKANGEM IEKFEGAKDC VVTNYYGPKR LTQALIPLLQ LSPSPRIVNV
SSSFGSLLLL WNEWAKGVLG DEDRLTEERV DEVVEVFLKD IKEGKLEESQ WPPHFAAERV
SKAALNAYTK IAAKKYPSFR INAICPGYAK TDITFHAGPL SVAEAAQVPV KLALLPDGGP
SGCFFPRDKA LALY
