MFS_MENPI
ID MFS_MENPI Reviewed; 493 AA.
AC Q947B7; B0F4H0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=(+)-menthofuran synthase;
DE EC=1.14.14.143 {ECO:0000269|PubMed:11396930};
DE AltName: Full=(+)-pulegone 9-hydroxylase;
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], AND CATALYTIC ACTIVITY.
RC TISSUE=Peltate glandular trichome;
RX PubMed=11396930; DOI=10.1006/abbi.2001.2378;
RA Bertea C.M., Schalk M., Karp F., Maffei M., Croteau R.;
RT "Demonstration that menthofuran synthase of mint (Mentha) is a cytochrome
RT P450 monooxygenase: cloning, functional expression, and characterization of
RT the responsible gene.";
RL Arch. Biochem. Biophys. 390:279-286(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Madhuras;
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.
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=14623962; DOI=10.1073/pnas.2436325100;
RA Mahmoud S.S., Croteau R.B.;
RT "Menthofuran regulates essential oil biosynthesis in peppermint by
RT controlling a downstream monoterpene reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14481-14486(2003).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the formation of (+)-
CC menthofuran from (+)-pulegone.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pulegone + O2 + reduced [NADPH--hemoprotein reductase] =
CC (R)-menthofuran + H(+) + 2 H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:25658, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:6750, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:35596, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.143;
CC Evidence={ECO:0000269|PubMed:11396930};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Co-suppression of menthofuran synthase leads to a
CC decrease of pulegone level and an increase of piperitone and
CC piperitenone levels due to an increased pulegone reductase activity.
CC {ECO:0000269|PubMed:14623962}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF346833; AAL06397.1; -; mRNA.
DR EMBL; EU108704; ABW86888.1; -; mRNA.
DR EMBL; EU108703; ABW86887.1; -; Genomic_DNA.
DR AlphaFoldDB; Q947B7; -.
DR SMR; Q947B7; -.
DR KEGG; ag:AAL06397; -.
DR BioCyc; MetaCyc:MON-6783; -.
DR BRENDA; 1.14.13.104; 3222.
DR BRENDA; 1.14.14.143; 3222.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0052582; F:(+)-menthofuran synthase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006721; P:terpenoid metabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..493
FT /note="(+)-menthofuran synthase"
FT /id="PRO_0000398335"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..19
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 20..493
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 434
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 268
FT /note="L -> P (in Ref. 2; ABW86887)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="K -> R (in Ref. 2; ABW86887)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="E -> G (in Ref. 2; ABW86887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 55360 MW; 052E1D55523B4CFA CRC64;
MAALLVFFSV SLILLAVLFH KRKSSLSSRK RPPPSPLRLP VIGHFHLIGA LSHRSFTSLS
KRYGEVMLLH FGSAPVLVAS SAAAAREIMK NQDVIFASRP RLSIFDRLMY SGKGVAFAPY
GEHWRNARSM CMLQLLSAKR VQSFGGIREE ETSAMIEKIR RSKPTTVVNL SEMFMALTNG
VIHRAVLGRK GDGGDDFNRI LIKVIKLLGS FNVGDYVPWL SWINRINGVD AEVEKVGTKL
DGSMEGILRK YRRKKVGDDE TNFVDTLLQF QRESKDTDPV EDDVIKALIF DMVSAGTDTT
FAALEWTMAE LIKNPRTLKT LQNEVREVSR NKGGITEDDV DKMPYLKAVS KEILRLHPPF
AILLPRELTQ DANMLGYDIP RGTVVLVNNW AISRDPSLWE NPEEFRPERF LETSIDYKGL
HFEMLPFGSG RRGCPGSTFA MALYELALSK LVNEFDFRLG NGDRAEDLDM TEAPGFVVHK
KSPLLVLATP RQS
