ID   C71DD_MENPI             Reviewed;         500 AA.
AC   Q9XHE7;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cytochrome P450 71D13;
DE            EC=1.14.14.99 {ECO:0000269|PubMed:10415126, ECO:0000269|PubMed:11368174};
DE   AltName: Full=(-)-(4S)-Limonene-3-hydroxylase;
DE   AltName: Full=Cytochrome P450 isoform PM17;
GN   Name=CYP71D13;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Black Mitcham;
RX   PubMed=10415126; DOI=10.1006/abbi.1999.1298;
RA   Lupien S., Karp F., Wildung M., Croteau R.;
RT   "Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha)
RT   species: cDNA isolation, characterization, and functional expression of
RT   (-)-4S-limonene-3-hydroxylase and (-)-4S-limonene-6-hydroxylase.";
RL   Arch. Biochem. Biophys. 368:181-192(1999).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11368174; DOI=10.1006/abbi.2000.2248;
RA   Wuest M., Little D.B., Schalk M., Croteau R.;
RT   "Hydroxylation of limonene enantiomers and analogs by recombinant (-)-
RT   limonene 3- and 6-hydroxylases from mint (Mentha) species: evidence for
RT   catalysis within sterically constrained active sites.";
RL   Arch. Biochem. Biophys. 387:125-136(2001).
CC   -!- FUNCTION: Hydroxylates (-)-(4S)-limonene to (-)-trans-isopiperitenol, a
CC       precursor of (-)-menthol, responsible for the cooling sensation of
CC       peppermint. {ECO:0000269|PubMed:10415126, ECO:0000269|PubMed:11368174}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4S)-limonene + O2 + reduced [NADPH--hemoprotein reductase] =
CC         (1S,6R)-isopiperitenol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:15129, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15383, ChEBI:CHEBI:15406, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.99;
CC         Evidence={ECO:0000269|PubMed:10415126, ECO:0000269|PubMed:11368174};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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; AF124816; AAD44151.1; -; mRNA.
DR   AlphaFoldDB; Q9XHE7; -.
DR   SMR; Q9XHE7; -.
DR   KEGG; ag:AAD44151; -.
DR   BioCyc; MetaCyc:MON-6762; -.
DR   BRENDA; 1.14.13.47; 3222.
DR   BRENDA; 1.14.14.99; 3222.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0018674; F:(S)-limonene 3-monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..500
FT                   /note="Cytochrome P450 71D13"
FT                   /id="PRO_0000389500"
FT   TRANSMEM        3..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   BINDING         439
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"
SQ   SEQUENCE   500 AA;  56601 MW;  402324F738F5949F CRC64;
     MELQISSAII ILVVTYTISL LIIKQWRKPK PQENLPPGPP KLPLIGHLHL LWGKLPQHAL
     ASVAKQYGPV AHVQLGEVFS VVLSSREATK EAMKLVDPAC ADRFESIGTK IMWYDNDDII
     FSPYSVHWRQ MRKICVSELL SARNVRSFGF IRQDEVSRLL GHLRSSAAAG EAVDLTERIA
     TLTCSIICRA AFGSVIRDHE ELVELVKDAL SMASGFELAD MFPSSKLLNL LCWNKSKLWR
     MRRRVDAILE AIVEEHKLKK SGEFGGEDII DVLFRMQKDS QIKVPITTNA IKAFIFDTFS
     AGTETSSTTT LWVMAELMRN PEVMAKAQAE VRAALKGKTD WDVDDVQELK YMKSVVKETM
     RMHPPIPLIP RSCREECEVN GYTIPNKARI MINVWSMGRN PLYWEKPETF WPERFDQVSR
     DFMGNDFEFI PFGAGRRICP GLNFGLANVE VPLAQLLYHF DWKLAEGMNP SDMDMSEAEG
     LTGIRKNNLL LVPTPYDPSS