C71DI_MENSP
ID C71DI_MENSP Reviewed; 496 AA.
AC Q9XHE8;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cytochrome P450 71D18;
DE EC=1.14.14.51 {ECO:0000269|PubMed:10415126, ECO:0000269|PubMed:11368174};
DE AltName: Full=(-)-(4S)-Limonene-6-hydroxylase;
GN Name=CYP71D18;
OS Mentha spicata (Spearmint).
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=29719;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-21; 176-200 AND 375-398,
RP CATALYTIC ACTIVITY, AND FUNCTION.
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 MUTAGENESIS OF LEU-357; LEU-359; PHE-363; GLN-369 AND SER-370.
RX PubMed=11050228; DOI=10.1073/pnas.97.22.11948;
RA Schalk M., Croteau R.;
RT "A single amino acid substitution (F363I) converts the regiochemistry of
RT the spearmint (-)-limonene hydroxylase from a C6- to a C3-hydroxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11948-11953(2000).
RN [3]
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-carveol, a
CC precursor of (-)-carvone, responsible for the typical spearmint flavor
CC note. Fluorinated substrate analogs are hydroxylated with the same
CC regio- and stereochemistry. {ECO:0000269|PubMed:10415126,
CC ECO:0000269|PubMed:11368174}.
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: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 -!- WEB RESOURCE: Name=Protein Spotlight; Note=Mint condition - Issue 113
CC of January 2010;
CC URL="https://web.expasy.org/spotlight/back_issues/113";
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DR EMBL; AF124815; AAD44150.1; -; mRNA.
DR AlphaFoldDB; Q9XHE8; -.
DR SMR; Q9XHE8; -.
DR KEGG; ag:AAD44150; -.
DR BioCyc; MetaCyc:MON-15424; -.
DR BRENDA; 1.14.14.51; 3225.
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:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0018675; F:(S)-limonene 6-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 Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..496
FT /note="Cytochrome P450 71D18"
FT /id="PRO_0000389497"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 436
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 MUTAGEN 357
FT /note="L->M: No effect on regiospecificity."
FT /evidence="ECO:0000269|PubMed:11050228"
FT MUTAGEN 359
FT /note="L->M: No effect on regiospecificity."
FT /evidence="ECO:0000269|PubMed:11050228"
FT MUTAGEN 363
FT /note="F->I: Conversion to the regiospecificity and
FT catalytic efficiency of the peppermint limonene-3-
FT hydroxylase."
FT /evidence="ECO:0000269|PubMed:11050228"
FT MUTAGEN 369
FT /note="Q->S: No effect on regiospecificity."
FT /evidence="ECO:0000269|PubMed:11050228"
FT MUTAGEN 370
FT /note="S->C: No effect on regiospecificity."
FT /evidence="ECO:0000269|PubMed:11050228"
SQ SEQUENCE 496 AA; 56149 MW; 06E4370F95EB91C0 CRC64;
MELDLLSAII ILVATYIVSL LINQWRKSKS QQNLPPSPPK LPVIGHLHFL WGGLPQHVFR
SIAQKYGPVA HVQLGEVYSV VLSSAEAAKQ AMKVLDPNFA DRFDGIGSRT MWYDKDDIIF
SPYNDHWRQM RRICVTELLS PKNVRSFGYI RQEEIERLIR LLGSSGGAPV DVTEEVSKMS
CVVVCRAAFG SVLKDQGSLA ELVKESLALA SGFELADLYP SSWLLNLLSL NKYRLQRMRR
RLDHILDGFL EEHREKKSGE FGGEDIVDVL FRMQKGSDIK IPITSNCIKG FIFDTFSAGA
ETSSTTISWA LSELMRNPAK MAKVQAEVRE ALKGKTVVDL SEVQELKYLR SVLKETLRLH
PPFPLIPRQS REECEVNGYT IPAKTRIFIN VWAIGRDPQY WEDPDTFRPE RFDEVSRDFM
GNDFEFIPFG AGRRICPGLH FGLANVEIPL AQLLYHFDWK LPQGMTDADL DMTETPGLSG
PKKKNVCLVP TLYKSP
