C71DF_MENPI
ID C71DF_MENPI Reviewed; 498 AA.
AC Q9XHE6;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cytochrome P450 71D15;
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 PM2;
GN Name=CYP71D15;
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 NUCLEOTIDE SEQUENCE [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 MUTAGENESIS OF MET-358; MET-360; ILE-364; SER-370 AND CYS-371.
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 [4]
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. Fluorinated substrate analogs are hydroxylated with the
CC same 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,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 -!- 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; AF124817; AAD44152.1; -; mRNA.
DR EMBL; EU108698; ABW86882.1; -; mRNA.
DR AlphaFoldDB; Q9XHE6; -.
DR SMR; Q9XHE6; -.
DR KEGG; ag:AAD44152; -.
DR BioCyc; MetaCyc:MON-6761; -.
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..498
FT /note="Cytochrome P450 71D15"
FT /id="PRO_0000389499"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 437
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 358
FT /note="M->L: No effect on activity or regiospecificity."
FT /evidence="ECO:0000269|PubMed:11050228"
FT MUTAGEN 360
FT /note="M->L: Strong decrease of activity."
FT /evidence="ECO:0000269|PubMed:11050228"
FT MUTAGEN 364
FT /note="I->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11050228"
FT MUTAGEN 370
FT /note="S->Q: No effect on activity or regiospecificity."
FT /evidence="ECO:0000269|PubMed:11050228"
FT MUTAGEN 371
FT /note="C->S: No effect on activity or regiospecificity."
FT /evidence="ECO:0000269|PubMed:11050228"
SQ SEQUENCE 498 AA; 56532 MW; D78DDC2CD5C7EA48 CRC64;
MELLQLWSAL IILVVTYTIS LLINQWRKPK PQGKFPPGPP KLPLIGHLHL LWGKLPQHAL
ASVAKEYGPV AHVQLGEVFS VVLSSREATK EAMKLVDPAC ANRFESIGTR IMWYDNEDII
FSPYSEHWRQ MRKICVSELL SSRNVRSFGF IRQDEVSRLL RHLRSSAGAA VDMTERIETL
TCSIICRAAF GSVIRDNAEL VGLVKDALSM ASGFELADMF PSSKLLNLLC WNKSKLWRMR
RRVDTILEAI VDEHKFKKSG EFGGEDIIDV LFRMQKDTQI KVPITTNSIK AFIFDTFSAG
TETSSTTTLW VLAELMRNPA VMAKAQAEVR AALKEKTNWD VDDVQELKYM KSVVKETMRM
HPPIPLIPRS CREECVVNGY TIPNKARIMI NVWSMGRNPL YWEKPDTFWP ERFDQVSKDF
MGNDFEFVPF GAGRRICPGL NFGLANVEVP LAQLLYHFDW KLAEGMKPSD MDMSEAEGLT
GILKNNLLLV PTPYDPSS
