Cytochrome P450 71D15 - Mentha piperita (Peppermint)

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Q9XHE6 (C71DF_MENPI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytochrome P450 71D15
EC=1.14.13.47

Alternative name(s):
(-)-(4S)-Limonene-3-hydroxylase
Cytochrome P450 isoform PM2

Gene names

Name:

CYP71D15

Organism

Mentha piperita (Peppermint)

Taxonomic identifier

34256 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Lamiaceae › Nepetoideae › Mentheae › Mentha

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydroxylates (-)-(4S)-limonene to (-)-trans-isopiperitenol, a precursor of (-)-menthol, responsible for the cooling sensation of peppermint. Fluorinated substrate analogs are hydroxylated with the same regio- and stereochemistry. Ref.1 Ref.4
Catalytic activity	^--(S)-limonene + NADPH + O₂ = (-)-trans-isopiperitenol + NADP⁺ + H₂O. Ref.1 Ref.4
Cofactor	Heme group By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein Potential.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Gene Ontology (GO)
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	(S)-limonene 3-monooxygenase activity Inferred from direct assay Ref.1. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 498

498

Cytochrome P450 71D15

PRO_0000389499

Regions

Transmembrane

3 – 23

Helical; Signal-anchor for type II membrane protein; Potential

Sites

Metal binding

437

Iron (heme axial ligand) By similarity

Experimental info

Mutagenesis

358

M → L: No effect on activity or regiospecificity. Ref.3

Mutagenesis

360

M → L: Strong decrease of acitvity. Ref.3

Mutagenesis

364

I → F: Loss of activity. Ref.3

Mutagenesis

370

S → Q: No effect on activity or regiospecificity. Ref.3

Mutagenesis

371

C → S: No effect on activity or regiospecificity. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q9XHE6 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: D78DDC2CD5C7EA48
Show »

FASTA

498

56,532

        10         20         30         40         50         60 
MELLQLWSAL IILVVTYTIS LLINQWRKPK PQGKFPPGPP KLPLIGHLHL LWGKLPQHAL 

        70         80         90        100        110        120 
ASVAKEYGPV AHVQLGEVFS VVLSSREATK EAMKLVDPAC ANRFESIGTR IMWYDNEDII 

       130        140        150        160        170        180 
FSPYSEHWRQ MRKICVSELL SSRNVRSFGF IRQDEVSRLL RHLRSSAGAA VDMTERIETL 

       190        200        210        220        230        240 
TCSIICRAAF GSVIRDNAEL VGLVKDALSM ASGFELADMF PSSKLLNLLC WNKSKLWRMR 

       250        260        270        280        290        300 
RRVDTILEAI VDEHKFKKSG EFGGEDIIDV LFRMQKDTQI KVPITTNSIK AFIFDTFSAG 

       310        320        330        340        350        360 
TETSSTTTLW VLAELMRNPA VMAKAQAEVR AALKEKTNWD VDDVQELKYM KSVVKETMRM 

       370        380        390        400        410        420 
HPPIPLIPRS CREECVVNGY TIPNKARIMI NVWSMGRNPL YWEKPDTFWP ERFDQVSKDF 

       430        440        450        460        470        480 
MGNDFEFVPF GAGRRICPGL NFGLANVEVP LAQLLYHFDW KLAEGMKPSD MDMSEAEGLT 

       490 
GILKNNLLLV PTPYDPSS

« Hide

References

[1]	"Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha) species: cDNA isolation, characterization, and functional expression of (-)-4S-limonene-3-hydroxylase and (-)-4S-limonene-6-hydroxylase." Lupien S., Karp F., Wildung M., Croteau R. Arch. Biochem. Biophys. 368:181-192(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY. Strain: cv. Black Mitcham.
[2]	"Isolation of full-length genes of menthol biosynthesis pathway from Mentha x piperita cv. Madhuras." Gupta M.K., Gupta S., Shasany A.K., Khanuja S.P.S. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Madhuras.
[3]	"A single amino acid substitution (F363I) converts the regiochemistry of the spearmint (-)-limonene hydroxylase from a C6- to a C3-hydroxylase." Schalk M., Croteau R. Proc. Natl. Acad. Sci. U.S.A. 97:11948-11953(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF MET-358; MET-360; ILE-364; SER-370 AND CYS-371.
[4]	"Hydroxylation of limonene enantiomers and analogs by recombinant (-)-limonene 3- and 6-hydroxylases from mint (Mentha) species: evidence for catalysis within sterically constrained active sites." Wuest M., Little D.B., Schalk M., Croteau R. Arch. Biochem. Biophys. 387:125-136(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Mint condition - Issue 113 of January 2010

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF124817 mRNA. Translation: AAD44152.1. EU108698 mRNA. Translation: ABW86882.1.
3D structure databases
HSSP	HSSP built from PDB template 1W0E based on UniProtKB P08684.
ProteinModelPortal	Q9XHE6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-6761.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C71DF_MENPI

Accession

Primary (citable) accession number: Q9XHE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 24, 2009
Last sequence update:	November 1, 1999
Last modified:	April 3, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents