C71A6_NEPRA
ID C71A6_NEPRA Reviewed; 511 AA.
AC O04164;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cytochrome P450 71A6;
DE EC=1.14.-.-;
DE Flags: Fragment;
GN Name=CYP71A6;
OS Nepeta racemosa (Catmint) (Raceme catnip).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Nepetinae;
OC Nepeta.
OX NCBI_TaxID=54731;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=9106511; DOI=10.1023/a:1005706609510;
RA Clark I.M., Forde B.G., Hallahan D.L.;
RT "Spatially distinct expression of two new cytochrome P450s in leaves of
RT Nepeta racemosa: identification of a trichome-specific isoform.";
RL Plant Mol. Biol. 33:875-885(1997).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; Y09424; CAA70576.1; -; mRNA.
DR AlphaFoldDB; O04164; -.
DR SMR; O04164; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; 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 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN <1..511
FT /note="Cytochrome P450 71A6"
FT /id="PRO_0000052060"
FT TRANSMEM <1..15
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 450
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|UniProtKB:P04798"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT NON_TER 1
SQ SEQUENCE 511 AA; 57955 MW; EEFC238BD8112432 CRC64;
ILIALLCTLP FLFFLKKWRR SYSGKTPPPS PPKLPVLGNL HQLGTFPHRS LQSLSRRYGP
VMQLHFGSVP VLVASSPEAA REIMKNQDLN FSNRPNLSIP RRLLYDNHDV AFAPYGEYWR
QIRSICVLQL LSNKRVQSFR RVREEETSIM VEKIMQLQKT TPTAAVNLTD LLTCLTNDVF
CRIALGKKYG GTTTGDGEYH VRSLKKNLAE FYVLLGISPL WEYIPWLEWT RRFDGVDRRI
EEVSRTFDEF LGKVIQEHRV RDKREDTTVV GDTVGLDFVD LLLQFQRENE RSSSPVDDLT
IKAVILDMFL AGTDTTVTAL EWALSELIKN PRAMKILQKE VRGVAGSKGE IEESDLEKMP
YLKAVMKESL RLHAPVPLLV PRESTRDTKV LGYDVASGTR VLINCWAIGR DSSVWEESET
FLPERFLETS IDYRGMHFEL IPFGSGRRGC PGATFAAAID ELALATLVHK FDFKLPNGVR
VEDLDMSEGS GFTIHKKFPL LVVPTPHACT S