ID Q76M94_ASPOF Unreviewed; 498 AA.
AC Q76M94;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:BAD06417.1};
GN Name=Asp-3 {ECO:0000313|EMBL:BAD06417.1};
OS Asparagus officinalis (Garden asparagus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC Asparagoideae; Asparagus.
OX NCBI_TaxID=4686 {ECO:0000313|EMBL:BAD06417.1};
RN [1] {ECO:0000313|EMBL:BAD06417.1}
RP NUCLEOTIDE SEQUENCE.
RA Imaishi H., Iwai C., Iwamura H., Ohkawa H.;
RT "P450 in Asparagus.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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; AB052131; BAD06417.1; -; mRNA.
DR AlphaFoldDB; Q76M94; -.
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 CDD; cd11072; CYP71-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR47956; CYTOCHROME P450 71B11-RELATED; 1.
DR PANTHER; PTHR47956:SF123; OS05G0424300 PROTEIN; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..498
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004287504"
SQ SEQUENCE 498 AA; 56518 MW; 250978855CC59454 CRC64;
MPLILVILLL LPILLLVIRR EKSTSSKLPP CPPKLPLIGN LHQLGSLPHQ SLHALSVKYG
PLMLLKLGEI PTLIVSSSDM AREIMRTHDH IFASRPSLLT SDILLNGATD VVFAPYGEHW
RQMRKLCVNH LLSAKMVQSF RLMREEEVSS MLTRISGLVN MSEVLNLFTS KILFNAISGK
FFVEEEGRIN VFCKLIRENI AILAQLSVSD FFPSLGWLDL VFGVGARARA TAKKWDDVLD
EVIEDHVKRS NETGDADDQE ERADFVSVLM ALQEDDNTGF TLNRNIIKAI LQDMIAAGTE
TSFLVLDWGM TELVRNPGTM KKLKDEVRSV AGSETVVREE DISKMFYLKA VIKEILRLHP
PVPLLIPRES MDHCNVQQYE VPSKTRVLIN AWSMGRDPKV WEDPEEFRPE RFLDSDIDFR
GQCFEFVPFG AGRRICPGMH FAAANLELAL ANLMYRFDWE LPDGMKSEDL DMGDSPGLTT
RRRQNLHLVA RPFQRVKR
//