ID   C79B1_SINAL             Reviewed;         542 AA.
AC   O81345;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Cytochrome P450 79B1;
DE            EC=1.14.-.-;
GN   Name=CYP79B1;
OS   Sinapis alba (White mustard) (Brassica hirta).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX   NCBI_TaxID=3728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Carla;
RX   PubMed=9862490; DOI=10.1023/a:1006064202774;
RA   Bak S., Nielsen H.L., Halkier B.A.;
RT   "The presence of CYP79 homologues in glucosinolate-producing plants shows
RT   evolutionary conservation of the enzymes in the conversion of amino acid to
RT   aldoxime in the biosynthesis of cyanogenic glucosides and glucosinolates.";
RL   Plant Mol. Biol. 38:725-734(1998).
CC   -!- FUNCTION: Converts tyrosine to para-hydrophenylacetaldoxime in para-
CC       hydroxybenzylglucosinolate biosynthesis.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF069494; AAD03415.1; -; mRNA.
DR   AlphaFoldDB; O81345; -.
DR   SMR; O81345; -.
DR   BioCyc; MetaCyc:MON-20257; -.
DR   SABIO-RK; O81345; -.
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   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..542
FT                   /note="Cytochrome P450 79B1"
FT                   /id="PRO_0000052155"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         478
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"
SQ   SEQUENCE   542 AA;  61291 MW;  F8CB41ADD2E54F41 CRC64;
     MNTFTSNSSD LTSTTKQTLS FSNMYLLTTL QAFVAITLVM LLKKVLVNDT NKKKLSLPPG
     PTGWPIIGMV PTMLKSRPVF RWLHSIMKQL NTEIACVRLG STHVITVTCP KIAREVLKQQ
     DALFASRPMT YAQNVLSNGY KTCVITPFGE QFKKMRKVVM TELVCPARHR WLHQKRAEEN
     DHLTAWVYNM VNNSDSVDFR FVTRHYCGNA IKKLMFGTRT FSQNTAPNGG PTAEDIEHME
     AMFEALGFTF SFCISDYLPI LTGLDLNGHE KIMRDSSAIM DKYHDPIIDA RIKMWREGKK
     TQIEDFLDIF ISIKDEEGNP LLTADEIKPT IKELVMAAPD NPSNAVEWAM AEMVNKPEIL
     RKAMEEIDRV VGKERLVQES DIPKLNYVKA ILREAFRLHP VAAFNLPHVA LSDATVAGYH
     IPKGSQVLLS RYGLGRNPKV WADPLSFKPE RHLNECSEVT LTENDLRFIS FSTGKRGCAA
     PALGTALTTM LLARLLQGFT WKLPENETRV ELMESSHDMF LAKPLVMVGE LRLPEHLYPT
     VK