ID   C76AD_BETVU             Reviewed;         497 AA.
AC   I3PFJ5;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Cytochrome P450 76AD1 {ECO:0000303|PubMed:22660548};
DE            EC=1.14.-.- {ECO:0000305};
GN   Name=CYP76AD1 {ECO:0000303|PubMed:22660548};
GN   Synonyms=Bv2g029890_ucyh {ECO:0000303|PubMed:25249410},
GN   Bv_ucyh {ECO:0000303|PubMed:25249410};
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934 {ECO:0000312|EMBL:AET43289.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. C869, and cv. W357B;
RX   PubMed=22660548; DOI=10.1038/ng.2297;
RA   Hatlestad G.J., Sunnadeniya R.M., Akhavan N.A., Gonzalez A., Goldman I.L.,
RA   McGrath J.M., Lloyd A.M.;
RT   "The beet R locus encodes a new cytochrome P450 required for red betalain
RT   production.";
RL   Nat. Genet. 44:816-820(2012).
RN   [2]
RP   NOMENCLATURE.
RC   STRAIN=cv. KWS2320;
RX   PubMed=25249410; DOI=10.1186/s12870-014-0249-8;
RA   Stracke R., Holtgrawe D., Schneider J., Pucker B., Rosleff Sorensen T.,
RA   Weisshaar B.;
RT   "Genome-wide identification and characterisation of R2R3-MYB genes in sugar
RT   beet (Beta vulgaris).";
RL   BMC Plant Biol. 14:249-249(2014).
RN   [3]
RP   INDUCTION.
RX   PubMed=25436858; DOI=10.1038/ng.3163;
RA   Hatlestad G.J., Akhavan N.A., Sunnadeniya R.M., Elam L., Cargile S.,
RA   Hembd A., Gonzalez A., McGrath J.M., Lloyd A.M.;
RT   "The beet Y locus encodes an anthocyanin MYB-like protein that activates
RT   the betalain red pigment pathway.";
RL   Nat. Genet. 47:92-96(2015).
CC   -!- FUNCTION: Converts L-DOPA to cyclo-DOPA in the betalain pathway.
CC       Provides the cyclo-DOPA moiety of all red betacyanins.
CC       {ECO:0000269|PubMed:22660548}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Pigment biosynthesis; betalain biosynthesis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Regulated by MYB1. {ECO:0000269|PubMed:25436858}.
CC   -!- MISCELLANEOUS: A frameshift mutant replacing 108 native amino acids
CC       with 27 new residues followed by a stop codon results in an inactive
CC       protein (AC P0DKI2) and a yellow mutant phenotype.
CC       {ECO:0000269|PubMed:22660548}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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; HQ656023; AET43289.1; -; mRNA.
DR   EMBL; HQ656024; AET43290.1; -; mRNA.
DR   AlphaFoldDB; I3PFJ5; -.
DR   SMR; I3PFJ5; -.
DR   UniPathway; UPA00278; -.
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..497
FT                   /note="Cytochrome P450 76AD1"
FT                   /id="PRO_0000431983"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         439
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   497 AA;  56212 MW;  8E94BC295A505281 CRC64;
     MDHATLAMIL AIWFISFHFI KLLFSQQTTK LLPPGPKPLP IIGNILEVGK KPHRSFANLA
     KIHGPLISLR LGSVTTIVVS SADVAKEMFL KKDHPLSNRT IPNSVTAGDH HKLTMSWLPV
     SPKWRNFRKI TAVHLLSPQR LDACQTFRHA KVQQLYEYVQ ECAQKGQAVD IGKAAFTTSL
     NLLSKLFFSV ELAHHKSHTS QEFKELIWNI MEDIGKPNYA DYFPILGCVD PSGIRRRLAC
     SFDKLIAVFQ GIICERLAPD SSTTTTTTTD DVLDVLLQLF KQNELTMGEI NHLLVDIFDA
     GTDTTSSTFE WVMTELIRNP EMMEKAQEEI KQVLGKDKQI QESDIINLPY LQAIIKETLR
     LHPPTVFLLP RKADTDVELY GYIVPKDAQI LVNLWAIGRD PNAWQNADIF SPERFIGCEI
     DVKGRDFGLL PFGAGRRICP GMNLAIRMLT LMLATLLQFF NWKLEGDISP KDLDMDEKFG
     IALQKTKPLK LIPIPRY