UniProt functional annotation for P30986

UniProt code: P30986.

Organism: Eschscholzia californica (California poppy).
Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Eschscholzioideae; Eschscholzia.
 
Function: Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine.
 
Catalytic activity: Reaction=(S)-reticuline + O2 = (S)-scoulerine + H(+) + H2O2; Xref=Rhea:RHEA:19885, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17129, ChEBI:CHEBI:57873; EC=1.21.3.3;
Cofactor: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16728404, ECO:0000269|PubMed:19457868}; Note=Binds 1 FAD per subunit in a bicovalent manner. {ECO:0000269|PubMed:16728404, ECO:0000269|PubMed:19457868};
Cofactor: Name=a metal cation; Xref=ChEBI:CHEBI:25213;
Pathway: Alkaloid biosynthesis; (S)-scoulerine biosynthesis; (S)- scoulerine from (S)-reticuline: step 1/1.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:24240298}. Note=Found in cytoplasmic vesicles that are highly specific and unique compartments serving only alkaloid biosynthesis. The protein composition of these vesicles reveals the presence of only about 20 separable proteins. {ECO:0000269|PubMed:24240298}.
Ptm: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha- N1-histidyl FAD linkage. {ECO:0000269|PubMed:16728404, ECO:0000269|PubMed:19457868}.
Similarity: Belongs to the oxygen-dependent FAD-linked oxidoreductase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.