ID   C3H_NARPS               Reviewed;         509 AA.
AC   A0A2H5AIX6;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=p-coumarate 3-hydroxylase {ECO:0000303|PubMed:29229969};
DE            EC=1.14.13.- {ECO:0000312|EMBL:AUG71937.1};
DE   AltName: Full=Cytochrome P450 C3H {ECO:0000305};
GN   Name=C3H {ECO:0000303|PubMed:29229969};
OS   Narcissus pseudonarcissus (Daffodil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Amaryllidoideae; Narcissus.
OX   NCBI_TaxID=39639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, REVIEW ON THE AMARYLLIDACEAE ALKALOID
RP   METABOLISM, PATHWAY, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. King Alfred; TISSUE=Bulb;
RX   PubMed=29229969; DOI=10.1038/s41598-017-17724-0;
RA   Singh A., Desgagne-Penix I.;
RT   "Transcriptome and metabolome profiling of Narcissus pseudonarcissus 'King
RT   Alfred' reveal components of Amaryllidaceae alkaloid metabolism.";
RL   Sci. Rep. 7:17356-17356(2017).
CC   -!- FUNCTION: Cytochrome P450 which catalyzes 3'-hydroxylation of p-
CC       coumaric esters of shikimic/quinic acids to form lignin monomers and
CC       caffeic acid (By similarity). Involved in the biosynthesis of
CC       phenylpropanoids and Amaryllidaceae alkaloids, including
CC       haemanthamine- and crinamine-type alkaloids, promising anticancer
CC       agents (PubMed:29229969). {ECO:0000250|UniProtKB:O22203,
CC       ECO:0000303|PubMed:29229969}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000303|PubMed:29229969}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in stems, and, to a lower extent,
CC       in bulbs, roots, leaves and flowers. {ECO:0000269|PubMed:29229969}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; MF416092; AUG71937.1; -; mRNA.
DR   AlphaFoldDB; A0A2H5AIX6; -.
DR   SMR; A0A2H5AIX6; -.
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   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
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   Alkaloid metabolism; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="p-coumarate 3-hydroxylase"
FT                   /id="PRO_0000450634"
FT   TRANSMEM        1..21
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|UniProtKB:Q96242"
SQ   SEQUENCE   509 AA;  57711 MW;  8E5F19CE1BE83AAF CRC64;
     MDPSPLSISI AIFSLLISFL LYKKLTTKLP PGPKPWPVVG NLYDIKPVRF RCFAEWAQTY
     GPIMSVWFGT TLNIVVSSSE LAKEVLKEKD QILADRPRNR AAARFSRDGK DLIWADYGPH
     YVKVRKVCNL ELFSPKRLEG LRPIREDEVT AMVESIFREC TQQDKIGNSL VVRNHLSGVA
     FSNITRLAFG KRFVNSEGVM DEQGLEFKAI VANGLKLGAS LSLGEYVTWL KWMFPFDEEA
     VAKHGARRDR LTRAIMEEHS LARKESGARQ HFVDALLTLQ EKYDLSEDTI IGLLWDMITA
     GMDTTVISVE WAMAELVKHP RVQEKVQEEL DRVIGVDRIM TESDFPNLPY LHCVVKEALR
     LHPPTPLMLP HKASANTKIG GYDIPKGAVV HVNVWAIARD PNSWKNPLEF RPERFQEESI
     DIKGNDFRVL PFGAGRRVCP GAQLGINLVQ SMLGHLLHHF KWELPEGMKP EEIDMTENPG
     MVTFMHTPLQ AVAIPRLPSH LYKRMAVDM