TCMO_NARPS
ID TCMO_NARPS Reviewed; 505 AA.
AC A0A2H5AIX7;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Trans-cinnamate 4-monooxygenase {ECO:0000305};
DE EC=1.14.14.91 {ECO:0000250|UniProtKB:Q04468};
DE AltName: Full=Cinnamic acid 4-hydroxylase {ECO:0000303|PubMed:29229969};
DE Short=C4H {ECO:0000303|PubMed:29229969};
DE Short=CA4H {ECO:0000305};
DE AltName: Full=Cytochrome P450 C4H {ECO:0000305};
GN Name=C4H {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: Catalyzes the first oxidative step of the phenylpropanoid
CC pathway in higher plants by transforming trans-cinnamate into p-
CC coumarate (By similarity). The compounds formed by this pathway are
CC essential components for lignification, pollination, and defense
CC against ultraviolet light, predators and pathogens (By similarity).
CC Trans-4-coumarate is a precursor to all amaryllidaceae alkaloids such
CC as galanthamine, lycorine and haemanthamine, and including
CC haemanthamine- and crinamine-type alkaloids, promising anticancer
CC agents (Probable). {ECO:0000250|UniProtKB:Q04468,
CC ECO:0000305|PubMed:29229969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + O2 + reduced [NADPH--hemoprotein reductase] =
CC (E)-4-coumarate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:10608, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:12876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15669, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.91;
CC Evidence={ECO:0000250|UniProtKB:Q04468};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000303|PubMed:29229969}.
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-4-coumarate biosynthesis;
CC trans-4-coumarate from trans-cinnamate: step 1/1. {ECO:0000305}.
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; MF416091; AUG71936.1; -; mRNA.
DR AlphaFoldDB; A0A2H5AIX7; -.
DR SMR; A0A2H5AIX7; -.
DR UniPathway; UPA00825; UER00789.
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:0016710; F:trans-cinnamate 4-monooxygenase activity; IEA:UniProtKB-EC.
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..505
FT /note="Trans-cinnamate 4-monooxygenase"
FT /id="PRO_0000450633"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 213..218
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q94IP1"
FT BINDING 306
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q94IP1"
FT BINDING 447
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:Q94IP1"
SQ SEQUENCE 505 AA; 58018 MW; B34AE607F2DCE768 CRC64;
MDLILLEKSL LAVFFAVIFS IIVSKLRGKK LKLPPGPFPV PVFGNWIQVG DDLNHRNLAG
LAKKFGDIFL LRMGQRNLVV VSSPDLARDV LHTHGVEFGS RTRNVVFDIF TGKGQDMVFT
VYGEHWRKMR RIMTVPFFTN KVVNQYRFGW EEEAARVVED VKKDPMAAAE GIVLRRRLQL
LMYNNMYRIM FDRRFESVDD PLFLKLTALN GERSRLAQSF EYNYGDFIPI LRPFLRGYLK
ICKQVKERRF KLFKDYFLEE RKKLASTKPT DNAGLKCAID HILDAEKKGE INEDNVLYIV
ENINVAAIET TLWSIEWGIA ELVNHPNVQQ KLRNELDAVL GPGVQITEPD TYRLPYLQAV
IKETLRLRMA IPLLVPHMNL YDAKLGSYDI PAESKILVNA WWLANNPAHW KDPQEFRPER
FLEEEAKVEA NGNDFRYIPF GVGRRSCPGI ILALPILGIT IGRLVQNFEL LPPPGQDKLD
TTEKGGQFSL HILKHSTIVA KPRVF
