ID   TCMO_PEA                Reviewed;         505 AA.
AC   Q43067; Q9FVK9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Trans-cinnamate 4-monooxygenase;
DE            EC=1.14.14.91 {ECO:0000250|UniProtKB:Q04468};
DE   AltName: Full=Cinnamic acid 4-hydroxylase;
DE            Short=C4H;
DE            Short=CA4H;
DE   AltName: Full=Cytochrome P450 73;
DE   AltName: Full=Cytochrome P450C4H;
GN   Name=CYP73A9;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE OF 1-497.
RC   STRAIN=cv. Little Marvel; TISSUE=Stem;
RX   PubMed=10982421; DOI=10.1104/pp.124.1.47;
RA   Whitbred J.M., Schuler M.A.;
RT   "Molecular characterization of CYP73A9 and CYP82A1 P450 genes involved in
RT   plant defense in pea.";
RL   Plant Physiol. 124:47-58(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-505.
RC   TISSUE=Stem;
RX   PubMed=8819874; DOI=10.1104/pp.110.3.1035;
RA   Frank M.R., Deyneka J.M., Schuler M.A.;
RT   "Cloning of wound-induced cytochrome P450 monooxygenases expressed in
RT   pea.";
RL   Plant Physiol. 110:1035-1046(1996).
RN   [3]
RP   SEQUENCE REVISION TO 208; 394; 404 AND 460.
RA   Schuler M.A.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000250|UniProtKB:Q04468}.
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: 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   -!- INDUCTION: By wounding.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF175275; AAG09205.1; -; Genomic_DNA.
DR   EMBL; U29243; AAC49187.2; -; mRNA.
DR   PIR; T06522; T06522.
DR   AlphaFoldDB; Q43067; -.
DR   SMR; Q43067; -.
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   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..505
FT                   /note="Trans-cinnamate 4-monooxygenase"
FT                   /id="PRO_0000052248"
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"
FT   CONFLICT        271
FT                   /note="Y -> D (in Ref. 1; AAG09205)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   505 AA;  57991 MW;  1D8C4F348D4B820A CRC64;
     MDLLLLEKTL LALFLAAITA ITISKLRGKP FKLPPGPFPV PVFGNWLQVG DDLNHRNLTD
     LAKRFAEILL LRMEQRNLVV ISSPELAKEV LHTQGVEFGS RTRNVVFDIF TGKGQDIVFT
     VYGEHWRKMR RIMTVPFFTN KVVQQYRFGW ESEAASVVDD VKKNSKASVN GIVIRRRLQL
     MMYNIMYRIM FDRRFESEED PLFVKLKALN GERSRLAQSF EYNYGDFIPI LRPFLKGYLK
     VCKEVKDRRL QLFKDYFVDE RKKLGSTKST YNEGLKCAID HILDAQKKGE INDDNVLYIV
     ENINVAAIET TLWSIEWGIA ELVNHQEIQN KLREEMDKVL GPGHQVTEPD LEKLPYLQAV
     IKETLRLRMA IPLLVPHMNL HDAKLGGFDI PAESKILVNA WWLANNPALW KKPEEFRPER
     FLEEEAHVEA NGNDFRYLPF GVGRRSCPGI ILALPILGIT IGRLVQNFEL LPPPGQSKID
     TSEKGGQFSL HILKHSTIVA KPRAF