ID   TCMO_POPKI              Reviewed;         505 AA.
AC   Q43054; O04989; Q40906; Q43044;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=CYP73A16; Synonyms=CYP73;
OS   Populus kitakamiensis (Aspen) (Populus sieboldii x Populus grandidentata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=34292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Y-63;
RX   PubMed=8987656; DOI=10.1271/bbb.60.1586;
RA   Kawai S., Mori A., Shiokawa T., Kajita S., Katayama Y., Morohoshi N.;
RT   "Isolation and analysis of cinnamic acid 4-hydroxylase homologous genes
RT   from a hybrid aspen, Populus kitakamiensis.";
RL   Biosci. Biotechnol. Biochem. 60:1586-1597(1996).
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D82812; BAA11576.1; -; Genomic_DNA.
DR   EMBL; D82815; BAA11579.1; -; mRNA.
DR   AlphaFoldDB; Q43054; -.
DR   SMR; Q43054; -.
DR   ChEMBL; CHEMBL2268005; -.
DR   PRIDE; Q43054; -.
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_0000052251"
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;  57973 MW;  FA97C0FA9B138151 CRC64;
     MDLLLLEKTL LGSFVAVLVA ILVSKLRGKR FKLPPGPLPV PVFGNWLQVG DDLNHRNLTD
     LAKKFGDIFL LRMGQRNLVV VSSPDLSKEV LHTQGVEFGS RTRNVVFDIF TGKGQDMVFT
     VYGEHWRKMR RIMTVPFFTN KVVQQYRYGW EEEAAQVVED VKKNPEAATN GIVLRRRLQL
     MMYNNMYRIM FDRRFESEDD PLFNKLKALN GERSRLAQSF DYNYGDFIPI LRPFLRGYLK
     ICQEVKERRL QLFKDYFVDE RKKLASTKNM SNEGLKCAID HILDAQKKGE INEDNVLYIV
     ENINVAAIET TLWSIEWGIA ELVNHPEIQK KLRHELDTLL GPGHQITEPD TYKLPYLNAV
     VKETLRLRMA IPLLVPHMNL HDAKLGGFDI PAESKILVNA WWLANNPAHW KNPEEFRPER
     FLEEGAKVEA NGNDFRYLPF GVGRRSCPGI ILALPILGIT LGRLVQNFEL LPPPGQSKID
     TSEKGGQFSL HILKHSTIVA KPRSF