ID   TCMO_ZINVI              Reviewed;         505 AA.
AC   Q43240;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=CYP73A12;
OS   Zinnia violacea (Garden zinnia) (Zinnia elegans).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Zinnia.
OX   NCBI_TaxID=34245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Peter Pan;
RA   Ye Z.-H., Varner J.E.;
RT   "Expression patterns of cinnamic acid 4-hydroxylase gene during
RT   lignification in Zinnia elegans.";
RL   Plant Sci. 121:133-141(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U19922; AAB42024.1; -; mRNA.
DR   AlphaFoldDB; Q43240; -.
DR   SMR; Q43240; -.
DR   PRIDE; Q43240; -.
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:0051762; P:sesquiterpene biosynthetic process; IEA:UniProt.
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_0000052255"
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;  57914 MW;  C51AAAEBD36C55C8 CRC64;
     MDLLLVEKTL LALFAAIIAS IFISKLRGKR FKLPPGPVPV PIFGNWLQVG DDLNHRNLTD
     LAKKFGEIFL LRMGQRNLVV VSSPNLAKEV LHTQGVEFGS RTRNVVFDIF TGKGQDMVFT
     VYGEHWRKMR RIMTVPFFTN KVVQQYRTGW EAEAAAVVDD VKKNPKAATE GVVIRKRLQL
     MMYNNMFRIM FDRRFESEDD PLFVKLKMLN GERSRLAQSF EYNYGDFIPI LRPFLKGYLK
     LCKEVKEKRF QLFKDYFVDE RKKLGSTKSM DNNQLKCAID HILDAKDKGE INEDNVLYIV
     ENINVAAIET TLWSIEWAIA ELVNHPEIQA KLRHELVSQL GPGVQVTEPD LHKLPYLQAV
     IKETLRLRMA IPLLVPHMNL HDAKLGGYDI PAESKILVNA WWLANNPDQW KKPEEFRPER
     FLEEESKVEA NGNDFRYLPF GVGRRSCPGI ILALPILGIT IGRLVQNFEL LPPPGQDKVD
     TTEKGGQFSL HILKHSTIVA KPRVL