ID   TCMO_RUTGR              Reviewed;         506 AA.
AC   Q9AR74;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=CYP73A2;
OS   Ruta graveolens (Common rue).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Rutoideae; Ruta.
OX   NCBI_TaxID=37565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gravot A., Gontier E., Bourgaud F., Deleury E., Goergen J.L.;
RT   "Molecular cloning and expression of Ruta graveolens cinnamate 4-
RT   hydroxylase cDNA.";
RL   Submitted (APR-2001) 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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AJ309127; CAC35977.1; -; mRNA.
DR   AlphaFoldDB; Q9AR74; -.
DR   SMR; Q9AR74; -.
DR   PRIDE; Q9AR74; -.
DR   BRENDA; 1.14.14.91; 5486.
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..506
FT                   /note="Trans-cinnamate 4-monooxygenase"
FT                   /id="PRO_0000052253"
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   506 AA;  58105 MW;  7609D7508B9803D9 CRC64;
     MDLLLLEKAL LGLFAAAVVA IAVSKLRGKR FKLPPGPLGF PVFGNWLQVG DDLNQRKLAN
     LSKKFGDVYL LRMGQRNLVV VSSPEMAKEV LHTQGVEFGS RTRNVVFDIF TGKGQDMVFT
     VYSEHWRKMR RIMTVPFFTN KVVQQQRFNW EDEAARVVED VKKDPQAATT GIVLRRRLQL
     LMYNNMYRIM FDRRFESVDD PLFNKLKALN GERSRLAQSF EYNYGDFIPI LRPFLRGYLK
     LVKEVKERRL KLFKDYFVEE RKKLTSTKSM TEENFKCAID HVLDAQQKGE INEDNVLYIV
     ENINVAAIET TLWSIEWGIA ELVNHPDIQK KLRAEIDRVL GPDHQITEPD THKLPYLQAV
     IKETLRLRMA IPLLVPHMNL NDAKLAGYDI PAESKILVNA WWLANNPAHW KDPQVFRPER
     FLEEESGVEA NGNDFRYIPF GVGRRSCPGI ILALPILGIT IGRMVQNFEL LPPPGQSKID
     TSEKGGQFSL FILNHSTIVL KPRSSV