ID   TCMO_MEDSA              Reviewed;         506 AA.
AC   P37114;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=CYP73A3;
OS   Medicago sativa (Alfalfa).
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; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8373188; DOI=10.1006/abbi.1993.1454;
RA   Fahrendorf T., Dixon R.A.;
RT   "Stress responses in alfalfa (Medicago sativa L.). XVIII: molecular cloning
RT   and expression of the elicitor-inducible cinnamic acid 4-hydroxylase
RT   cytochrome P450.";
RL   Arch. Biochem. Biophys. 305:509-515(1993).
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 fungal elicitor.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; L11046; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; S36878; S36878.
DR   AlphaFoldDB; P37114; -.
DR   SMR; P37114; -.
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_0000052247"
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         307
FT                   /ligand="(E)-cinnamate"
FT                   /ligand_id="ChEBI:CHEBI:15669"
FT                   /evidence="ECO:0000250|UniProtKB:Q94IP1"
FT   BINDING         448
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;  58280 MW;  5CD72A57FC031E0F CRC64;
     MDLLLLEKTL LALFIAATIA VTISKLRGKR FKLPPGPIPV PIFGYWLQVG DDLNHRNLTD
     YAKRFGEIFL LRMGQRNLVV VSSPELAKEV LHTQCVEFGS RTRNVVFDIF TGKGQDMVFT
     VYGEHWRKMR RIMTVPFFTN KVVQQYRYGW ESEAESVVND VKNNAEASVG GIVIRKRLQL
     MMYNIMYRIM FDRRFESEED PLFVKLKALN GERSRLAQSF EYNYGDFIPI LRPFLKGYLK
     VCKEVKDRRL QLFKDYFVDE RKKLESTKST TSNDGLKCAI DHILDAQKKG EINDDNVLYI
     VENINVAAIE TTLWSIEWGI AELVNHQDIQ NKVREEMDRV LGPGHQVTEP DLHKLPYLQA
     VIKETLRLRM AIPLLVPHMN LHDPKLNGFD IPAESKILVN AWWLPNNPAH WKKPEEFRPE
     RFLEEESHVE ANGNDFRYLP FGVGRRSCPG IILALPILGI TIGRLVQNVE LLPPPGQSKI
     DTSEKGGQFS LHILKHSTIV AKPRSF