ID   TCMO_VIGRR              Reviewed;         505 AA.
AC   P37115;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 99.
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   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-49; 255-262 AND
RP   485-501.
RC   TISSUE=Hypocotyl;
RX   PubMed=8439336; DOI=10.1006/bbrc.1993.1130;
RA   Mizutani M., Ward E., Dimaio J., Ohta D., Ryals J., Sato R.;
RT   "Molecular cloning and sequencing of a cDNA encoding mung bean cytochrome
RT   P450 (P450C4H) possessing cinnamate 4-hydroxylase activity.";
RL   Biochem. Biophys. Res. Commun. 190:875-880(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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; L07634; AAA33755.1; -; mRNA.
DR   PIR; JC1458; JC1458.
DR   RefSeq; NP_001304077.1; NM_001317148.1.
DR   AlphaFoldDB; P37115; -.
DR   SMR; P37115; -.
DR   STRING; 3916.P37115; -.
DR   GeneID; 106764845; -.
DR   KEGG; vra:106764845; -.
DR   UniPathway; UPA00825; UER00789.
DR   Proteomes; UP000087766; Chromosome 6.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Membrane; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..505
FT                   /note="Trans-cinnamate 4-monooxygenase"
FT                   /id="PRO_0000052250"
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   VARIANT         40
FT                   /note="V -> I (in clone PC4H-II)"
FT   CONFLICT        38
FT                   /note="L -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        498
FT                   /note="V -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   505 AA;  57888 MW;  563615D61D33BD95 CRC64;
     MDLLLLEKTL LGLFLAAVVA IVVSKLRGKR FKLPPGPLPV PIFGNWLQVG DDLNHRNLTQ
     LAKRFGDIFL LRMGQRNLVV VSSPDLAKEV LHTQGVEFGS RTRNVVFDIF TGEGQDMVFT
     VYGEHWRKMR RIMTVPFFTN KVVQQYRHGW EAEAAAVVDD VRKNPDAAVS GLVIRRRLQL
     MMYNNMYRIM FDRRFESEED PLFQRLKALN GERSRLAQSF EYNYGDFIPI LRPFLKGYLK
     ICKEVKETRL KLFKDYFVDE RKNIGSTKST NNEGLKCAID HILDAEKKGE INEDNVLYIV
     ENINVAAIET TLWSIEWGIA ELVNHPEIQQ KVRDEIDRVL GVGHQVTEPD IQKLPYLQAV
     VKETLRLRMA IPLLVPHMNL HDAKLGGYDI PAESKILVNA WWLANNPAHW KKPEEFRPER
     FFEEESHVEA NGNDFRYLPF GVGRRSCPGI ILALPILGIT LGRLVQNFEL LPPPGQSQID
     TSEKGGQFSL HILKHSTVVA KPRSF