ID   TCMO_PEA                Reviewed;         505 AA.
AC   Q43067; Q9FVK9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   24-MAR-2009, entry version 54.
DE   RecName: Full=Trans-cinnamate 4-monooxygenase;
DE            EC=1.14.13.11;
DE   AltName: Full=Cinnamic acid 4-hydroxylase;
DE            Short=CA4H;
DE            Short=C4H;
DE   AltName: Full=P450C4H;
DE   AltName: Full=Cytochrome P450 73;
GN   Name=CYP73A9;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE OF 1-497.
RC   STRAIN=cv. Little Marvel; TISSUE=Stem;
RX   MEDLINE=20438200; PubMed=10982421; DOI=10.1104/pp.124.1.47;
RA   Whitbred J.M., Schuler M.A.;
RT   "Molecular characterization of CYP73A9 and CYP82A1 P450 genes involved
RT   in plant defense in pea.";
RL   Plant Physiol. 124:47-58(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-505.
RC   TISSUE=Stem;
RX   MEDLINE=96417083; PubMed=8819874; DOI=10.1104/pp.110.3.1035;
RA   Frank M.R., Deyneka J.M., Schuler M.A.;
RT   "Cloning of wound-induced cytochrome P450 monooxygenases expressed in
RT   pea.";
RL   Plant Physiol. 110:1035-1046(1996).
RN   [3]
RP   SEQUENCE REVISION TO 208; 394; 404 AND 460.
RA   Schuler M.A.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Controls carbon flux to pigments essential for
CC       pollination or UV protection, to numerous pytoalexins synthesized
CC       by plants when challenged by pathogens, and to lignins.
CC   -!- CATALYTIC ACTIVITY: Trans-cinnamate + NADPH + O(2) = 4-
CC       hydroxycinnamate + NADP(+) + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Phenylpropanoid metabolism; 4-coumaric acid biosynthesis;
CC       4-coumaric acid from trans-cinnamic acid: step 1/1.
CC   -!- INDUCTION: By wounding.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AF175275; AAG09205.1; -; Genomic_DNA.
DR   EMBL; U29243; AAC49187.2; -; mRNA.
DR   PIR; T06522; T06522.
DR   BRENDA; 1.14.13.11; 287.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016710; F:trans-cinnamate 4-monooxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN         1    505       Trans-cinnamate 4-monooxygenase.
FT                                /FTId=PRO_0000052248.
FT   METAL       447    447       Iron (heme axial ligand) (By similarity).
FT   CONFLICT    271    271       Y -> D (in Ref. 1; AAG09205).
SQ   SEQUENCE   505 AA;  57991 MW;  1D8C4F348D4B820A CRC64;
     MDLLLLEKTL LALFLAAITA ITISKLRGKP FKLPPGPFPV PVFGNWLQVG DDLNHRNLTD
     LAKRFAEILL LRMEQRNLVV ISSPELAKEV LHTQGVEFGS RTRNVVFDIF TGKGQDIVFT
     VYGEHWRKMR RIMTVPFFTN KVVQQYRFGW ESEAASVVDD VKKNSKASVN GIVIRRRLQL
     MMYNIMYRIM FDRRFESEED PLFVKLKALN GERSRLAQSF EYNYGDFIPI LRPFLKGYLK
     VCKEVKDRRL QLFKDYFVDE RKKLGSTKST YNEGLKCAID HILDAQKKGE INDDNVLYIV
     ENINVAAIET TLWSIEWGIA ELVNHQEIQN KLREEMDKVL GPGHQVTEPD LEKLPYLQAV
     IKETLRLRMA IPLLVPHMNL HDAKLGGFDI PAESKILVNA WWLANNPALW KKPEEFRPER
     FLEEEAHVEA NGNDFRYLPF GVGRRSCPGI ILALPILGIT IGRLVQNFEL LPPPGQSKID
     TSEKGGQFSL HILKHSTIVA KPRAF
//