ID   C4H2_PETHY              Reviewed;         505 AA.
AC   F1B283;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Trans-cinnamate 4-monooxygenase C4H2 {ECO:0000305};
DE            EC=1.14.14.91 {ECO:0000250|UniProtKB:Q04468};
DE   AltName: Full=Cinnamate-4-hydroxylase 2 {ECO:0000303|PubMed:21068208};
DE            Short=PhC4H2 {ECO:0000303|PubMed:21068208};
DE   AltName: Full=Cytochrome P450 C4H2 {ECO:0000305};
GN   Name=C4H2 {ECO:0000303|PubMed:21068208};
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], REPRESSION BY MYB4, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Mitchell;
RX   PubMed=21068208; DOI=10.1093/jxb/erq342;
RA   Colquhoun T.A., Kim J.Y., Wedde A.E., Levin L.A., Schmitt K.C.,
RA   Schuurink R.C., Clark D.G.;
RT   "PhMYB4 fine-tunes the floral volatile signature of Petunia x hybrida
RT   through PhC4H.";
RL   J. Exp. Bot. 62:1133-1143(2011).
CC   -!- FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid
CC       (FVBP) biosynthetic pathway that controls carbon flux to pigments
CC       essential for pollination or UV protection, to numerous pytoalexins
CC       synthesized by plants when challenged by pathogens, and to lignins.
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:Q8RN03};
CC   -!- PATHWAY: Phenylpropanoid metabolism; trans-4-coumarate biosynthesis;
CC       trans-4-coumarate from trans-cinnamate: step 1/1.
CC       {ECO:0000250|UniProtKB:Q04468}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC   -!- DEVELOPMENTAL STAGE: In corollas, accumulates progressively during
CC       flower development, from buds to anthesis, with a peak at flower
CC       opening, but fades out in senescing flowers.
CC       {ECO:0000269|PubMed:21068208}.
CC   -!- INDUCTION: Repressed by MYB4. {ECO:0000269|PubMed:21068208}.
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; HM447145; ADX33333.1; -; mRNA.
DR   AlphaFoldDB; F1B283; -.
DR   SMR; F1B283; -.
DR   UniPathway; UPA00825; UER00789.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; Metal-binding; Monooxygenase; Nucleus; Oxidoreductase.
FT   CHAIN           1..505
FT                   /note="Trans-cinnamate 4-monooxygenase C4H2"
FT                   /id="PRO_0000451517"
FT   MOTIF           161..168
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           247..254
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
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:Q8RN03"
SQ   SEQUENCE   505 AA;  58309 MW;  762C9A1A3B5D3207 CRC64;
     MDLLLLEKTL IGLFIAIIIA TIVSKLRSKR FKLPPGPIPV PVFGNWLQVG DDLNHRNLTE
     YAKKFGDLFL LRMGQRNLVV VSSPDLAKEV LHTQGVEFGS RTRNVVFDIF TGKGQDMVFT
     VYGEHWRKMR RIMTVPFFTN KVVQQYRGGW EYEVESVVED VKKMKESNTN GIVLRKRLQL
     MMYNNMFRIM FDRRFESEDD PLFVKLKALN GERSRLAQSF EYNYGDFIPI LRPFLRGYLK
     ICKEVKEKRL KLFKDYFVDE RKKLANTKSM DSNALKCAID HILEAQQKGE INEDNVLYIV
     ENINVAAIET TLWSIEWGIA ELVNHPHIQK KLRDEIDTVL GPGVQVTEPD THKLPYLQAV
     IKETLRLRMA IPLLVPHMNL HEAKLGGYDI PAESKILVNA WWLANNPAHW KNPEEFRPER
     FFEEEKHVEA NGNDFRYLPF GVGRRSCPGI ILALPILGIT LGRLVQNFEL LPPPGQSKID
     TTEKGGQFSL HILKHSTIVL KPRSF