ID   C4H1_PETHY              Reviewed;         506 AA.
AC   F1B282;
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 C4H1 {ECO:0000305};
DE            EC=1.14.14.91 {ECO:0000250|UniProtKB:Q04468};
DE   AltName: Full=Cinnamate-4-hydroxylase 1 {ECO:0000303|PubMed:21068208};
DE            Short=PhC4H1 {ECO:0000303|PubMed:21068208};
DE   AltName: Full=Cytochrome P450 C4H1 {ECO:0000305};
GN   Name=C4H1 {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}.
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DR   EMBL; HM447144; ADX33332.1; -; mRNA.
DR   AlphaFoldDB; F1B282; -.
DR   SMR; F1B282; -.
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..506
FT                   /note="Trans-cinnamate 4-monooxygenase C4H1"
FT                   /id="PRO_0000451516"
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         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:Q8RN03"
SQ   SEQUENCE   506 AA;  58485 MW;  97D35CCD837339BD CRC64;
     MDLLLLEKTL IGLFFAIIIA IVVSKLRSKK FKLPPGPIPV PVFGNWLQVG DDLNHRNLTE
     YAKKFGDLFL LRMGQRNLVV VSSPELAKEV LHTQGVEFGS RTRNVVFDIF TGKGQDMVFT
     VYGEHWRKMR RIMTVPFFTN KVVQQYRGGW EDEVAHVIDD VKKMPESATN GIVLRKRLQL
     MMYNNMYRIM FDRRFESEDD PLFNKLKALN GERSRLAQSF EYNYGDFIPI LRPFLRGYLK
     ICKEVKQRRL QLFKDYFVDE RKKLSTTTKS MDNNALKCAI DHILEAEQKG EINEDNVLYI
     VENINVAAIE TTLWSIEWGI AELVNHPEIQ KKLRDEIDSV LGPGVQITEP HTHKLPYLQA
     VIKETLRLRM AIPLLVPHMN LHDAKLAGYD IPAESKILVN AWWLANNPAT WKRPEEFRPE
     RFFEEEKHVE ANGNDFRYLP FGVGRRSCPG IILALPILGI TLGRLVQNFE LLPPPGQSKL
     DTTEKGGQFS LHILKHFTIV MKPRSF