TCMO_ARATH
ID TCMO_ARATH Reviewed; 505 AA.
AC P92994; O04995; O49834; P92993;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
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;
DE AltName: Full=Protein REDUCED EPIDERMAL FLUORESCENCE 3 {ECO:0000303|PubMed:19682296};
GN Name=CYP73A5 {ECO:0000303|PubMed:9085571};
GN Synonyms=CYP73 {ECO:0000303|PubMed:9085571},
GN REF3 {ECO:0000303|PubMed:19682296};
GN OrderedLocusNames=At2g30490 {ECO:0000312|Araport:AT2G30490};
GN ORFNames=T6B20.16 {ECO:0000312|EMBL:AAB63088.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND INDUCTION
RP BY WOUNDING.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=9085570; DOI=10.1104/pp.113.3.729;
RA Bell-Lelong D.A., Cusumano J.C., Meyer K., Chapple C.;
RT "Cinnamate-4-hydroxylase expression in Arabidopsis. Regulation in response
RT to development and the environment.";
RL Plant Physiol. 113:729-738(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=9085571; DOI=10.1104/pp.113.3.755;
RA Mizutani M., Ohta D., Sato R.;
RT "Isolation of a cDNA and a genomic clone encoding cinnamate 4-hydroxylase
RT from Arabidopsis and its expression manner in planta.";
RL Plant Physiol. 113:755-763(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-99; ARG-249 AND ALA-306.
RX PubMed=19682296; DOI=10.1111/j.1365-313x.2009.03996.x;
RA Schilmiller A.L., Stout J., Weng J.K., Humphreys J., Ruegger M.O.,
RA Chapple C.;
RT "Mutations in the cinnamate 4-hydroxylase gene impact metabolism, growth
RT and development in Arabidopsis.";
RL Plant J. 60:771-782(2009).
RN [7]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
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 (PubMed:19682296).
CC {ECO:0000250|UniProtKB:Q04468, ECO:0000269|PubMed:19682296}.
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 -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:9085570, ECO:0000269|PubMed:9085571}.
CC -!- INDUCTION: Induced by wounding. {ECO:0000269|PubMed:9085570,
CC ECO:0000269|PubMed:9085571}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U71081; AAB58356.1; -; mRNA.
DR EMBL; U71080; AAB58355.1; -; Genomic_DNA.
DR EMBL; D78596; BAA24355.1; -; mRNA.
DR EMBL; U93215; AAB63088.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08397.1; -; Genomic_DNA.
DR EMBL; AY065145; AAL38321.1; -; mRNA.
DR EMBL; BT008875; AAP68314.1; -; mRNA.
DR PIR; A84709; A84709.
DR RefSeq; NP_180607.1; NM_128601.3.
DR AlphaFoldDB; P92994; -.
DR SMR; P92994; -.
DR BioGRID; 2948; 11.
DR IntAct; P92994; 7.
DR STRING; 3702.AT2G30490.1; -.
DR PaxDb; P92994; -.
DR PRIDE; P92994; -.
DR ProteomicsDB; 246431; -.
DR EnsemblPlants; AT2G30490.1; AT2G30490.1; AT2G30490.
DR GeneID; 817599; -.
DR Gramene; AT2G30490.1; AT2G30490.1; AT2G30490.
DR KEGG; ath:AT2G30490; -.
DR Araport; AT2G30490; -.
DR TAIR; locus:2064402; AT2G30490.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; P92994; -.
DR OMA; QIRLGNC; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P92994; -.
DR BioCyc; ARA:AT2G30490-MON; -.
DR BioCyc; MetaCyc:AT2G30490-MON; -.
DR SABIO-RK; P92994; -.
DR UniPathway; UPA00825; UER00789.
DR PRO; PR:P92994; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P92994; baseline and differential.
DR Genevisible; P92994; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:TAIR.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016710; F:trans-cinnamate 4-monooxygenase activity; IDA:TAIR.
DR GO; GO:0032502; P:developmental process; IMP:TAIR.
DR GO; GO:0009808; P:lignin metabolic process; IMP:TAIR.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:TAIR.
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 Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..505
FT /note="Trans-cinnamate 4-monooxygenase"
FT /id="PRO_0000052242"
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 92
FT /note="L -> H (in strain: cv. Landsberg erecta)"
FT MUTAGEN 99
FT /note="G->E: In ref3-3; reduces lignin deposition and
FT alters lignin monomer content; dwarf phenotype, male
FT sterility and development of swellings at branch
FT junctions."
FT /evidence="ECO:0000269|PubMed:19682296"
FT MUTAGEN 249
FT /note="R->K: In ref3-2; reduces lignin deposition and
FT alters lignin monomer content; dwarf phenotype, male
FT sterility and development of swellings at branch
FT junctions."
FT /evidence="ECO:0000269|PubMed:19682296"
FT MUTAGEN 306
FT /note="A->T: In ref3-1; reduces lignin deposition and
FT alters lignin monomer content; dwarf phenotype, male
FT sterility and development of swellings at branch
FT junctions."
FT /evidence="ECO:0000269|PubMed:19682296"
FT CONFLICT 184
FT /note="N -> T (in Ref. 2; BAA24355)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="R -> G (in Ref. 2; BAA24355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 57792 MW; 61DEAAA9463362CF CRC64;
MDLLLLEKSL IAVFVAVILA TVISKLRGKK LKLPPGPIPI PIFGNWLQVG DDLNHRNLVD
YAKKFGDLFL LRMGQRNLVV VSSPDLTKEV LLTQGVEFGS RTRNVVFDIF TGKGQDMVFT
VYGEHWRKMR RIMTVPFFTN KVVQQNREGW EFEAASVVED VKKNPDSATK GIVLRKRLQL
MMYNNMFRIM FDRRFESEDD PLFLRLKALN GERSRLAQSF EYNYGDFIPI LRPFLRGYLK
ICQDVKDRRI ALFKKYFVDE RKQIASSKPT GSEGLKCAID HILEAEQKGE INEDNVLYIV
ENINVAAIET TLWSIEWGIA ELVNHPEIQS KLRNELDTVL GPGVQVTEPD LHKLPYLQAV
VKETLRLRMA IPLLVPHMNL HDAKLAGYDI PAESKILVNA WWLANNPNSW KKPEEFRPER
FFEEESHVEA NGNDFRYVPF GVGRRSCPGI ILALPILGIT IGRMVQNFEL LPPPGQSKVD
TSEKGGQFSL HILNHSIIVM KPRNC
