C84A4_ARATH
ID C84A4_ARATH Reviewed; 512 AA.
AC F4JW83; Q9LKP9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Cytochrome P450 84A4;
DE EC=1.14.-.-;
GN Name=CYP84A4; OrderedLocusNames=At5g04330; ORFNames=T19N18.60;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-447.
RA Rees J.D., Bolwell G.P.;
RT "Arabidopsis thaliana (CYP84), partial genomic sequence.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, 3D-STRUCTURE MODELING, AND TISSUE SPECIFICITY.
RX PubMed=22923580; DOI=10.1126/science.1221614;
RA Weng J.K., Li Y., Mo H., Chapple C.;
RT "Assembly of an evolutionarily new pathway for alpha-pyrone biosynthesis in
RT Arabidopsis.";
RL Science 337:960-964(2012).
CC -!- FUNCTION: Cytochrome P450 involved in the production of catechol-
CC substituted substrates needed for the arabidopyrones biosynthesis.
CC Converts p-coumaraldehyde into caffealdehyde.
CC {ECO:0000269|PubMed:22923580}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41 uM for p-coumaraldehyde {ECO:0000269|PubMed:22923580};
CC Vmax=0.69 pmol/sec/mg enzyme {ECO:0000269|PubMed:22923580};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems and
CC inflorescence nodes. Low or no expression in leaves, flowers, seeds and
CC lignifying tissue. {ECO:0000269|PubMed:22923580}.
CC -!- DISRUPTION PHENOTYPE: Deficient in arabidopyrones, but normal amounts
CC of sinapate esters. {ECO:0000269|PubMed:22923580}.
CC -!- MISCELLANEOUS: Arabidopyrones are derived from phenylalanine instead of
CC tyrosine like other ring-cleavage-derived plant metabolites.
CC {ECO:0000305|PubMed:22923580}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CP002688; AED90728.1; -; Genomic_DNA.
DR EMBL; AF267140; AAF78943.1; -; Genomic_DNA.
DR RefSeq; NP_196053.2; NM_120515.3.
DR AlphaFoldDB; F4JW83; -.
DR SMR; F4JW83; -.
DR STRING; 3702.AT5G04330.1; -.
DR PaxDb; F4JW83; -.
DR PRIDE; F4JW83; -.
DR ProteomicsDB; 240238; -.
DR EnsemblPlants; AT5G04330.1; AT5G04330.1; AT5G04330.
DR GeneID; 830312; -.
DR Gramene; AT5G04330.1; AT5G04330.1; AT5G04330.
DR KEGG; ath:AT5G04330; -.
DR Araport; AT5G04330; -.
DR TAIR; locus:2179959; AT5G04330.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; F4JW83; -.
DR OMA; DLAFCNY; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-19383; -.
DR PRO; PR:F4JW83; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JW83; baseline and differential.
DR Genevisible; F4JW83; AT.
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:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0009809; P:lignin biosynthetic process; IBA:GO_Central.
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..512
FT /note="Cytochrome P450 84A4"
FT /id="PRO_0000424077"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 512 AA; 57955 MW; 901A88C42451FAB5 CRC64;
MLTLMTLIVL VPLLLFLFPH LLLRRQMLLK PYPPGPKGLP VIGNILMMNQ FNHRGLAKLS
RIYGGLLHLR LGFSHIFVVS SPDIARQVLQ VQDHVFSNRP TTIAIRYLTY GGSDLAFCNY
GPFWRRMRKL YVMMLFSRKR AESWVSVDEE VHKSVRLVAS NVGKPLNICK LAFSLSRDIT
FRAAFGSSSS TSDESRLDEF LEIIQEFSKL FGEFNVADYV PSWLSWIDPQ GINGRVEKAR
KSLDGFIESV IDDHLHKKKR EHDNVDEETD MVDQLLAFYE EEVKVNNSVT KINLDNIKGI
IMDVMFGGTE TVALAIEWVL TEILRSPENM KRVQDELTSV VGLDRWRVED THLEKLTFLK
CILKETLRLH PPFPLLLHET VKDTEISGYF IPKGSRVMVN TYALGRDPNS WSDPESFNPG
RFLNPIAPDL KGNNFEFVPF GSGRRSCPGM QLGLYAFELA VAHLLHCFTW SLPDGMNPGD
VDTVEGPGLT VPKAIPLVAV PTTRLLCPIV VS
