C98A8_ARATH
ID C98A8_ARATH Reviewed; 497 AA.
AC Q9CA61; A0MEG3; Q8L9A4;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cytochrome P450 98A8;
DE EC=1.14.-.-;
DE AltName: Full=p-coumarate 3-hydroxylase;
GN Name=CYP98A8; OrderedLocusNames=At1g74540; ORFNames=F1M20.22;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=11429408; DOI=10.1074/jbc.m104047200;
RA Schoch G., Goepfert S., Morant M., Hehn A., Meyer D., Ullmann P.,
RA Werck-Reichhart D.;
RT "CYP98A3 from Arabidopsis thaliana is a 3'-hydroxylase of phenolic esters,
RT a missing link in the phenylpropanoid pathway.";
RL J. Biol. Chem. 276:36566-36574(2001).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19762055; DOI=10.1016/j.phytochem.2009.08.010;
RA Fellenberg C., Boettcher C., Vogt T.;
RT "Phenylpropanoid polyamine conjugate biosynthesis in Arabidopsis thaliana
RT flower buds.";
RL Phytochemistry 70:1392-1400(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, 3D-STRUCTURE MODELING, AND TISSUE
RP SPECIFICITY.
RX PubMed=19779199; DOI=10.1126/science.1174095;
RA Matsuno M., Compagnon V., Schoch G.A., Schmitt M., Debayle D.,
RA Bassard J.E., Pollet B., Hehn A., Heintz D., Ullmann P., Lapierre C.,
RA Bernier F., Ehlting J., Werck-Reichhart D.;
RT "Evolution of a novel phenolic pathway for pollen development.";
RL Science 325:1688-1692(2009).
CC -!- FUNCTION: Acts redundantly with CYP98A9 as tricoumaroylspermidine meta-
CC hydroxylase. Catalyzes also the meta-hydroxylation of the three
CC triferuloylspermidine phenolic rings. Unable to use 5-O-(4-coumaroyl)
CC D-quinate or 5-O-(4-coumaroyl) shikimate as substrates.
CC {ECO:0000269|PubMed:11429408, ECO:0000269|PubMed:19762055,
CC ECO:0000269|PubMed:19779199}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in inflorescence tips, young
CC flower buds, seeds, stamen, tapetum and pollen.
CC {ECO:0000269|PubMed:19762055, ECO:0000269|PubMed:19779199}.
CC -!- DISRUPTION PHENOTYPE: Drastic reduction in flower buds of the content
CC in N1,N5,N10-tri-(hydroxyferuloyl)-spermidine and N1,N5-
CC di(hydroxyferuloyl)-N10-sinapoyl-spermidine.
CC {ECO:0000269|PubMed:19762055}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28467.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC011765; AAG52369.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35607.1; -; Genomic_DNA.
DR EMBL; DQ446429; ABE65772.1; -; mRNA.
DR EMBL; DQ652933; ABK28467.1; ALT_SEQ; mRNA.
DR EMBL; AY088555; AAM66087.1; -; mRNA.
DR PIR; E96774; E96774.
DR RefSeq; NP_177594.1; NM_106114.2.
DR AlphaFoldDB; Q9CA61; -.
DR SMR; Q9CA61; -.
DR STRING; 3702.AT1G74540.1; -.
DR PaxDb; Q9CA61; -.
DR PRIDE; Q9CA61; -.
DR ProteomicsDB; 223860; -.
DR EnsemblPlants; AT1G74540.1; AT1G74540.1; AT1G74540.
DR GeneID; 843795; -.
DR Gramene; AT1G74540.1; AT1G74540.1; AT1G74540.
DR KEGG; ath:AT1G74540; -.
DR Araport; AT1G74540; -.
DR TAIR; locus:2019240; AT1G74540.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9CA61; -.
DR OMA; HRIARMT; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9CA61; -.
DR BioCyc; ARA:AT1G74540-MON; -.
DR BioCyc; MetaCyc:AT1G74540-MON; -.
DR PRO; PR:Q9CA61; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA61; differential.
DR Genevisible; Q9CA61; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0072548; F:dicoumaroyl monocaffeoyl spermidine meta-hydroxylase activity; IDA:TAIR.
DR GO; GO:0072551; F:diferuloyl mono-(hydroxyferuloyl) spermidine meta-hydroxylase activity; IMP:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0072549; F:monocoumaroyl dicaffeoyl spermidine meta-hydroxylase activity; IDA:TAIR.
DR GO; GO:0072552; F:monoferuloyl di-(hydroxyferuloyl) spermidine meta-hydroxylase activity; IMP:TAIR.
DR GO; GO:0072532; F:tri-(feruloyl or hydroxyferuloyl) spermidine meta-hydroxylase activity; IDA:TAIR.
DR GO; GO:0072547; F:tricoumaroylspermidine meta-hydroxylase activity; IDA:TAIR.
DR GO; GO:0072550; F:triferuloylspermidine meta-hydroxylase activity; IMP:TAIR.
DR GO; GO:0080088; P:spermidine hydroxycinnamate conjugate biosynthetic process; IDA:TAIR.
DR GO; GO:0008216; P:spermidine metabolic 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..497
FT /note="Cytochrome P450 98A8"
FT /id="PRO_0000419516"
FT TRANSMEM 2..19
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 431
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"
FT CONFLICT 211
FT /note="G -> D (in Ref. 4; AAM66087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 56741 MW; 490ABBBE46F46C99 CRC64;
MIIYLISLLP IIVATLMLYQ RWWRSNIPPG PKPKFLLGNL HQMKPLWTHS FSEWSETYGP
IISVWIGSQL TVVVSSSDLA RQVLRDKDHQ LSNRHRIARM TQTGTDLVWS DYSPHYVKLR
KLCTLELFSL KSIENFRSLR EMEARSMVVS ILKDLMSNSG DDQERKPVIV RKYLAAVVLN
TISRLMIGKE FGSEEGKEFK AIVEKEHLLS GSGTILDHVW WLKWVSSWFF SDKEFLAHKD
RRTKWFRGAI MVEEDIEIED HRGFVRKLLV LKEQKELSEE TVGGLVWNML TAGADTTAVV
IEWAMAEMIK CPTVQEKAQQ ELDSVVGSER LMTESDIPIL PYLQCVVKEA LRLHPSTPLM
LPHKASETVW VGGYKVPKGA TVYVNVQAIG RDPANWINPY EFRPERFLQE ETDVKGRDFR
VLPFGSGRRM CPAAQLSMNL MTLVMGNLLH CFSWSSPVPG ERIDMSENPG LLCNMRTPLQ
ALALPRAAAR AIPLPLD
