ID   C98A9_ARATH             Reviewed;         487 AA.
AC   Q9CA60;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Cytochrome P450 98A9;
DE            EC=1.14.-.-;
DE   AltName: Full=p-coumarate 3-hydroxylase;
GN   Name=CYP98A9; OrderedLocusNames=At1g74550; ORFNames=F1M20.23;
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].
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   [4]
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   [5]
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 CYP98A8 as tricoumaroylspermidine meta-
CC       hydroxylase. Involved in phenolamide synthesis, but a recombinant
CC       CYP98A9 is unable to hydroxylate triferuloylspermidine. Unable to use
CC       5-O-(4-coumaroyl) D-quinate or 5-O-(4-coumaroyl) shikimate as
CC       substrates. {ECO:0000269|PubMed:11429408, 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 root tips, inflorescence
CC       tips, young flower buds, stamen, tapetum and pollen. Detected in aging
CC       vasculature. {ECO:0000269|PubMed:19779199}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AC011765; AAG52373.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35608.1; -; Genomic_DNA.
DR   EMBL; AY086275; AAM67314.1; -; mRNA.
DR   PIR; F96774; F96774.
DR   RefSeq; NP_177595.1; NM_106115.3.
DR   AlphaFoldDB; Q9CA60; -.
DR   SMR; Q9CA60; -.
DR   STRING; 3702.AT1G74550.1; -.
DR   PaxDb; Q9CA60; -.
DR   PRIDE; Q9CA60; -.
DR   EnsemblPlants; AT1G74550.1; AT1G74550.1; AT1G74550.
DR   GeneID; 843796; -.
DR   Gramene; AT1G74550.1; AT1G74550.1; AT1G74550.
DR   KEGG; ath:AT1G74550; -.
DR   Araport; AT1G74550; -.
DR   TAIR; locus:2019250; AT1G74550.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_0_1; -.
DR   InParanoid; Q9CA60; -.
DR   OMA; PREHIDM; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; Q9CA60; -.
DR   BioCyc; ARA:AT1G74550-MON; -.
DR   PRO; PR:Q9CA60; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CA60; baseline and differential.
DR   Genevisible; Q9CA60; 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: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:0072547; F:tricoumaroylspermidine meta-hydroxylase activity; IDA:TAIR.
DR   GO; GO:0008216; P:spermidine metabolic process; IDA: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..487
FT                   /note="Cytochrome P450 98A9"
FT                   /id="PRO_0000419517"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         425
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   487 AA;  55419 MW;  B5521947A5F97F03 CRC64;
     MDLLLISLTT IIIAAYMQNL RRRGSNIPPG PPTRFLVGNL HQLKPLWTQS FSEWSQTYGP
     IISVWLGSQL AVVVSSSDLA KQVLRDKDYQ LCNRHRTARM TQNGSDLIWS DYGAHYVKMR
     KLCTLELFSL KSIECFRSMR EMEVSSMVKS IFNDFMSDDQ KPVVLRNYLD SVALNIVSRL
     VIGKTFEPKD GREFRSIVER ETRLPGATKM LDYTVWLKRL SSWFTSDKAF MKHMARKRNW
     FKRAVMDEVY GGRDQKCFVQ SLLELKEKDE LTEETVMGLV WNMLTAGADT TAITIEWAMA
     EMIRCPTVKE KVQDELDSVV GSGRLMSDAD IPKLPFLQCV LKEALRLHPP TPLMLPHKAS
     ESVQVGGYKV PKGATVYVNV QAIARDPANW SNPDEFRPER FLVEETDVKG QDFRVLPFGS
     GRRVCPAAQL SLNMMTLALG SLLHCFSWTS STPREHIDMT EKPGLVCYMK APLQALASSR
     LPQELYL