C89A9_ARATH
ID C89A9_ARATH Reviewed; 511 AA.
AC Q9SRQ1; Q944R6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cytochrome P450 89A9 {ECO:0000303|PubMed:23723324};
DE EC=1.14.14.- {ECO:0000269|PubMed:23723324};
GN Name=CYP89A9 {ECO:0000303|PubMed:23723324};
GN OrderedLocusNames=At3g03470 {ECO:0000312|Araport:AT3G03470};
GN ORFNames=T21P5.11 {ECO:0000312|EMBL:AAF01588.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP REVIEW.
RX PubMed=21167811; DOI=10.1016/j.bbabio.2010.12.007;
RA Hoertensteiner S., Kraeutler B.;
RT "Chlorophyll breakdown in higher plants.";
RL Biochim. Biophys. Acta 1807:977-988(2011).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND PATHWAY.
RA Christ B., Bichsel N., Hoertensteiner S.;
RT "A cytochrome P450 monooxygenase is involved in chlorophyll breakdown in
RT Arabidopsis thaliana.";
RL Unpublished observations (JAN-2012).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, PATHWAY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=23723324; DOI=10.1105/tpc.113.112151;
RA Christ B., Suessenbacher I., Moser S., Bichsel N., Egert A., Mueller T.,
RA Kraeutler B., Hoertensteiner S.;
RT "Cytochrome P450 CYP89A9 is involved in the formation of major chlorophyll
RT catabolites during leaf senescence in Arabidopsis.";
RL Plant Cell 25:1868-1880(2013).
RN [8]
RP REVIEW.
RX PubMed=24302623; DOI=10.1002/chem.201303398;
RA Suessenbacher I., Christ B., Hoertensteiner S., Kraeutler B.;
RT "Hydroxymethylated phyllobilins: a puzzling new feature of the dioxobilin
RT branch of chlorophyll breakdown.";
RL Chemistry 20:87-92(2014).
CC -!- FUNCTION: Involved in the chlorophyll breakdown by its action in
CC nonpolar primary fluorescent chlorophyll catabolite (pFCC)
CC decarbonylation (Ref.6, PubMed:23723324). Involved in the formation of
CC major chlorophyll breakdown products, including non-fluorescent
CC dioxobilin-type chlorophyll catabolites (NDCCs), during leaf senescence
CC (PubMed:23723324). {ECO:0000269|PubMed:23723324, ECO:0000269|Ref.6}.
CC -!- CATALYTIC ACTIVITY: [Cytochrome P450 89A9]:
CC Reaction=O2 + primary fluorescent chlorophyll catabolite + reduced
CC [NADPH--hemoprotein reductase] = formate + 2 H(+) + oxidized [NADPH--
CC hemoprotein reductase] + primary fluorescent dioxobilin-type
CC chlorophyll catabolite; Xref=Rhea:RHEA:67172, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:77670, ChEBI:CHEBI:167885;
CC Evidence={ECO:0000269|PubMed:23723324};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC degradation. {ECO:0000269|PubMed:23723324, ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23723324, ECO:0000269|Ref.6}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impaired accumulation of non-fluorescent
CC dioxobilin-type chlorophyll catabolites (NDCCs) compensated by higher
CC amounts of non-fluorescent chlorophyll catabolites (NCCs) in senescing
CC leaves. {ECO:0000269|PubMed:23723324}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AC009895; AAF01588.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73948.1; -; Genomic_DNA.
DR EMBL; AF424581; AAL11575.1; -; mRNA.
DR EMBL; BT015915; AAU95451.1; -; mRNA.
DR RefSeq; NP_186997.1; NM_111218.4.
DR AlphaFoldDB; Q9SRQ1; -.
DR SMR; Q9SRQ1; -.
DR STRING; 3702.AT3G03470.1; -.
DR PaxDb; Q9SRQ1; -.
DR PRIDE; Q9SRQ1; -.
DR ProteomicsDB; 223857; -.
DR EnsemblPlants; AT3G03470.1; AT3G03470.1; AT3G03470.
DR GeneID; 821250; -.
DR Gramene; AT3G03470.1; AT3G03470.1; AT3G03470.
DR KEGG; ath:AT3G03470; -.
DR Araport; AT3G03470; -.
DR TAIR; locus:2099714; AT3G03470.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9SRQ1; -.
DR OMA; AIMVKYP; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9SRQ1; -.
DR BioCyc; ARA:AT3G03470-MON; -.
DR UniPathway; UPA00674; -.
DR PRO; PR:Q9SRQ1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRQ1; baseline and differential.
DR Genevisible; Q9SRQ1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0106371; F:fluorescent chlorophyll catabolite monooxygenase (deformylase) activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IMP:UniProtKB.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IMP:UniProtKB.
DR GO; GO:0033310; P:chlorophyll a catabolic process; IDA:TAIR.
DR GO; GO:0015996; P:chlorophyll catabolic process; IMP:UniProtKB.
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 Chlorophyll catabolism; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..511
FT /note="Cytochrome P450 89A9"
FT /id="PRO_0000416128"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 454
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:Q96242"
FT CONFLICT 385
FT /note="H -> R (in Ref. 3; AAL11575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 59255 MW; 92B0488E7B204034 CRC64;
MEITTIIFLI ISSLTFSIFL KLIFFFSTHK LPPGPPRFPV IGNIIWLKKN NFSDFQGVLR
DLASRHGPII TLHVGSKPSI WVTDRSLAHQ ALVQNGAVFS DRSLALPTTK VITSNQHDIH
SSVYGSLWRT LRRNLTSEIL QPSRVKAHAP SRKWSLEILV DLFETEQREK GHISDALDHL
RHAMFYLLAL MCFGEKLRKE EIREIEEAQY QMLISYTKFS VLNIFPSVTK FLLRRKWKEF
LELRKSQESV ILRYVNARSK ETTGDVLCYV DTLLNLEIPT EEKEGGKKRK LSDSEIVSLC
SEFLNAATDP TATSMQWIMA IMVKYPEIQR KVYEEMKTVF AGEEEEREEI REEDLGKLSY
LKAVILECLR RHPPGHYLSY HKVTHDTVLG GFLIPRQGTI NFMVGEMGRD PKIWEDPLTF
KPERFLENGE ACDFDMTGTR EIKMMPFGAG RRMCPGYALS LLHLEYYVAN LVWKFEWKCV
EGEEVDLSEK QQFITMVMKN PFKANIYPRR K
