C89A2_ARATH
ID C89A2_ARATH Reviewed; 506 AA.
AC Q42602; Q9XIQ6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cytochrome P450 89A2;
DE EC=1.14.-.-;
DE AltName: Full=ATH 6-1;
DE AltName: Full=CYPLXXXIX;
GN Name=CYP89A2; Synonyms=CYP89; OrderedLocusNames=At1g64900;
GN ORFNames=F13O11.20;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Courtney K.J., Percival F.W., Hallahan D.L., Christoffersen R.E.;
RT "Cloning and sequencing of a cytochrome P450, CYP89, from Arabidopsis
RT thaliana.";
RL (er) Plant Gene Register PGR96-061(1996).
RN [2]
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 [3]
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 [4]
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).
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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB67854.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U61231; AAB67854.1; ALT_FRAME; mRNA.
DR EMBL; AC006193; AAD38264.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34303.1; -; Genomic_DNA.
DR EMBL; BT002531; AAO00891.1; -; mRNA.
DR EMBL; BT010377; AAQ56820.1; -; mRNA.
DR PIR; D96672; D96672.
DR RefSeq; NP_176670.1; NM_105164.3.
DR AlphaFoldDB; Q42602; -.
DR SMR; Q42602; -.
DR BioGRID; 28019; 4.
DR IntAct; Q42602; 4.
DR STRING; 3702.AT1G64900.1; -.
DR PaxDb; Q42602; -.
DR PRIDE; Q42602; -.
DR ProteomicsDB; 240456; -.
DR EnsemblPlants; AT1G64900.1; AT1G64900.1; AT1G64900.
DR GeneID; 842798; -.
DR Gramene; AT1G64900.1; AT1G64900.1; AT1G64900.
DR KEGG; ath:AT1G64900; -.
DR Araport; AT1G64900; -.
DR TAIR; locus:2010781; AT1G64900.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q42602; -.
DR OMA; FMGEEVF; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q42602; -.
DR BioCyc; ARA:AT1G64900-MON; -.
DR PRO; PR:Q42602; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42602; baseline and differential.
DR Genevisible; Q42602; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; 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 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..506
FT /note="Cytochrome P450 89A2"
FT /id="PRO_0000052182"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 449
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 17
FT /note="L -> F (in Ref. 1; AAB67854)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="E -> D (in Ref. 1; AAB67854)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="E -> Q (in Ref. 1; AAB67854)"
FT /evidence="ECO:0000305"
FT CONFLICT 212..213
FT /note="TK -> SR (in Ref. 1; AAB67854)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="V -> I (in Ref. 1; AAB67854)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="Q -> E (in Ref. 1; AAB67854)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="V -> L (in Ref. 1; AAB67854)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="Q -> E (in Ref. 1; AAB67854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 58605 MW; 8B39794DAE011E62 CRC64;
MEIWLLILAS LSGSLLLHLL LRRRNSSSPP LPPDPNFLPF LGTLQWLREG LGGLESYLRS
VHHRLGPIVT LRITSRPAIF VADRSLTHEA LVLNGAVYAD RPPPAVISKI VDEHNISSGS
YGATWRLLRR NITSEILHPS RVRSYSHARH WVLEILFERF RNHGGEEPIV LIHHLHYAMF
ALLVLMCFGD KLDEKQIKEV EFIQRLQLLS LTKFNIFNIW PKFTKLILRK RWQEFLQIRR
QQRDVLLPLI RARRKIVEER KRSEQEDKKD YVQSYVDTLL DLELPEENRK LNEEDIMNLC
SEFLTAGTDT TATALQWIMA NLVKYPEIQE RLHEEIKSVV GEEAKEVEEE DVEKMPYLKA
VVLEGLRRHP PGHFLLPHSV TEDTVLGGYK VPKNGTINFM VAEIGRDPVE WEEPMAFKPE
RFMGEEEAVD LTGSRGIKMM PFGAGRRICP GIGLAMLHLE YYVANMVREF QWKEVQGHEV
DLTEKLEFTV VMKHPLKALA VPRRCH
