ID   C7A11_ARATH             Reviewed;         512 AA.
AC   Q9LUC9;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Cytochrome P450 72A11;
DE            EC=1.14.-.-;
GN   Name=CYP72A11; OrderedLocusNames=At3g14650; ORFNames=MIE1.15;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AB023038; BAB02397.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75551.1; -; Genomic_DNA.
DR   EMBL; AK228721; BAF00623.1; -; mRNA.
DR   RefSeq; NP_188083.1; NM_112326.4.
DR   AlphaFoldDB; Q9LUC9; -.
DR   SMR; Q9LUC9; -.
DR   STRING; 3702.AT3G14650.1; -.
DR   PaxDb; Q9LUC9; -.
DR   PRIDE; Q9LUC9; -.
DR   ProteomicsDB; 240534; -.
DR   EnsemblPlants; AT3G14650.1; AT3G14650.1; AT3G14650.
DR   GeneID; 820693; -.
DR   Gramene; AT3G14650.1; AT3G14650.1; AT3G14650.
DR   KEGG; ath:AT3G14650; -.
DR   Araport; AT3G14650; -.
DR   TAIR; locus:2089586; AT3G14650.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_5_0_1; -.
DR   InParanoid; Q9LUC9; -.
DR   OMA; PFGGFYF; -.
DR   OrthoDB; 825914at2759; -.
DR   PhylomeDB; Q9LUC9; -.
DR   BioCyc; ARA:AT3G14650-MON; -.
DR   PRO; PR:Q9LUC9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LUC9; baseline and differential.
DR   Genevisible; Q9LUC9; 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; IBA:GO_Central.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
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.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..512
FT                   /note="Cytochrome P450 72A11"
FT                   /id="PRO_0000425855"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         460
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;  58138 MW;  EF095098F7803517 CRC64;
     MEISVASVTV SVAVVVVSWW VWRTLQWVWF KPKMLESYLR RQGLAGTPYT PLVGDLKKNF
     SMRAEARSKP INLTDDITPR IVPYPLQMLK THGRTFFTWF GAIPTITIMD PEQITEVLNK
     VYDFQKAHTF PLGRLIATGV LSYDGDKWAK HRRIINPAFH LEKIKNMVPA FHQSCSEIVC
     KWDKLVSDKE SSCEVDVWPG LVSMTADVIS RTAFGSSCVE GQRIFELQAE LAQLIIQTVR
     KAFIPGYSYL PTKGNRRMKA KAREIQVILR GIVNKRLRAR EAGEAPNDDL LGILLESNLG
     QTKGNGMSTE DLMEECKLFY FVGQETTSVL LVWTMVLLSQ HQDWQARARE EVKQVFGDKE
     PDAEGLNQLK VMTMILYEVL RLYPPIPQLS RAIHKEMELG DLTLPGGVLI NLPILLVQRD
     TELWGNDAGE FKPDRFKDGL SKATKNQASF FPFAWGSRIC IGQNFALLEA KMAMALILQR
     FSFELSPSYV HAPYTVFTIH PQFGAPLIMH KL