ID   C71BK_ARATH             Reviewed;         502 AA.
AC   Q9LTM3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Cytochrome P450 71B20;
DE            EC=1.14.-.-;
GN   Name=CYP71B20; OrderedLocusNames=At3g26180; ORFNames=MTC11.9;
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;
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9LTM3-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB024038; BAB02439.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77130.1; -; Genomic_DNA.
DR   EMBL; AY056270; AAL07119.1; -; mRNA.
DR   EMBL; AY143938; AAN28877.1; -; mRNA.
DR   RefSeq; NP_189249.1; NM_113525.4. [Q9LTM3-1]
DR   AlphaFoldDB; Q9LTM3; -.
DR   SMR; Q9LTM3; -.
DR   STRING; 3702.AT3G26180.1; -.
DR   PaxDb; Q9LTM3; -.
DR   PRIDE; Q9LTM3; -.
DR   ProteomicsDB; 239167; -. [Q9LTM3-1]
DR   EnsemblPlants; AT3G26180.1; AT3G26180.1; AT3G26180. [Q9LTM3-1]
DR   GeneID; 822219; -.
DR   Gramene; AT3G26180.1; AT3G26180.1; AT3G26180. [Q9LTM3-1]
DR   KEGG; ath:AT3G26180; -.
DR   Araport; AT3G26180; -.
DR   TAIR; locus:2093516; AT3G26180.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; Q9LTM3; -.
DR   OMA; MTHEDID; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; Q9LTM3; -.
DR   BioCyc; ARA:AT3G26180-MON; -.
DR   PRO; PR:Q9LTM3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LTM3; baseline and differential.
DR   Genevisible; Q9LTM3; 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; IEA:UniProtKB-KW.
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; 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   Alternative splicing; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..502
FT                   /note="Cytochrome P450 71B20"
FT                   /id="PRO_0000052097"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         444
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   502 AA;  57416 MW;  074A178F40A16871 CRC64;
     MAISFLCFCL ITLASLIFFA KKIKHLKWNL PPSPPKFPVI GNLHQIGELP HRSLQHLAER
     YGPVMLLHFG FVPVTVVSSR EAAEEVLRTH DLDCCSRPKL VGTRLLSRNF KDVCFTPYGN
     EWKARRKFAL RELFCLKKVQ SFRHIREEEC NFLVKQLSES AVNRSPVDLS KSLFWLTASI
     FFRVALGQNF HESNFIDKEK IEELVFEAET ALASFTCSDF FPVAGLGWLV DWFSGQHKRL
     NDVFYKLDAL FQHVIDDHLN PGRSKEHEDI IDSMLDAIHK EGKDSSLELI IDHIKGFLAN
     IFLAGIDTGA LTMIWAMTEL VKNPKLIKKV QGEIREQLGS NKARITEEDI DKVPYLKMVI
     KETFRLHPAA PLILPRETMA HIKVQGYDIP PKRRILVNVS AIGRDPKLWT NPEEFDPERF
     MDSSVDYRGQ HYELLPFGSG RRICPGMPMG IAAVELGLLN LLYFFDWKLP DGMTHKDIDT
     EEAGTLTIVK KVPLQLVPVR VQ