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C71BM_ARATH
ID   C71BM_ARATH             Reviewed;         500 AA.
AC   Q9LTM1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Cytochrome P450 71B22;
DE            EC=1.14.-.-;
GN   Name=CYP71B22; OrderedLocusNames=At3g26200; ORFNames=MTC11.11;
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB024038; BAB02441.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77133.1; -; Genomic_DNA.
DR   EMBL; AF360271; AAK25981.1; -; mRNA.
DR   EMBL; AY040080; AAK64138.1; -; mRNA.
DR   RefSeq; NP_189251.1; NM_113527.2.
DR   AlphaFoldDB; Q9LTM1; -.
DR   SMR; Q9LTM1; -.
DR   BioGRID; 7552; 7.
DR   IntAct; Q9LTM1; 7.
DR   STRING; 3702.AT3G26200.1; -.
DR   PaxDb; Q9LTM1; -.
DR   PRIDE; Q9LTM1; -.
DR   ProteomicsDB; 240530; -.
DR   EnsemblPlants; AT3G26200.1; AT3G26200.1; AT3G26200.
DR   GeneID; 822221; -.
DR   Gramene; AT3G26200.1; AT3G26200.1; AT3G26200.
DR   KEGG; ath:AT3G26200; -.
DR   Araport; AT3G26200; -.
DR   TAIR; locus:2093521; AT3G26200.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_1_1; -.
DR   InParanoid; Q9LTM1; -.
DR   OMA; CTRPKLT; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; Q9LTM1; -.
DR   BioCyc; ARA:AT3G26200-MON; -.
DR   PRO; PR:Q9LTM1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LTM1; baseline and differential.
DR   Genevisible; Q9LTM1; 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   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..500
FT                   /note="Cytochrome P450 71B22"
FT                   /id="PRO_0000052099"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         441
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   500 AA;  57033 MW;  5C70FBE542B1C6CE CRC64;
     MSISLYFLLL LPLFLIFFKK LSPSKGKLPP GPLGLPIIGN LHQLGKSLHR SFHKLSQNYG
     PVMFLHFGVV PVVVVSTREA AEEVLKTHDL ETCTRPKLTA TKLFSYNYKD IGFAQYGDDW
     REMRKLAMLE LFSSKKLKAF RYIREEESEV LVNKLSKSAE TRTMVDLRKA LFSYTASIVC
     RLAFGQNFHE CDFVDMDKVE DLVLESETNL GSFAFTDFFP AGLGWVIDRI SGQHSELHKA
     FARLSNFFQH VIDDHLKPGQ SQDHSDIIGV MLDMINKESK VGSFQVTYDH LKGVMSDVFL
     AGVNAGAITM IWAMTELARH PRVMKKLQQE IREILGDNKE KITEQDLEKV HYLKLVIEET
     FRLHPPAPLL LPRETMSDLK IQGYNIPKNT MIEINTYSIG RDPNCWENPN DFNPERFIDS
     PVEYKGQHYE LLPFGAGRRI CPGMATGITI VELGLLNVLY FFDWSLPDGM KIEDIDMEEA
     GAFVVAKKVP LELIPTPHQW
 
 
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