ID   C71BJ_ARATH             Reviewed;         502 AA.
AC   Q9LTM4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cytochrome P450 71B19;
DE            EC=1.14.-.-;
GN   Name=CYP71B19; OrderedLocusNames=At3g26170; ORFNames=MTC11.8;
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   -!- INTERACTION:
CC       Q9LTM4; P59220: CAM7; NbExp=2; IntAct=EBI-1239070, EBI-1236031;
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; BAB02438.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77129.1; -; Genomic_DNA.
DR   EMBL; BT005891; AAO64826.1; -; mRNA.
DR   RefSeq; NP_189248.1; NM_113524.5.
DR   AlphaFoldDB; Q9LTM4; -.
DR   SMR; Q9LTM4; -.
DR   BioGRID; 7549; 11.
DR   IntAct; Q9LTM4; 11.
DR   STRING; 3702.AT3G26170.1; -.
DR   PaxDb; Q9LTM4; -.
DR   PRIDE; Q9LTM4; -.
DR   ProteomicsDB; 240499; -.
DR   EnsemblPlants; AT3G26170.1; AT3G26170.1; AT3G26170.
DR   GeneID; 822218; -.
DR   Gramene; AT3G26170.1; AT3G26170.1; AT3G26170.
DR   KEGG; ath:AT3G26170; -.
DR   Araport; AT3G26170; -.
DR   TAIR; locus:2093511; AT3G26170.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_1_1; -.
DR   InParanoid; Q9LTM4; -.
DR   OMA; ANELMHV; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; Q9LTM4; -.
DR   BioCyc; ARA:AT3G26170-MON; -.
DR   PRO; PR:Q9LTM4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LTM4; baseline and differential.
DR   Genevisible; Q9LTM4; 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   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..502
FT                   /note="Cytochrome P450 71B19"
FT                   /id="PRO_0000052096"
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;  57519 MW;  1B45401B4DBBB488 CRC64;
     MAISFLCVFL ITFVSLIFFA KKIKRSKWNL PPSPPKFPVI GNLHQIGELP HRSLQHLAER
     YGPVMLLHFG FVPITVVSSR EAAEEVLRTH DLDCCSRPKL VGTRLLSRDF KDIGFTPYGN
     EWKARRKFAL RELFCLKKVQ SFRHIREEEC NFLVKQLSES AVDRSPVDLS KSLFWLTASI
     LFRVALGQNF HESDFIDKEK IEELVFEAET ALASFTCSDF FPVAGLGWLV DWFSGQHKRL
     NDVFYKLDAL FQHVIDDHLN PGRSKEHEDI IDSMLDVIHK QGEDSSLELT IDHIKGFLAN
     IFLAGIDTGA ITMIWAVTEL VKNPKLIKKV QGDIREQLGS NKERITEEDI EKVPYLKMVI
     KETFRLHPAA PLILPRETMA HIKVQGYDIP PKRRILVNVS AIGRDPKLWT NPKEFDPERF
     MDSFVDYRGQ HYELLPFGSG RRICPGMPMG IAAVELGLLN LLYFFDWKLP DGMTHKDIDT
     EEAGTLTIVK KVPLKLVPVR VQ