ID   C71BP_ARATH             Reviewed;         501 AA.
AC   Q9LTL2; Q1PEL4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Cytochrome P450 71B25;
DE            EC=1.14.-.-;
GN   Name=CYP71B25; OrderedLocusNames=At3g26270; ORFNames=MTC11.20;
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 [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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
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; BAB02450.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77140.1; -; Genomic_DNA.
DR   EMBL; DQ446703; ABE65971.1; -; mRNA.
DR   RefSeq; NP_189258.1; NM_113534.1.
DR   AlphaFoldDB; Q9LTL2; -.
DR   SMR; Q9LTL2; -.
DR   PaxDb; Q9LTL2; -.
DR   PRIDE; Q9LTL2; -.
DR   EnsemblPlants; AT3G26270.1; AT3G26270.1; AT3G26270.
DR   GeneID; 822230; -.
DR   Gramene; AT3G26270.1; AT3G26270.1; AT3G26270.
DR   KEGG; ath:AT3G26270; -.
DR   Araport; AT3G26270; -.
DR   TAIR; locus:2093526; AT3G26270.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_1_1; -.
DR   InParanoid; Q9LTL2; -.
DR   OMA; ERFINCP; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; Q9LTL2; -.
DR   BioCyc; ARA:AT3G26270-MON; -.
DR   PRO; PR:Q9LTL2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LTL2; baseline and differential.
DR   Genevisible; Q9LTL2; 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..501
FT                   /note="Cytochrome P450 71B25"
FT                   /id="PRO_0000052102"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         445
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   501 AA;  57535 MW;  A9C880F285C9E4D9 CRC64;
     MAILQSFLLL LSLPFLFTLI YTKKMKESKR NLPPGPAKLP IVGNLHQLQG MVHRCLHELS
     KKHGPVMHLQ LGFVPLVLIS SSEAAEEALK THDIECCTRP NTNAARVFSR NNKNIGLGAY
     SDEWRELRKV AVREYFSVKK VQSFRYVREE ENHLMVKKLR DLALKQSPVD LSKTLFCLAA
     STVFRPVFGQ SFSDNKHFSE EKIEELVFEA QKSLTFKFSD LFPIPGLGWF IGFVSGQHKG
     LHKVFIEVDN FLNHMIDDHQ KQNQPQDRSD IVGSLLDMIH NQEQDKSFKL TIDHLKGITQ
     DIFLAGIDTS AITMIWAMAE LVNNPRVMKK VQDEIRSCIG IKKERIEEED VGKLQYLKLV
     IKETLRLHPA APLLLPRETM ADIKIQGYDI PRKTLLLVSA WSLGRDPKYW KNPEEFNPER
     FIDCPVDYKG HSFEFLPFGS GRRFCPGMAS AIATIELTLL NLLYFFDWKL PEEMKDMNME
     ESGDVTIVKK VPLELLPVLY H