ID   C71B8_ARATH             Reviewed;         506 AA.
AC   P58048; F4K1E1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Cytochrome P450 71B8;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450, family 71, subfamily B, polypeptide 8;
GN   Name=CYP71B8; OrderedLocusNames=At5g35715; ORFNames=MXH1.7;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
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).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AB011485; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AED94008.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AED94008.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB011485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED94008.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_680342.2; NM_148037.2.
DR   AlphaFoldDB; P58048; -.
DR   SMR; P58048; -.
DR   BioGRID; 18799; 1.
DR   IntAct; P58048; 1.
DR   STRING; 3702.AT5G35715.1; -.
DR   PaxDb; P58048; -.
DR   PeptideAtlas; P58048; -.
DR   PRIDE; P58048; -.
DR   ProteomicsDB; 240389; -.
DR   EnsemblPlants; AT5G35715.1; AT5G35715.1; AT5G35715.
DR   GeneID; 833546; -.
DR   Gramene; AT5G35715.1; AT5G35715.1; AT5G35715.
DR   KEGG; ath:AT5G35715; -.
DR   Araport; AT5G35715; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_1_1; -.
DR   InParanoid; P58048; -.
DR   OrthoDB; 561463at2759; -.
DR   PhylomeDB; P58048; -.
DR   BioCyc; ARA:AT5G35715-MON; -.
DR   PRO; PR:P58048; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P58048; baseline and differential.
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   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..506
FT                   /note="Cytochrome P450 71B8"
FT                   /id="PRO_0000052086"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         443
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   506 AA;  57970 MW;  8D2DD8A920998986 CRC64;
     MIKSILLCFF FLFPLLLTLF KKLLPSKWKL PPGPTGLPII GNLHQLGRLL HSSFHKLSLE
     HGPVMLLRFG VVPMVVISSK EAAKQVLKSR DLETCSRPKL VANGLFTRNF KDIAFAQYGE
     DWREMKKLVG LELFNPKKHK FFRYIREEEG DLLVKKLSKS SQTQTLVDLR KAFFSFTAGI
     IFRVSFGQNF RECDFIDMDR LEELVQESET NVFSFAFTDF FPTGLGWLVD RISGQHSRIE
     KAFSKLTKFF QHVIDEELKI GQSQDHSNLV SSMLDMINRS TEYGSFKITS DHLIAMMTDI
     VLGGVNAGTI TMIWTMTELT RHPRVMKKLR EEIRATLGPN KERITEEDLE KVEYLKLVIK
     ETFRLHPPGP FLLPRQVMSD IEIQGYHIPK NAHIKISTYA IGRDPKCWTN PEEFNPERFA
     NTSINYKGQH YELLPFGAGR RSCPGMTLGI TILELGLLNI LYYFDWSLPN GMTIKDIDME
     EDGALTIAKK VPLELIPTLP ASLCIK