ID   C76C4_ARATH             Reviewed;         511 AA.
AC   O64635;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Cytochrome P450 76C4;
DE            EC=1.14.-.-;
GN   Name=CYP76C4; OrderedLocusNames=At2g45550; ORFNames=F17K2.8;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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}.
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DR   EMBL; AC003680; AAC06156.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10569.1; -; Genomic_DNA.
DR   PIR; T00868; T00868.
DR   RefSeq; NP_182079.1; NM_130117.2.
DR   AlphaFoldDB; O64635; -.
DR   SMR; O64635; -.
DR   STRING; 3702.AT2G45550.1; -.
DR   PaxDb; O64635; -.
DR   PRIDE; O64635; -.
DR   EnsemblPlants; AT2G45550.1; AT2G45550.1; AT2G45550.
DR   GeneID; 819163; -.
DR   Gramene; AT2G45550.1; AT2G45550.1; AT2G45550.
DR   KEGG; ath:AT2G45550; -.
DR   Araport; AT2G45550; -.
DR   TAIR; locus:2043694; AT2G45550.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_2_1; -.
DR   InParanoid; O64635; -.
DR   OMA; ANYFPFM; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; O64635; -.
DR   BioCyc; ARA:AT2G45550-MON; -.
DR   PRO; PR:O64635; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O64635; baseline and differential.
DR   Genevisible; O64635; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0102311; F:8-hydroxygeraniol dehydrogenase activity; IDA:TAIR.
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..511
FT                   /note="Cytochrome P450 76C4"
FT                   /id="PRO_0000052144"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         450
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   511 AA;  56933 MW;  D8068676DE975A9B CRC64;
     MDIISGQALF LLFCFISSCF LISTTARSRR SSGRAATLPP GPPRLPIIGN IHQVGKNPHS
     SFADLAKIYG PIMSLKFGCL NSVVITSPEA AREVLRTHDQ ILSGRKSNDS IRCFGHEEVS
     VIWLPPSSAR WRMLRKLSVT LMFSPQRTEA TKALRMKKVQ ELVSFMNESS ERKEAVDISR
     ASYTTVLNII SNILFSVDLG SYDSKKSNEF QDTVIGAMEA AGKPDAANYF PFMGFLDLQG
     NRKAMRGLTE RLFRVFRGFM DAKIAEKSLG NYSKDVSNRD FLDSLLILNE GDEAELDNND
     IEHLLLDMFT AGTDTSSSTL EWAMAELLRN PKTMVKAQAE MDRVLGQNSV VQESDISGLP
     YLQAVVKETF RLHPAAPLLV PRKAESDVEV LGFMVPKDTQ VLVNVWAIGR DPSVWENPSQ
     FEPERFMGKD IDVKGRDYEL TPFGGGRRIC PGLPLAVKTV SLMLASLLYS FDWKLPNGVV
     SEDLDMDETF GITLHRTNTL YAIPVKKQTI N