ID   C705C_ARATH             Reviewed;         499 AA.
AC   Q9FH67;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Cytochrome P450 705A12 {ECO:0000303|PubMed:21876149};
DE            EC=1.14.-.- {ECO:0000305};
GN   Name=CYP705A12 {ECO:0000303|PubMed:21876149};
GN   OrderedLocusNames=At5g42580 {ECO:0000312|Araport:AT5G42580};
GN   ORFNames=K16E1.5 {ECO:0000312|EMBL:BAB09329.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(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   FUNCTION.
RX   PubMed=21876149; DOI=10.1073/pnas.1109273108;
RA   Field B., Fiston-Lavier A.S., Kemen A., Geisler K., Quesneville H.,
RA   Osbourn A.E.;
RT   "Formation of plant metabolic gene clusters within dynamic chromosomal
RT   regions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:16116-16121(2011).
CC   -!- FUNCTION: May be involved in hydroxylation of the triterpene marneral.
CC       {ECO:0000305|PubMed:21876149}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB022210; BAB09329.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94831.1; -; Genomic_DNA.
DR   RefSeq; NP_199072.1; NM_123622.2.
DR   AlphaFoldDB; Q9FH67; -.
DR   SMR; Q9FH67; -.
DR   STRING; 3702.AT5G42580.1; -.
DR   PaxDb; Q9FH67; -.
DR   PRIDE; Q9FH67; -.
DR   ProteomicsDB; 240562; -.
DR   EnsemblPlants; AT5G42580.1; AT5G42580.1; AT5G42580.
DR   GeneID; 834265; -.
DR   Gramene; AT5G42580.1; AT5G42580.1; AT5G42580.
DR   KEGG; ath:AT5G42580; -.
DR   Araport; AT5G42580; -.
DR   TAIR; locus:2152696; AT5G42580.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_0_1; -.
DR   InParanoid; Q9FH67; -.
DR   OMA; KEVYAGM; -.
DR   OrthoDB; 467733at2759; -.
DR   PhylomeDB; Q9FH67; -.
DR   BioCyc; ARA:AT5G42580-MON; -.
DR   PRO; PR:Q9FH67; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FH67; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
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..499
FT                   /note="Cytochrome P450 705A12"
FT                   /id="PRO_0000444435"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         439
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|UniProtKB:P04798"
SQ   SEQUENCE   499 AA;  56882 MW;  B2E7BA86E4348397 CRC64;
     MAELIIVDFQ NISIFILLCL FSFLCYALFF KKPKGFDLPP SPPSLPIIGH LHHLLSSSLP
     HKSFQKLSFK YGPLLHLRIF NFPMVLVSSA SMAYEVFRTN DVNVSYRFVP VNKDSLVFGS
     SGFVTAPYGD YWKFMKKLIS TKLLRPHALE LSKGNRAEEL RRFCLDLQGK ARKKESVEIG
     KVALKLTNNI ICRMSMGRSC SEKNGVAERA RELVNKSFAL SVKLFFSNMF RKDIMGVSRE
     FDEFLERILV EHEENLEGDQ DRDMIDHLLE AYRNEEAEYK ITRKQIKSLI VEIFLGGTDS
     SAQTIQWTMA EILNNPGVLE KLRAEIDSVV GGKRLIQESD LPNLPYLQAV VKEGLRLHPS
     APVLLRVFGE SCEVKEFYVP EKTTLVVNLY AVNRDPDSWE DPDMFKPERF LVSSISGDEE
     KIREQAVKYV TFGGGRRTCP AVKLAHIFME TAIGAMVQCF DWRIKGEKVY MEEAVSGLSL
     KMAHPLKCTP VVRFDPFSF