ID   D7KMH5_ARALL            Unreviewed;       488 AA.
AC   D7KMH5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=sterol 14alpha-demethylase {ECO:0000256|ARBA:ARBA00038974};
DE            EC=1.14.14.154 {ECO:0000256|ARBA:ARBA00038974};
GN   ORFNames=ARALYDRAFT_471307 {ECO:0000313|EMBL:EFH66146.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|EMBL:EFH66146.1, ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 14alpha-methyl steroid + 3 reduced [NADPH--hemoprotein
CC         reductase] + 3 O2 = a Delta(14) steroid + formate + 3 oxidized
CC         [NADPH--hemoprotein reductase] + 4 H2O + 4 H(+);
CC         Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154;
CC         Evidence={ECO:0000256|ARBA:ARBA00051013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; GL348713; EFH66146.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7KMH5; -.
DR   SMR; D7KMH5; -.
DR   STRING; 81972.D7KMH5; -.
DR   Gramene; fgenesh2_kg.1__1261__AT1G11680.1; fgenesh2_kg.1__1261__AT1G11680.1; fgenesh2_kg.1__1261__AT1G11680.1.
DR   eggNOG; KOG0684; Eukaryota.
DR   HOGENOM; CLU_001570_15_0_1; -.
DR   OrthoDB; 1055148at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008398; F:sterol 14-demethylase activity; IEA:UniProtKB-EC.
DR   CDD; cd11042; CYP51-like; 1.
DR   FunFam; 1.10.630.10:FF:000028; Cytochrome p450 51g1; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR050529; CYP51A1-like.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24304:SF2; 24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE; 1.
DR   PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         433
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:0000256|PIRSR:PIRSR602403-1"
SQ   SEQUENCE   488 AA;  55514 MW;  D8A32A166A6B5EF7 CRC64;
     MELDSENKLL KTGLVIVATL VIAKLIFSFF TSDSKKKRLP PTLKAWPPLI GSLIKFLKGP
     IVMLREEYPK LGSVFTVNLL HKKITFLIGP EVSAHFFKAS ESDLSQQEVY QFNVPTFGPG
     VVFDVDYSVR QEQFRFFTEA LRVTKLKGYV DMMVTEAEDY FSKWGESGEV DLKVELERLI
     ILTASRCLLG REVRDQLFDD VSALFHDLDN GMLPISVLFP YLPIPAHRRR DRAREKLAEI
     FSKIIGSRKR SGKSENDMLQ CFIESKYKDG RQTTESEVTG LLIAALFAGQ HTSSITSTWT
     GAYLMRYKEY FSAALDEQKN LIAKHGDKID HDILSEMDVL YRCIKEALRL HPPLIMLMRA
     SHSDFSVTAR DGKTYDIPKG HIVATSPAFA NRLPHIFKDP DTYDPERYSP GREEDKAAGA
     FSYISFGGGR HGCLGEPFAY LQIKAIWSHL LRNFELELVS PFPEIDWNAM VVGVKGNVMV
     RYKRRQLS
//