ID   CP51_SORBI              Reviewed;         492 AA.
AC   P93846;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   04-NOV-2026, entry version 132.
DE   RecName: Full=Obtusifoliol 14-alpha demethylase;
DE            EC=1.14.14.154;
DE   AltName: Full=CYPLI;
DE   AltName: Full=Cytochrome P450 51;
DE   AltName: Full=Cytochrome P450-LIA1;
GN   Name=CYP51;
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. SS1000; TISSUE=Etiolated seedling;
RX   PubMed=9076987; DOI=10.1046/j.1365-313x.1997.11020191.x;
RA   Bak S., Kahn R.A., Olsen C.E., Halkier B.A.;
RT   "Cloning and expression in Escherichia coli of the obtusifoliol 14 alpha-
RT   demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous
RT   to the sterol 14 alpha-demethylases (CYP51) from fungi and mammals.";
RL   Plant J. 11:191-201(1997).
CC   -!- FUNCTION: Catalyzes the 14-alpha demethylation of obtusifoliol to 4
CC       alpha-methyl-5 alpha-ergosta-8,14,24(28)-trien-3 beta-ol.
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 1/6.
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; U74319; AAC49659.1; -; mRNA.
DR   PIR; T14820; T14820.
DR   AlphaFoldDB; P93846; -.
DR   SMR; P93846; -.
DR   ChEMBL; CHEMBL2366482; -.
DR   eggNOG; KOG0684; Eukaryota.
DR   OMA; AAAYQYM; -.
DR   UniPathway; UPA00770; UER00754.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Metal-binding; Methyltransferase;
KW   Monooxygenase; Oxidoreductase; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..492
FT                   /note="Obtusifoliol 14-alpha demethylase"
FT                   /id="PRO_0000052013"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         434
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   492 AA;  55653 MW;  0C86160DFD812ECE CRC64;
     MDLADIPQQQ RLMAGLALVV ATVIFLKLLL SFRSGGGKKR LPPTIPGAPV VGGLVKFMRG
     PIPMIREQYA ALGSVFTVPI ITRRITFLIG PEVSAHFFKG NEAEMSQQEV YRFNVPTFGP
     GVVFDVDYSV RQEQFRFFTE ALRANKLRSY VDQMVAEAEE YFSKWGESGT VDLKYELEHL
     IILTASRCLL GREVREKLFD DVSALFHDLD NGIQPISVLF PYLPIPAHKR RDKARARLAE
     IFATIIKSRK ASGQSEEDML QCFIDSKYKN GRPTTEGEVT GLLIAALFAG QHTSSITSTW
     TGAYMLRFKQ YFAEAVEEQK DVMKRHGDKI DHDILAEMDV LYRCIKEALR LHPPLIMLLR
     QSHSDFTVTT KEGKEYDIPK GHIVATSPSF ANRLPHIYKN PDSYDPDRFG PGREEDKAAG
     AFSYISFGGG RHGCLGEPFA YLQIKAIWTH LLRNFEFELV SPFPENDWNA MVVGIKGEVM
     VNYKRRKLVV DN
//