CP51_WHEAT
ID CP51_WHEAT Reviewed; 453 AA.
AC P93596; P93595;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
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;
DE Flags: Fragment;
GN Name=CYP51;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Darius; TISSUE=Shoot;
RX PubMed=9016788; DOI=10.1006/bbrc.1996.5873;
RA Cabello-Hurtado F., Zimmerlin A., Rahier A., Taton M., Derose R.,
RA Nedelkina S., Batard Y., Durst F., Pallett K.E., Werck-Reichhart D.;
RT "Cloning and functional expression in yeast of a cDNA coding for an
RT obtusifoliol 14alpha-demethylase (CYP51) in wheat.";
RL Biochem. Biophys. Res. Commun. 230:381-385(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 O2 + 3 reduced [NADPH--
CC hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4
CC H2O + 3 oxidized [NADPH--hemoprotein reductase];
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}. Membrane; Single-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; Y09291; CAA70475.1; -; mRNA.
DR EMBL; Y09292; CAA70476.1; -; mRNA.
DR PIR; T06475; T06475.
DR AlphaFoldDB; P93596; -.
DR SMR; P93596; -.
DR STRING; 4565.Traes_4BS_1D0369514.2; -.
DR PRIDE; P93596; -.
DR eggNOG; KOG0684; Eukaryota.
DR UniPathway; UPA00770; UER00754.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P93596; baseline and differential.
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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008398; F:sterol 14-demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Methyltransferase; Monooxygenase; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transferase.
FT CHAIN <1..453
FT /note="Obtusifoliol 14-alpha demethylase"
FT /id="PRO_0000052014"
FT BINDING 395
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"
FT VARIANT 150
FT /note="Missing (in clone W516)"
FT VARIANT 175
FT /note="L -> Q (in clone W516)"
FT VARIANT 443
FT /note="N -> S (in clone W516)"
FT VARIANT 450
FT /note="I -> V (in clone W516)"
FT NON_TER 1
SQ SEQUENCE 453 AA; 51644 MW; 12A3D00952E3907D CRC64;
RPPPTIPGAP VVGGLLRFLR GPIPLIRAEY ARLGPVFTVP ILTRRITFLI GPDVSAHFFK
SNESDMSQQE VYRFNVPTFG PGVVFDVDYQ VRQEQFRFFT EALRANKLRS YVDQMVAEAE
EYFSKWGESG TVDLKYELEH LIILTASRCL LGREVREKLF DDVSALFHDL DNGMLPISVI
FPYLPIPAHR RRDQARTRLA EIFATIIKSR KASGQSEEDM LQCFIDSKYK NGRQTTESEV
TGLLIAALFA GQHTSSITST WTGAYLLKFQ QYFAEAVEEQ KEVMKRHGDK IDHDILAEMD
VLYRCIKEAL RLHPPLIMLL RQSHSDFSVT TREGKEFDIP KGHIVATSPA FANRLPHIFK
NPDSYDPDRF AAGREEDKVA GAFSYISFGG GRHGCLGEPF AYLQIKAIWT HLLRNFEFEL
VSPFPENDWN AMVVGIKGEV MVNYKRRKLI VDN
