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Sterol 14-alpha demethylase (Tc14DM) (EC 1.14.13.70) (Cytochrome P450 51) (Lanosterol 14-alpha demethylase)

 CP51_TRYCC              Reviewed;         481 AA.
Q7Z1V1; Q5I4E1; Q7Z1V0;
24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
25-APR-2018, entry version 95.
RecName: Full=Sterol 14-alpha demethylase {ECO:0000303|PubMed:16321980, ECO:0000312|EMBL:AAW47718.1};
Short=Tc14DM {ECO:0000303|PubMed:14599667};
EC=1.14.13.70;
AltName: Full=Cytochrome P450 51 {ECO:0000250|UniProtKB:P0A512};
AltName: Full=Lanosterol 14-alpha demethylase {ECO:0000303|PubMed:14599667, ECO:0000312|EMBL:AAP33131.1};
Name=CYP51 {ECO:0000312|EMBL:AAW47718.1};
ORFNames=Tc00.1047053506297.260, Tc00.1047053510101.50;
Trypanosoma cruzi (strain CL Brener).
Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma;
Schizotrypanum.
NCBI_TaxID=353153;
[1] {ECO:0000305, ECO:0000312|EMBL:AAP33131.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES 1 AND 2), AND DEVELOPMENTAL
STAGE.
STRAIN=Tulahuen {ECO:0000312|EMBL:AAP33131.1};
PubMed=14599667; DOI=10.1016/j.molbiopara.2003.07.004;
Buckner F.S., Joubert B.M., Boyle S.M., Eastman R.T.,
Verlinde C.L.M.J., Matsuda S.P.T.;
"Cloning and analysis of Trypanosoma cruzi lanosterol 14alpha-
demethylase.";
Mol. Biochem. Parasitol. 132:75-81(2003).
[2] {ECO:0000305, ECO:0000312|EMBL:AAW47718.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE 1), FUNCTION, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF ILE-105.
PubMed=16321980; DOI=10.1074/jbc.M510317200;
Lepesheva G.I., Zaitseva N.G., Nes W.D., Zhou W., Arase M., Liu J.,
Hill G.C., Waterman M.R.;
"CYP51 from Trypanosoma cruzi: a phyla-specific residue in the B'
helix defines substrate preferences of sterol 14alpha-demethylase.";
J. Biol. Chem. 281:3577-3585(2006).
[3] {ECO:0000312|EMBL:EAN98359.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES 1 AND 2).
STRAIN=CL Brener {ECO:0000312|EMBL:EAN98359.1};
PubMed=16020725; DOI=10.1126/science.1112631;
El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D.,
Aggarwal G., Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L.,
Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C.,
Haas B., Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E.,
Bringaud F., Burton P., Cadag E., Campbell D.A., Carrington M.,
Crabtree J., Darban H., da Silveira J.F., de Jong P., Edwards K.,
Englund P.T., Fazelina G., Feldblyum T., Ferella M., Frasch A.C.,
Gull K., Horn D., Hou L., Huang Y., Kindlund E., Klingbeil M.,
Kluge S., Koo H., Lacerda D., Levin M.J., Lorenzi H., Louie T.,
Machado C.R., McCulloch R., McKenna A., Mizuno Y., Mottram J.C.,
Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M.,
Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J.,
Simpson A.J., Sisk E., Tammi M.T., Tarleton R., Teixeira S.,
Van Aken S., Vogt C., Ward P.N., Wickstead B., Wortman J., White O.,
Fraser C.M., Stuart K.D., Andersson B.;
"The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
disease.";
Science 309:409-415(2005).
-!- FUNCTION: Catalyzes C14-demethylation of lanosterol which is
critical for ergosterol biosynthesis. It transforms lanosterol
into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol (By
similarity). Favors C4 dimethylated substrates, the substrate
preference order is 24-methylenedihydrolanosterol > 24,25-
dihydrolanosterol > lanosterol > obtusifoliol > norlanosterol.
{ECO:0000250|UniProtKB:P0A512, ECO:0000269|PubMed:16321980}.
-!- CATALYTIC ACTIVITY: A 14-alpha-methylsteroid + 3 O(2) + 3 NADPH =
a Delta(14)-steroid + formate + 3 NADP(+) + 4 H(2)O.
{ECO:0000269|PubMed:16321980}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P0A512};
-!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol
from lanosterol: step 1/6. {ECO:0000250|UniProtKB:P0A512}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}.
-!- DEVELOPMENTAL STAGE: Expressed in both the insect and mammalian
life-cycle stages. {ECO:0000269|PubMed:14599667}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000255}.
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EMBL; AY283022; AAP33131.1; -; Genomic_DNA.
EMBL; AY283023; AAP33132.1; -; Genomic_DNA.
EMBL; AY856083; AAW47718.1; -; Genomic_DNA.
EMBL; AAHK01000021; EAN99368.1; -; Genomic_DNA.
EMBL; AAHK01000058; EAN98359.1; -; Genomic_DNA.
RefSeq; XP_820210.1; XM_815117.1.
RefSeq; XP_821219.1; XM_816126.1.
PDB; 2WUZ; X-ray; 2.35 A; A/B=22-481.
PDB; 2WX2; X-ray; 2.27 A; A/B=22-481.
PDB; 3K1O; X-ray; 2.89 A; A=32-481.
PDB; 3KHM; X-ray; 2.85 A; A=32-481.
PDB; 3KSW; X-ray; 3.05 A; A=32-481.
PDB; 3ZG2; X-ray; 2.80 A; A=29-481.
PDB; 3ZG3; X-ray; 2.90 A; A=29-481.
PDB; 4BMM; X-ray; 2.84 A; A/B/C/D=32-481.
PDB; 4BY0; X-ray; 3.10 A; A/B=32-481.
PDB; 4C0C; X-ray; 2.04 A; A=32-481.
PDB; 4C27; X-ray; 1.95 A; A/B=29-481.
PDB; 4C28; X-ray; 2.03 A; A/B=29-481.
PDB; 4CK8; X-ray; 2.62 A; A/B=32-481.
PDB; 4CK9; X-ray; 2.74 A; A=32-481.
PDB; 4CKA; X-ray; 2.70 A; A=32-481.
PDB; 4COH; X-ray; 2.08 A; A/B=29-481.
PDB; 4H6O; X-ray; 2.80 A; A=29-481.
PDB; 4UQH; X-ray; 2.43 A; A=32-481.
PDB; 4UVR; X-ray; 2.48 A; A=32-481.
PDB; 5AJR; X-ray; 2.75 A; A=32-481.
PDBsum; 2WUZ; -.
PDBsum; 2WX2; -.
PDBsum; 3K1O; -.
PDBsum; 3KHM; -.
PDBsum; 3KSW; -.
PDBsum; 3ZG2; -.
PDBsum; 3ZG3; -.
PDBsum; 4BMM; -.
PDBsum; 4BY0; -.
PDBsum; 4C0C; -.
PDBsum; 4C27; -.
PDBsum; 4C28; -.
PDBsum; 4CK8; -.
PDBsum; 4CK9; -.
PDBsum; 4CKA; -.
PDBsum; 4COH; -.
PDBsum; 4H6O; -.
PDBsum; 4UQH; -.
PDBsum; 4UVR; -.
PDBsum; 5AJR; -.
ProteinModelPortal; Q7Z1V1; -.
SMR; Q7Z1V1; -.
STRING; 353153.XP_820210.1; -.
BindingDB; Q7Z1V1; -.
ChEMBL; CHEMBL1075110; -.
PaxDb; Q7Z1V1; -.
EnsemblProtists; EAN98359; EAN98359; Tc00.1047053506297.260.
EnsemblProtists; EAN99368; EAN99368; Tc00.1047053510101.50.
GeneDB; TcCLB.506297.260:pep; -.
GeneDB; TcCLB.510101.50:pep; -.
GeneID; 3552837; -.
GeneID; 3554116; -.
KEGG; tcr:506297.260; -.
KEGG; tcr:510101.50; -.
eggNOG; KOG0684; Eukaryota.
eggNOG; COG2124; LUCA.
KO; K05917; -.
BRENDA; 1.14.13.70; 6524.
UniPathway; UPA00770; UER00754.
EvolutionaryTrace; Q7Z1V1; -.
Proteomes; UP000002296; Unassembled WGS sequence.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0008398; F:sterol 14-demethylase activity; IEA:UniProtKB-EC.
GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002403; Cyt_P450_E_grp-IV.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00465; EP450IV.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Heme; Iron; Lipid biosynthesis;
Lipid metabolism; Membrane; Metal-binding; Monooxygenase; NADP;
Oxidoreductase; Polymorphism; Reference proteome;
Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
Sterol metabolism; Transmembrane; Transmembrane helix.
CHAIN 1 481 Sterol 14-alpha demethylase.
/FTId=PRO_0000389527.
TRANSMEM 1 21 Helical. {ECO:0000255}.
METAL 422 422 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P0A512}.
VARIANT 62 62 D -> E (in allele 2).
{ECO:0000269|PubMed:14599667,
ECO:0000269|PubMed:16020725}.
VARIANT 117 117 A -> S (in allele 2).
{ECO:0000269|PubMed:14599667,
ECO:0000269|PubMed:16020725}.
VARIANT 160 160 E -> K (in allele 2).
{ECO:0000269|PubMed:14599667,
ECO:0000269|PubMed:16020725}.
MUTAGEN 105 105 I->F: Increases activity on norlanosterol
and obtusifoliol.
{ECO:0000269|PubMed:16321980}.
CONFLICT 9 9 A -> G (in Ref. 2; AAW47718 and 3;
EAN98359). {ECO:0000305}.
STRAND 29 31 {ECO:0000244|PDB:2WUZ}.
STRAND 34 36 {ECO:0000244|PDB:2WX2}.
TURN 40 42 {ECO:0000244|PDB:4C27}.
HELIX 45 50 {ECO:0000244|PDB:4C27}.
HELIX 52 62 {ECO:0000244|PDB:4C27}.
STRAND 66 72 {ECO:0000244|PDB:4C27}.
STRAND 75 80 {ECO:0000244|PDB:4C27}.
HELIX 83 85 {ECO:0000244|PDB:4C27}.
HELIX 86 90 {ECO:0000244|PDB:4C27}.
TURN 94 96 {ECO:0000244|PDB:4C27}.
HELIX 99 102 {ECO:0000244|PDB:4C27}.
HELIX 104 106 {ECO:0000244|PDB:4C27}.
HELIX 107 110 {ECO:0000244|PDB:4C27}.
TURN 112 114 {ECO:0000244|PDB:2WX2}.
HELIX 115 117 {ECO:0000244|PDB:4C27}.
HELIX 120 132 {ECO:0000244|PDB:4C27}.
HELIX 136 138 {ECO:0000244|PDB:4C27}.
HELIX 139 141 {ECO:0000244|PDB:4CK8}.
HELIX 142 157 {ECO:0000244|PDB:4C27}.
STRAND 160 166 {ECO:0000244|PDB:4C27}.
HELIX 167 183 {ECO:0000244|PDB:4C27}.
HELIX 186 191 {ECO:0000244|PDB:4C27}.
HELIX 194 206 {ECO:0000244|PDB:4C27}.
HELIX 210 213 {ECO:0000244|PDB:4C27}.
HELIX 216 220 {ECO:0000244|PDB:4C27}.
HELIX 229 250 {ECO:0000244|PDB:4C27}.
TURN 252 254 {ECO:0000244|PDB:3KSW}.
HELIX 261 265 {ECO:0000244|PDB:4C27}.
STRAND 271 273 {ECO:0000244|PDB:2WUZ}.
HELIX 278 308 {ECO:0000244|PDB:4C27}.
HELIX 310 312 {ECO:0000244|PDB:4C27}.
HELIX 313 323 {ECO:0000244|PDB:4C27}.
STRAND 324 326 {ECO:0000244|PDB:4CK9}.
HELIX 332 337 {ECO:0000244|PDB:4C27}.
HELIX 340 352 {ECO:0000244|PDB:4C27}.
STRAND 359 365 {ECO:0000244|PDB:4C27}.
STRAND 367 369 {ECO:0000244|PDB:4C27}.
STRAND 372 374 {ECO:0000244|PDB:4C27}.
STRAND 379 382 {ECO:0000244|PDB:4C27}.
HELIX 384 387 {ECO:0000244|PDB:4C27}.
TURN 391 393 {ECO:0000244|PDB:4C27}.
STRAND 394 396 {ECO:0000244|PDB:4C27}.
HELIX 418 420 {ECO:0000244|PDB:4C27}.
HELIX 425 442 {ECO:0000244|PDB:4C27}.
STRAND 443 451 {ECO:0000244|PDB:4C27}.
STRAND 459 461 {ECO:0000244|PDB:4C27}.
HELIX 466 468 {ECO:0000244|PDB:4C27}.
STRAND 470 475 {ECO:0000244|PDB:4C27}.
SEQUENCE 481 AA; 54683 MW; C83BA5243C959151 CRC64;
MFIEAIVLAL TALILYSVYS VKSFNTTRPT DPPVYPVTVP FLGHIVQFGK NPLEFMQRCK
RDLKSGVFTI SIGGQRVTIV GDPHEHSRFF SPRNEILSPR EVYTIMTPVF GEGVAYAAPY
PRMREQLNFL AEELTIAKFQ NFVPAIQHEV RKFMAENWKE DEGVINLLED CGAMIINTAC
QCLFGEDLRK RLNARHFAQL LSKMESSLIP AAVFMPWLLR LPLPQSARCR EARAELQKIL
GEIIVAREKE EASKDNNTSD LLGGLLKAVY RDGTRMSLHE VCGMIVAAMF AGQHTSTITT
SWSMLHLMHP KNKKWLDKLH KEIDEFPAQL NYDNVMDEMP FAERCVRESI RRDPPLLMVM
RMVKAEVKVG SYVVPKGDII ACSPLLSHHD EEAFPNPRLW DPERDEKVDG AFIGFGAGVH
KCIGQKFALL QVKTILATAF REYDFQLLRD EVPDPDYHTM VVGPTLNQCL VKYTRKKKLP
S


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