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Q7Z1V1

- CP51_TRYCC

UniProt

Q7Z1V1 - CP51_TRYCC

Protein

Sterol 14-alpha demethylase

Gene

CYP51

Organism
Trypanosoma cruzi (strain CL Brener)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    Catalytic activityi

    A 14-alpha-methylsteroid + 3 O2 + 3 NADPH = a Delta(14)-steroid + formate + 3 NADP+ + 4 H2O.1 Publication

    Cofactori

    Heme group.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi422 – 4221Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. sterol 14-demethylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. sterol biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    UniPathwayiUPA00770; UER00754.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sterol 14-alpha demethylaseImported1 Publication (EC:1.14.13.70)
    Short name:
    Tc14DM1 Publication
    Alternative name(s):
    Cytochrome P450 51By similarity
    Lanosterol 14-alpha demethylaseImported1 Publication
    Gene namesi
    Name:CYP51Imported
    ORF Names:Tc00.1047053506297.260, Tc00.1047053510101.50
    OrganismiTrypanosoma cruzi (strain CL Brener)
    Taxonomic identifieri353153 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum
    ProteomesiUP000002296: Unassembled WGS sequence

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi105 – 1051I → F: Increases activity on norlanosterol and obtusifoliol. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 481481Sterol 14-alpha demethylasePRO_0000389527Add
    BLAST

    Expressioni

    Developmental stagei

    Expressed in both the insect and mammalian life-cycle stages.1 Publication

    Interactioni

    Structurei

    Secondary structure

    1
    481
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 313
    Beta strandi34 – 363
    Turni40 – 423
    Helixi45 – 506
    Helixi52 – 6211
    Beta strandi66 – 727
    Beta strandi75 – 806
    Helixi83 – 853
    Helixi86 – 905
    Turni94 – 963
    Beta strandi97 – 993
    Helixi100 – 1067
    Helixi107 – 1104
    Turni112 – 1143
    Helixi115 – 1173
    Helixi120 – 13213
    Helixi136 – 1383
    Helixi139 – 1413
    Helixi142 – 15716
    Beta strandi160 – 1667
    Helixi167 – 18317
    Helixi186 – 1916
    Helixi194 – 20613
    Helixi210 – 2134
    Helixi216 – 2205
    Helixi229 – 24820
    Turni249 – 2546
    Helixi261 – 2666
    Beta strandi271 – 2733
    Helixi278 – 30831
    Helixi310 – 3123
    Helixi313 – 32311
    Beta strandi324 – 3263
    Helixi332 – 3376
    Helixi340 – 35213
    Beta strandi359 – 3657
    Beta strandi367 – 3693
    Beta strandi372 – 3743
    Beta strandi379 – 3824
    Helixi384 – 3874
    Turni391 – 3933
    Beta strandi394 – 3963
    Helixi418 – 4203
    Helixi425 – 44218
    Beta strandi443 – 4519
    Beta strandi459 – 4613
    Helixi466 – 4683
    Beta strandi470 – 4767

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WUZX-ray2.35A/B22-481[»]
    2WX2X-ray2.27A/B22-481[»]
    3K1OX-ray2.89A32-481[»]
    3KHMX-ray2.85A32-481[»]
    3KSWX-ray3.05A32-481[»]
    3ZG2X-ray2.80A29-481[»]
    3ZG3X-ray2.90A29-481[»]
    4BMMX-ray2.84A/B/C/D32-481[»]
    4BY0X-ray3.10A/B32-481[»]
    4COHX-ray2.08A/B29-481[»]
    4H6OX-ray2.80A29-481[»]
    ProteinModelPortaliQ7Z1V1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7Z1V1.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1 – 2121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Sequence Analysis

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    KOiK05917.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002403. Cyt_P450_E_grp-IV.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00465. EP450IV.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7Z1V1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFIEAIVLAL TALILYSVYS VKSFNTTRPT DPPVYPVTVP FLGHIVQFGK    50
    NPLEFMQRCK RDLKSGVFTI SIGGQRVTIV GDPHEHSRFF SPRNEILSPR 100
    EVYTIMTPVF GEGVAYAAPY PRMREQLNFL AEELTIAKFQ NFVPAIQHEV 150
    RKFMAENWKE DEGVINLLED CGAMIINTAC QCLFGEDLRK RLNARHFAQL 200
    LSKMESSLIP AAVFMPWLLR LPLPQSARCR EARAELQKIL GEIIVAREKE 250
    EASKDNNTSD LLGGLLKAVY RDGTRMSLHE VCGMIVAAMF AGQHTSTITT 300
    SWSMLHLMHP KNKKWLDKLH KEIDEFPAQL NYDNVMDEMP FAERCVRESI 350
    RRDPPLLMVM RMVKAEVKVG SYVVPKGDII ACSPLLSHHD EEAFPNPRLW 400
    DPERDEKVDG AFIGFGAGVH KCIGQKFALL QVKTILATAF REYDFQLLRD 450
    EVPDPDYHTM VVGPTLNQCL VKYTRKKKLP S 481
    Length:481
    Mass (Da):54,683
    Last modified:October 1, 2003 - v1
    Checksum:iC83BA5243C959151
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91A → G in AAW47718. (PubMed:16321980)Curated
    Sequence conflicti9 – 91A → G in EAN98359. (PubMed:16020725)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621D → E in allele 2. 2 Publications
    Natural varianti117 – 1171A → S in allele 2. 2 Publications
    Natural varianti160 – 1601E → K in allele 2. 2 Publications

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY283022 Genomic DNA. Translation: AAP33131.1.
    AY283023 Genomic DNA. Translation: AAP33132.1.
    AY856083 Genomic DNA. Translation: AAW47718.1.
    AAHK01000021 Genomic DNA. Translation: EAN99368.1.
    AAHK01000058 Genomic DNA. Translation: EAN98359.1.
    RefSeqiXP_820210.1. XM_815117.1.
    XP_821219.1. XM_816126.1.

    Genome annotation databases

    GeneIDi3552837.
    3554116.
    KEGGitcr:506297.260.
    tcr:510101.50.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY283022 Genomic DNA. Translation: AAP33131.1 .
    AY283023 Genomic DNA. Translation: AAP33132.1 .
    AY856083 Genomic DNA. Translation: AAW47718.1 .
    AAHK01000021 Genomic DNA. Translation: EAN99368.1 .
    AAHK01000058 Genomic DNA. Translation: EAN98359.1 .
    RefSeqi XP_820210.1. XM_815117.1.
    XP_821219.1. XM_816126.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WUZ X-ray 2.35 A/B 22-481 [» ]
    2WX2 X-ray 2.27 A/B 22-481 [» ]
    3K1O X-ray 2.89 A 32-481 [» ]
    3KHM X-ray 2.85 A 32-481 [» ]
    3KSW X-ray 3.05 A 32-481 [» ]
    3ZG2 X-ray 2.80 A 29-481 [» ]
    3ZG3 X-ray 2.90 A 29-481 [» ]
    4BMM X-ray 2.84 A/B/C/D 32-481 [» ]
    4BY0 X-ray 3.10 A/B 32-481 [» ]
    4COH X-ray 2.08 A/B 29-481 [» ]
    4H6O X-ray 2.80 A 29-481 [» ]
    ProteinModelPortali Q7Z1V1.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q7Z1V1.
    ChEMBLi CHEMBL1075110.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3552837.
    3554116.
    KEGGi tcr:506297.260.
    tcr:510101.50.

    Phylogenomic databases

    KOi K05917.

    Enzyme and pathway databases

    UniPathwayi UPA00770 ; UER00754 .

    Miscellaneous databases

    EvolutionaryTracei Q7Z1V1.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002403. Cyt_P450_E_grp-IV.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00465. EP450IV.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and analysis of Trypanosoma cruzi lanosterol 14alpha-demethylase."
      Buckner F.S., Joubert B.M., Boyle S.M., Eastman R.T., Verlinde C.L.M.J., Matsuda S.P.T.
      Mol. Biochem. Parasitol. 132:75-81(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES 1 AND 2), DEVELOPMENTAL STAGE.
      Strain: TulahuenImported.
    2. "CYP51 from Trypanosoma cruzi: a phyla-specific residue in the B' helix defines substrate preferences of sterol 14alpha-demethylase."
      Lepesheva G.I., Zaitseva N.G., Nes W.D., Zhou W., Arase M., Liu J., Hill G.C., Waterman M.R.
      J. Biol. Chem. 281:3577-3585(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE 1), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-105.
    3. "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease."
      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.
      Science 309:409-415(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES 1 AND 2).
      Strain: CL BrenerImported.

    Entry informationi

    Entry nameiCP51_TRYCC
    AccessioniPrimary (citable) accession number: Q7Z1V1
    Secondary accession number(s): Q5I4E1, Q7Z1V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 24, 2009
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3