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Protein

Sterol 14-alpha demethylase

Gene

CYP51

Organism
Trypanosoma cruzi (strain CL Brener)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

hemeBy similarity

Pathwayi: zymosterol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes zymosterol from lanosterol.By similarity
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Sterol 14-alpha demethylase (CYP51)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
This subpathway is part of the pathway zymosterol biosynthesis, which is itself part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi422Iron (heme axial ligand)By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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

BRENDAi1.14.13.70. 6524.
UniPathwayiUPA00770; UER00754.

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol 14-alpha demethylase1 PublicationImported (EC:1.14.13.70)
Short name:
Tc14DM1 Publication
Alternative name(s):
Cytochrome P450 51By similarity
Lanosterol 14-alpha demethylase1 PublicationImported
Gene namesi
Name:CYP51Imported
ORF Names:Tc00.1047053506297.260, Tc00.1047053510101.50
OrganismiTrypanosoma cruzi (strain CL Brener)
Taxonomic identifieri353153 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum
Proteomesi
  • UP000002296 Componenti: Unassembled WGS sequence

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei1 – 21HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105I → F: Increases activity on norlanosterol and obtusifoliol. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075110.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003895271 – 481Sterol 14-alpha demethylaseAdd BLAST481

Proteomic databases

PaxDbiQ7Z1V1.

Expressioni

Developmental stagei

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

Interactioni

Protein-protein interaction databases

STRINGi353153.XP_820210.1.

Chemistry databases

BindingDBiQ7Z1V1.

Structurei

Secondary structure

1481
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 31Combined sources3
Beta strandi34 – 36Combined sources3
Turni40 – 42Combined sources3
Helixi45 – 50Combined sources6
Helixi52 – 62Combined sources11
Beta strandi66 – 72Combined sources7
Beta strandi75 – 80Combined sources6
Helixi83 – 85Combined sources3
Helixi86 – 90Combined sources5
Turni94 – 96Combined sources3
Helixi99 – 102Combined sources4
Helixi104 – 106Combined sources3
Helixi107 – 110Combined sources4
Turni112 – 114Combined sources3
Helixi115 – 117Combined sources3
Helixi120 – 132Combined sources13
Helixi136 – 138Combined sources3
Helixi139 – 141Combined sources3
Helixi142 – 157Combined sources16
Beta strandi160 – 166Combined sources7
Helixi167 – 183Combined sources17
Helixi186 – 191Combined sources6
Helixi194 – 206Combined sources13
Helixi210 – 213Combined sources4
Helixi216 – 220Combined sources5
Helixi229 – 250Combined sources22
Turni252 – 254Combined sources3
Helixi261 – 265Combined sources5
Beta strandi271 – 273Combined sources3
Helixi278 – 308Combined sources31
Helixi310 – 312Combined sources3
Helixi313 – 323Combined sources11
Beta strandi324 – 326Combined sources3
Helixi332 – 337Combined sources6
Helixi340 – 352Combined sources13
Beta strandi359 – 365Combined sources7
Beta strandi367 – 369Combined sources3
Beta strandi372 – 374Combined sources3
Beta strandi379 – 382Combined sources4
Helixi384 – 387Combined sources4
Turni391 – 393Combined sources3
Beta strandi394 – 396Combined sources3
Helixi418 – 420Combined sources3
Helixi425 – 442Combined sources18
Beta strandi443 – 451Combined sources9
Beta strandi459 – 461Combined sources3
Helixi466 – 468Combined sources3
Beta strandi470 – 475Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4C0CX-ray2.04A32-481[»]
4C27X-ray1.95A/B29-481[»]
4C28X-ray2.03A/B29-481[»]
4CK8X-ray2.62A/B32-481[»]
4CK9X-ray2.74A32-481[»]
4CKAX-ray2.70A32-481[»]
4COHX-ray2.08A/B29-481[»]
4H6OX-ray2.80A29-481[»]
4UQHX-ray2.43A32-481[»]
4UVRX-ray2.48A32-481[»]
5AJRX-ray2.75A32-481[»]
ProteinModelPortaliQ7Z1V1.
SMRiQ7Z1V1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7Z1V1.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Sequence analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0684. Eukaryota.
COG2124. LUCA.
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

        10         20         30         40         50
MFIEAIVLAL TALILYSVYS VKSFNTTRPT DPPVYPVTVP FLGHIVQFGK
60 70 80 90 100
NPLEFMQRCK RDLKSGVFTI SIGGQRVTIV GDPHEHSRFF SPRNEILSPR
110 120 130 140 150
EVYTIMTPVF GEGVAYAAPY PRMREQLNFL AEELTIAKFQ NFVPAIQHEV
160 170 180 190 200
RKFMAENWKE DEGVINLLED CGAMIINTAC QCLFGEDLRK RLNARHFAQL
210 220 230 240 250
LSKMESSLIP AAVFMPWLLR LPLPQSARCR EARAELQKIL GEIIVAREKE
260 270 280 290 300
EASKDNNTSD LLGGLLKAVY RDGTRMSLHE VCGMIVAAMF AGQHTSTITT
310 320 330 340 350
SWSMLHLMHP KNKKWLDKLH KEIDEFPAQL NYDNVMDEMP FAERCVRESI
360 370 380 390 400
RRDPPLLMVM RMVKAEVKVG SYVVPKGDII ACSPLLSHHD EEAFPNPRLW
410 420 430 440 450
DPERDEKVDG AFIGFGAGVH KCIGQKFALL QVKTILATAF REYDFQLLRD
460 470 480
EVPDPDYHTM VVGPTLNQCL VKYTRKKKLP S
Length:481
Mass (Da):54,683
Last modified:October 1, 2003 - v1
Checksum:iC83BA5243C959151
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9A → G in AAW47718 (PubMed:16321980).Curated1
Sequence conflicti9A → G in EAN98359 (PubMed:16020725).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti62D → E in allele 2. 2 Publications1
Natural varianti117A → S in allele 2. 2 Publications1
Natural varianti160E → K in allele 2. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsemblProtistsiEAN98359; EAN98359; Tc00.1047053506297.260.
EAN99368; EAN99368; Tc00.1047053510101.50.
GeneIDi3552837.
3554116.
KEGGitcr:506297.260.
tcr:510101.50.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4C0CX-ray2.04A32-481[»]
4C27X-ray1.95A/B29-481[»]
4C28X-ray2.03A/B29-481[»]
4CK8X-ray2.62A/B32-481[»]
4CK9X-ray2.74A32-481[»]
4CKAX-ray2.70A32-481[»]
4COHX-ray2.08A/B29-481[»]
4H6OX-ray2.80A29-481[»]
4UQHX-ray2.43A32-481[»]
4UVRX-ray2.48A32-481[»]
5AJRX-ray2.75A32-481[»]
ProteinModelPortaliQ7Z1V1.
SMRiQ7Z1V1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi353153.XP_820210.1.

Chemistry databases

BindingDBiQ7Z1V1.
ChEMBLiCHEMBL1075110.

Proteomic databases

PaxDbiQ7Z1V1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAN98359; EAN98359; Tc00.1047053506297.260.
EAN99368; EAN99368; Tc00.1047053510101.50.
GeneIDi3552837.
3554116.
KEGGitcr:506297.260.
tcr:510101.50.

Phylogenomic databases

eggNOGiKOG0684. Eukaryota.
COG2124. LUCA.
KOiK05917.

Enzyme and pathway databases

UniPathwayiUPA00770; UER00754.
BRENDAi1.14.13.70. 6524.

Miscellaneous databases

EvolutionaryTraceiQ7Z1V1.
PROiQ7Z1V1.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 90 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.