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Protein

Sterol 14-alpha demethylase

Gene

CYP51

Organism
Trypanosoma cruzi (strain CL Brener)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandHeme, 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

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
InterProiView protein in InterPro
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002403 Cyt_P450_E_grp-IV
IPR036396 Cyt_P450_sf
PfamiView protein in Pfam
PF00067 p450, 1 hit
PRINTSiPR00465 EP450IV
PR00385 P450
SUPFAMiSSF48264 SSF48264, 1 hit
PROSITEiView protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit

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
GeneDBiTcCLB.506297.260:pep
TcCLB.510101.50:pep
GeneIDi3552837
3554116
KEGGitcr:506297.260
tcr:510101.50

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCP51_TRYCC
AccessioniPrimary (citable) accession number: Q7Z1V1
Secondary accession number(s): Q5I4E1, Q7Z1V0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: October 1, 2003
Last modified: April 25, 2018
This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health