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Protein

Squalene monooxygenase

Gene

ERG1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway.By similarity

Catalytic activityi

Squalene + [reduced NADPH--hemoprotein reductase] + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH--hemoprotein reductase] + H2O.By similarity

Cofactori

Pathwayi: lanosterol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes lanosterol from farnesyl diphosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Squalene monooxygenase (ERG1)
  3. Lanosterol synthase (ERG7)
This subpathway is part of the pathway lanosterol biosynthesis, which is itself part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lanosterol from farnesyl diphosphate, the pathway lanosterol biosynthesis and in Terpene metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 3528FADSequence analysisAdd
BLAST

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: InterPro
  • squalene monooxygenase activity Source: CGD

GO - Biological processi

  • cell growth mode switching, budding to filamentous Source: CGD
  • cellular response to drug Source: CGD
  • cellular response to starvation Source: CGD
  • ergosterol biosynthetic process Source: CGD
  • filamentous growth Source: CGD
  • filamentous growth of a population of unicellular organisms in response to biotic stimulus Source: CGD
  • filamentous growth of a population of unicellular organisms in response to chemical stimulus Source: CGD
  • filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
  • localization within membrane Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

UniPathwayiUPA00767; UER00752.

Names & Taxonomyi

Protein namesi
Recommended name:
Squalene monooxygenase (EC:1.14.14.17By similarity)
Alternative name(s):
Squalene epoxidase
Short name:
SE
Gene namesi
Name:ERG1
ORF Names:CaO19.406, CaO19.8036
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000179458. ERG1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4 – 2421HelicalSequence analysisAdd
BLAST
Transmembranei431 – 45121HelicalSequence analysisAdd
BLAST
Transmembranei466 – 48621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: CGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Chemistry

DrugBankiDB00525. Tolnaftate.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Squalene monooxygenasePRO_0000209848Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ92206.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the squalene monooxygenase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiQ92206.
KOiK00511.
OrthoDBiEOG092C1N2D.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR013698. Squalene_epoxidase.
[Graphical view]
PfamiPF08491. SE. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.

Sequencei

Sequence statusi: Complete.

Q92206-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVKYDAII IGAGVIGPTI ATAFARQGRK VLIVERDWSK PDRIVGELMQ
60 70 80 90 100
PAGIKALREL GMIKAINNIR AVDCTGYYIK YYDETITIPY PLKKDACITN
110 120 130 140 150
PVKPVPDAVD GVNDKLDSDS TLNVDDWDFD ERVRGAAFHH GDFLMNLRQI
160 170 180 190 200
CRDEPNVTAV EATVTKILRD PSDPNTVIGV QTKQPSGTVD YHAKLTISCD
210 220 230 240 250
GIYSKFRKEL SPTNVPTIGS YFIGLYLKNA ELPAKGKGHV LLGGHAPALI
260 270 280 290 300
YSVSPTETRV LCVYVSSKPP SAANDAVYKY LRDNILPAIP KETVPAFKEA
310 320 330 340 350
LEERKFRIMP NQYLSAMKQG SENHKGFILL GDSLNMRHPL TGGGMTVGLN
360 370 380 390 400
DSVLLAKLLH PKFVEDFDDH QLIAKRLKTF HRKRKNLDAV INTLSISLYS
410 420 430 440 450
LFAADKKPLR ILRNGCFKYF QRGGECVNGP IGLLSGMLPF PMLLFNHFFS
460 470 480 490
VAFYSVYLNF IERGLLGFPL ALFEAFEVLF TAIVIFTPYL WNEIVR
Length:496
Mass (Da):55,298
Last modified:February 1, 1997 - v1
Checksum:iC844CE43A679B920
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88252 Genomic DNA. Translation: BAA13565.1.
U69674 Genomic DNA. Translation: AAC49715.1.
AACQ01000177 Genomic DNA. Translation: EAK92686.1.
AACQ01000176 Genomic DNA. Translation: EAK92715.1.
RefSeqiXP_711894.1. XM_706801.1.
XP_711923.1. XM_706830.1.

Genome annotation databases

EnsemblFungiiEAK92686; EAK92686; CaO19.406.
EAK92715; EAK92715; CaO19.8036.
GeneIDi3646458.
3646509.
KEGGical:CaO19.406.
cal:CaO19.8036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88252 Genomic DNA. Translation: BAA13565.1.
U69674 Genomic DNA. Translation: AAC49715.1.
AACQ01000177 Genomic DNA. Translation: EAK92686.1.
AACQ01000176 Genomic DNA. Translation: EAK92715.1.
RefSeqiXP_711894.1. XM_706801.1.
XP_711923.1. XM_706830.1.

3D structure databases

ProteinModelPortaliQ92206.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB00525. Tolnaftate.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAK92686; EAK92686; CaO19.406.
EAK92715; EAK92715; CaO19.8036.
GeneIDi3646458.
3646509.
KEGGical:CaO19.406.
cal:CaO19.8036.

Organism-specific databases

CGDiCAL0000179458. ERG1.

Phylogenomic databases

InParanoidiQ92206.
KOiK00511.
OrthoDBiEOG092C1N2D.

Enzyme and pathway databases

UniPathwayiUPA00767; UER00752.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR013698. Squalene_epoxidase.
[Graphical view]
PfamiPF08491. SE. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiERG1_CANAL
AccessioniPrimary (citable) accession number: Q92206
Secondary accession number(s): Q59QB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: September 7, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.