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Protein

3-keto-steroid reductase

Gene

ERG27

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for the reduction of the keto group on the C-3 of sterols. Also facilitates the association of ERG7 with lipid particles preventing its digestion in the endoplasmic reticulum and the lipid particles.2 Publications

Catalytic activityi

A 3-beta-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH.

Pathwayi: zymosterol biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes zymosterol from lanosterol.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Lanosterol 14-alpha demethylase (ERG11)
  2. Delta(14)-sterol reductase (ERG24)
  3. Methylsterol monooxygenase (ERG25)
  4. Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (ERG26)
  5. 3-keto-steroid reductase (ERG27)
  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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei202 – 2021Proton acceptorBy similarity

GO - Molecular functioni

  • 3-keto sterol reductase activity Source: SGD

GO - Biological processi

  • ergosterol biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:YLR100W-MONOMER.
YEAST:YLR100W-MONOMER.
ReactomeiR-SCE-191273. Cholesterol biosynthesis.
UniPathwayiUPA00770; UER00758.

Names & Taxonomyi

Protein namesi
Recommended name:
3-keto-steroid reductase (EC:1.1.1.270)
Gene namesi
Name:ERG27
Ordered Locus Names:YLR100W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR100W.
SGDiS000004090. ERG27.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: SGD
  • endoplasmic reticulum membrane Source: SGD
  • lipid particle Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3473473-keto-steroid reductasePRO_0000054595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei345 – 3451PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12452.
PeptideAtlasiQ12452.
TopDownProteomicsiQ12452.

PTM databases

iPTMnetiQ12452.

Interactioni

Subunit structurei

Heterotetramer of ERG25, ERG26, ERG27 and ERG28. ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum. Interacts with ERG25 and ERG28. Also interacts with ERG7, but only in lipid particles.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERG25P530454EBI-38132,EBI-6506
ERG28P400306EBI-38132,EBI-22518
ERG7P386044EBI-38132,EBI-6572

Protein-protein interaction databases

BioGridi31374. 27 interactions.
DIPiDIP-1237N.
IntActiQ12452. 19 interactions.
MINTiMINT-387123.

Structurei

3D structure databases

ProteinModelPortaliQ12452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000013340.
HOGENOMiHOG000248600.
InParanoidiQ12452.
KOiK09827.
OMAiIQHRRGT.
OrthoDBiEOG741ZC1.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 2 hits.

Sequencei

Sequence statusi: Complete.

Q12452-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRKVAIVTG TNSNLGLNIV FRLIETEDTN VRLTIVVTSR TLPRVQEVIN
60 70 80 90 100
QIKDFYNKSG RVEDLEIDFD YLLVDFTNMV SVLNAYYDIN KKYRAINYLF
110 120 130 140 150
VNAAQGIFDG IDWIGAVKEV FTNPLEAVTN PTYKIQLVGV KSKDDMGLIF
160 170 180 190 200
QANVFGPYYF ISKILPQLTR GKAYIVWISS IMSDPKYLSL NDIELLKTNA
210 220 230 240 250
SYEGSKRLVD LLHLATYKDL KKLGINQYVV QPGIFTSHSF SEYLNFFTYF
260 270 280 290 300
GMLCLFYLAR LLGSPWHNID GYKAANAPVY VTRLANPNFE KQDVKYGSAT
310 320 330 340
SRDGMPYIKT QEIDPTGMSD VFAYIQKKKL EWDEKLKDQI VETRTPI
Length:347
Mass (Da):39,725
Last modified:November 1, 1996 - v1
Checksum:iD9A0589C049D8C49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53876 Genomic DNA. Translation: AAB67544.1.
Z73272 Genomic DNA. Translation: CAA97664.1.
BK006945 Genomic DNA. Translation: DAA09417.1.
PIRiS64936.
RefSeqiNP_013201.1. NM_001181987.1.

Genome annotation databases

EnsemblFungiiYLR100W; YLR100W; YLR100W.
GeneIDi850790.
KEGGisce:YLR100W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53876 Genomic DNA. Translation: AAB67544.1.
Z73272 Genomic DNA. Translation: CAA97664.1.
BK006945 Genomic DNA. Translation: DAA09417.1.
PIRiS64936.
RefSeqiNP_013201.1. NM_001181987.1.

3D structure databases

ProteinModelPortaliQ12452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31374. 27 interactions.
DIPiDIP-1237N.
IntActiQ12452. 19 interactions.
MINTiMINT-387123.

PTM databases

iPTMnetiQ12452.

Proteomic databases

MaxQBiQ12452.
PeptideAtlasiQ12452.
TopDownProteomicsiQ12452.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR100W; YLR100W; YLR100W.
GeneIDi850790.
KEGGisce:YLR100W.

Organism-specific databases

EuPathDBiFungiDB:YLR100W.
SGDiS000004090. ERG27.

Phylogenomic databases

GeneTreeiENSGT00390000013340.
HOGENOMiHOG000248600.
InParanoidiQ12452.
KOiK09827.
OMAiIQHRRGT.
OrthoDBiEOG741ZC1.

Enzyme and pathway databases

UniPathwayiUPA00770; UER00758.
BioCyciMetaCyc:YLR100W-MONOMER.
YEAST:YLR100W-MONOMER.
ReactomeiR-SCE-191273. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi966996.
PROiQ12452.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Characterization of the Saccharomyces cerevisiae ERG27 gene encoding the 3-keto reductase involved in C-4 sterol demethylation."
    Gachotte D., Sen S.E., Eckstein J., Barbuch R., Krieger M., Ray B.D., Bard M.
    Proc. Natl. Acad. Sci. U.S.A. 96:12655-12660(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, FUNCTION.
  4. "Protein-protein interactions among C-4 demethylation enzymes involved in yeast sterol biosynthesis."
    Mo C., Valachovic M., Randall S.K., Nickels J.T., Bard M.
    Proc. Natl. Acad. Sci. U.S.A. 99:9739-9744(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH ERG25 AND ERG28, SUBCELLULAR LOCATION.
  5. "In yeast sterol biosynthesis the 3-keto reductase protein (Erg27p) is required for oxidosqualene cyclase (Erg7p) activity."
    Mo C., Milla P., Athenstaedt K., Ott R., Balliano G., Daum G., Bard M.
    Biochim. Biophys. Acta 1633:68-74(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ERG7, SUBCELLULAR LOCATION.
  6. "Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex."
    Mo C., Bard M.
    J. Lipid Res. 46:1991-1998(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERG28.
  7. "The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy."
    Natter K., Leitner P., Faschinger A., Wolinski H., McCraith S., Fields S., Kohlwein S.D.
    Mol. Cell. Proteomics 4:662-672(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-345, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.

Entry informationi

Entry nameiERG27_YEAST
AccessioniPrimary (citable) accession number: Q12452
Secondary accession number(s): D6VYA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 125 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.