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Reviewed, UniProtKB/Swiss-Prot P53045 (ERG25_YEAST)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    C-4 methylsterol oxidase
    EC=1.14.13.72
Alternative name(s):
    Methylsterol monooxygenase
Gene names
Name: ERG25
Synonyms: FET6
Ordered Locus Names: YGR060W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol. Ref.2

Catalytic activity

4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)+ + H2O.

4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)+ + 2 H2O.

3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)H + O2 = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)+ + H2O.

Cofactor

Iron. Ref.2

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 3/6.

Subunit structure

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 ERG27 and ERG28. Ref.5 Ref.8

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Probable.

Domain

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Miscellaneous

Present with 77100 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Belongs to the sterol desaturase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309C-4 methylsterol oxidase
PRO_0000117039

Regions

Transmembrane56 – 7621 Potential
Motif160 – 1645Histidine box-1
Motif173 – 1775Histidine box-2
Motif257 – 2637Histidine box-3

Amino acid modifications

Cross-link96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

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Sequences

Sequence LengthMass (Da)Tools
P53045-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E0422C416DD17794

FASTA30936,479
        10         20         30         40         50         60 
MSAVFNNATL SGLVQASTYS QTLQNVAHYQ PQLNFMEKYW AAWYSYMNND VLATGLMFFL 

        70         80         90        100        110        120 
LHEFMYFFRC LPWFIIDQIP YFRRWKLQPT KIPSAKEQLY CLKSVLLSHF LVEAIPIWTF 

       130        140        150        160        170        180 
HPMCEKLGIT VEVPFPSLKT MALEIGLFFV LEDTWHYWAH RLFHYGVFYK YIHKQHHRYA 

       190        200        210        220        230        240 
APFGLSAEYA HPAETLSLGF GTVGMPILYV MYTGKLHLFT LCVWITLRLF QAVDSHSGYD 

       250        260        270        280        290        300 
FPWSLNKIMP FWAGAEHHDL HHHYFIGNYA SSFRWWDYCL DTESGPEAKA SREERMKKRA 


ENNAQKKTN

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and characterization of ERG25, the Saccharomyces cerevisiae gene encoding C-4 sterol methyl oxidase."
Bard M., Bruner D.A., Pierson C.A., Lees N.D., Biermann B., Frye L., Koegel C., Barbuch R.
Proc. Natl. Acad. Sci. U.S.A. 93:186-190(1996) [PubMed: 8552601] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue."
Li L., Kaplan J.
J. Biol. Chem. 271:16927-16933(1996) [PubMed: 8663358] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, SUBCELLULAR LOCATION.
[3]"Quantitative trait loci mapped to single-nucleotide resolution in yeast."
Deutschbauer A.M., Davis R.W.
Nat. Genet. 37:1333-1340(2005) [PubMed: 16273108] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SK1.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[5]"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: 12119386] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH ERG27 AND ERG28, SUBCELLULAR LOCATION.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed: 14557538] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-96, MASS SPECTROMETRY.
[8]"Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex."
Mo C., Bard M.
J. Lipid Res. 46:1991-1998(2005) [PubMed: 15995173] [Abstract]
Cited for: INTERACTION WITH ERG28.
[9]"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: 15716577] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U31885 Genomic DNA. Translation: AAC49139.1.
DQ115391 Genomic DNA. Translation: AAZ22473.1.
Z72845 Genomic DNA. Translation: CAA97062.1.
PIRS64354.
RefSeqNP_011574.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2799N.
IntActP53045. 111 interactions.

Proteomic databases

PeptideAtlasP53045.
PRIDEP53045.

Genome annotation databases

EnsemblYGR060W. Saccharomyces cerevisiae. [Contig view]
GeneID852951.
GenomeReviewsGene locus YGR060W in contig Y13135_GR.
KEGGsce:YGR060W.
NMPDRfig|4932.3.peg.2690.

Organism-specific databases

CYGDYGR060w.
SGDS000003292. ERG25.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP53045.
OMAP53045. EDTWHYW.

Enzyme and pathway databases

BRENDA1.14.13.72. 250.

Gene expression databases

GermOnlineYGR060W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR006694. Fatty_acid_hydroxylase.
[Graphical view]
PfamPF04116. FA_hydroxylase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio972708.

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Entry information

Entry nameERG25_YEAST
AccessionPrimary (citable) accession number: P53045
Secondary accession number(s): Q45U26
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents