Methylsterol monooxygenase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53045 (MSMO_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Methylsterol monooxygenase
EC=1.14.13.72

Alternative name(s):
C-4 methylsterol oxidase

Gene names

Name:	ERG25
Synonyms:	FET6
Ordered Locus Names:	YGR060W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.7 Ref.10
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein Probable Ref.2 Ref.7 Ref.11.
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.
Sequence similarities	Belongs to the sterol desaturase family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Iron NAD
Molecular function	Oxidoreductase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ergosterol biosynthetic process Inferred from direct assay Ref.2. Source: SGD fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	endoplasmic reticulum membrane Inferred from direct assay Ref.2. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.2. Source: SGD
Molecular_function	C-4 methylsterol oxidase activity Inferred from direct assay Ref.2. Source: SGD iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ERG11	P10614	3	EBI-6506,EBI-5127
ERG27	Q12452	4	EBI-6506,EBI-38132
ERG28	P40030	3	EBI-6506,EBI-22518
ERG3	P32353	3	EBI-6506,EBI-6554

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 309

309

Methylsterol monooxygenase

PRO_0000117039

Regions

Transmembrane

56 – 76

Helical; Potential

Motif

160 – 164

Histidine box-1

Motif

173 – 177

Histidine box-2

Motif

257 – 263

Histidine box-3

Amino acid modifications

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Experimental info

Sequence conflict

302

N → K in AAS56153. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P53045 [UniParc].

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

309

36,479

        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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[7]	"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 ERG27 AND ERG28, SUBCELLULAR LOCATION.
[8]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-96, MASS SPECTROMETRY.
[10]	"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.
[11]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U31885 Genomic DNA. Translation: AAC49139.1. DQ115391 Genomic DNA. Translation: AAZ22473.1. Z72845 Genomic DNA. Translation: CAA97062.1. AY557827 Genomic DNA. Translation: AAS56153.1. BK006941 Genomic DNA. Translation: DAA08156.1.
PIR	S64354.
RefSeq	NP_011574.3. NM_001181189.3.
3D structure databases
ProteinModelPortal	P53045.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2799N.
IntAct	P53045. 57 interactions.
MINT	MINT-536282.
Proteomic databases
PaxDb	P53045.
PeptideAtlas	P53045.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR060W; YGR060W; YGR060W.
GeneID	852951.
KEGG	sce:YGR060W. sce:YGR067C.
Organism-specific databases
CYGD	YGR060w.
SGD	S000003292. ERG25.
Phylogenomic databases
eggNOG	COG3000.
GeneTree	ENSGT00530000063017.
HOGENOM	HOG000162289.
KO	K07750.
OMA	VLEDTWH.
OrthoDB	EOG4SN4XQ.
Enzyme and pathway databases
BioCyc	MetaCyc:YGR060W-MONOMER.
UniPathway	UPA00770; UER00756.
Gene expression databases
Genevestigator	P53045.
GermOnline	YGR060W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006694. Fatty_acid_hydroxylase. [Graphical view]
Pfam	PF04116. FA_hydroxylase. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972708.

Entry information

Entry name

MSMO_YEAST

Accession

Primary (citable) accession number: P53045
Secondary accession number(s): D6VUJ5, E9P8T3, Q45U26

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents