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P53045

- MSMO_YEAST

UniProt

P53045 - MSMO_YEAST

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Protein

Methylsterol monooxygenase

Gene

ERG25

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

Functioni

Catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol.1 Publication

Catalytic activityi

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.

Cofactori

Fe cation1 Publication

Pathwayi

GO - Molecular functioni

  1. C-4 methylsterol oxidase activity Source: SGD
  2. iron ion binding Source: InterPro

GO - Biological processi

  1. ergosterol biosynthetic process Source: SGD
  2. fatty acid biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

Iron, NAD

Enzyme and pathway databases

BioCyciMetaCyc:YGR060W-MONOMER.
YEAST:YGR060W-MONOMER.
ReactomeiREACT_253879. Cholesterol biosynthesis.
UniPathwayiUPA00770; UER00756.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylsterol monooxygenase (EC:1.14.13.72)
Alternative name(s):
C-4 methylsterol oxidase
Gene namesi
Name:ERG25
Synonyms:FET6
Ordered Locus Names:YGR060W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR060w.
SGDiS000003292. ERG25.

Subcellular locationi

Endoplasmic reticulum membrane 3 Publications; Single-pass membrane protein 3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei56 – 7621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: SGD
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Methylsterol monooxygenasePRO_0000117039Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki96 – 96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP53045.
PaxDbiP53045.
PeptideAtlasiP53045.

Expressioni

Gene expression databases

GenevestigatoriP53045.

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 ERG27 and ERG28.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERG11P106143EBI-6506,EBI-5127
ERG27Q124524EBI-6506,EBI-38132
ERG28P400303EBI-6506,EBI-22518
ERG3P323533EBI-6506,EBI-6554

Protein-protein interaction databases

BioGridi33305. 235 interactions.
DIPiDIP-2799N.
IntActiP53045. 60 interactions.
MINTiMINT-536282.

Structurei

3D structure databases

ProteinModelPortaliP53045.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi160 – 1645Histidine box-1
Motifi173 – 1775Histidine box-2
Motifi257 – 2637Histidine box-3

Domaini

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

Sequence similaritiesi

Belongs to the sterol desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3000.
GeneTreeiENSGT00530000063017.
HOGENOMiHOG000162289.
InParanoidiP53045.
KOiK07750.
OMAiEKQWKCF.
OrthoDBiEOG7NW6M8.

Family and domain databases

InterProiIPR006694. Fatty_acid_hydroxylase.
[Graphical view]
PfamiPF04116. FA_hydroxylase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53045-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAVFNNATL SGLVQASTYS QTLQNVAHYQ PQLNFMEKYW AAWYSYMNND
60 70 80 90 100
VLATGLMFFL LHEFMYFFRC LPWFIIDQIP YFRRWKLQPT KIPSAKEQLY
110 120 130 140 150
CLKSVLLSHF LVEAIPIWTF HPMCEKLGIT VEVPFPSLKT MALEIGLFFV
160 170 180 190 200
LEDTWHYWAH RLFHYGVFYK YIHKQHHRYA APFGLSAEYA HPAETLSLGF
210 220 230 240 250
GTVGMPILYV MYTGKLHLFT LCVWITLRLF QAVDSHSGYD FPWSLNKIMP
260 270 280 290 300
FWAGAEHHDL HHHYFIGNYA SSFRWWDYCL DTESGPEAKA SREERMKKRA

ENNAQKKTN
Length:309
Mass (Da):36,479
Last modified:October 1, 1996 - v1
Checksum:iE0422C416DD17794
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti302 – 3021N → K in AAS56153. (PubMed:17322287)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS64354.
RefSeqiNP_011574.3. NM_001181189.3.

Genome annotation databases

EnsemblFungiiYGR060W; YGR060W; YGR060W.
GeneIDi852951.
KEGGisce:YGR060W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi S64354.
RefSeqi NP_011574.3. NM_001181189.3.

3D structure databases

ProteinModelPortali P53045.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33305. 235 interactions.
DIPi DIP-2799N.
IntActi P53045. 60 interactions.
MINTi MINT-536282.

Proteomic databases

MaxQBi P53045.
PaxDbi P53045.
PeptideAtlasi P53045.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR060W ; YGR060W ; YGR060W .
GeneIDi 852951.
KEGGi sce:YGR060W.

Organism-specific databases

CYGDi YGR060w.
SGDi S000003292. ERG25.

Phylogenomic databases

eggNOGi COG3000.
GeneTreei ENSGT00530000063017.
HOGENOMi HOG000162289.
InParanoidi P53045.
KOi K07750.
OMAi EKQWKCF.
OrthoDBi EOG7NW6M8.

Enzyme and pathway databases

UniPathwayi UPA00770 ; UER00756 .
BioCyci MetaCyc:YGR060W-MONOMER.
YEAST:YGR060W-MONOMER.
Reactomei REACT_253879. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi 972708.
PROi P53045.

Gene expression databases

Genevestigatori P53045.

Family and domain databases

InterProi IPR006694. Fatty_acid_hydroxylase.
[Graphical view ]
Pfami PF04116. FA_hydroxylase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. 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. 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.
  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.
  12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMSMO_YEAST
AccessioniPrimary (citable) accession number: P53045
Secondary accession number(s): D6VUJ5, E9P8T3, Q45U26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 77100 molecules/cell in log phase SD medium.1 Publication

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

External Data

Dasty 3