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P53045

- MSMO_YEAST

UniProt

P53045 - MSMO_YEAST

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
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    Iron.1 Publication

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

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

    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.
    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

    GO - Cellular componenti

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

    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...

    Transmembrane

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

    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.
    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

    MSAVFNNATL SGLVQASTYS QTLQNVAHYQ PQLNFMEKYW AAWYSYMNND    50
    VLATGLMFFL LHEFMYFFRC LPWFIIDQIP YFRRWKLQPT KIPSAKEQLY 100
    CLKSVLLSHF LVEAIPIWTF HPMCEKLGIT VEVPFPSLKT MALEIGLFFV 150
    LEDTWHYWAH RLFHYGVFYK YIHKQHHRYA APFGLSAEYA HPAETLSLGF 200
    GTVGMPILYV MYTGKLHLFT LCVWITLRLF QAVDSHSGYD FPWSLNKIMP 250
    FWAGAEHHDL HHHYFIGNYA SSFRWWDYCL DTESGPEAKA SREERMKKRA 300
    ENNAQKKTN 309
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    KOi K07750.
    OMAi EKQWKCF.
    OrthoDBi EOG7NW6M8.

    Enzyme and pathway databases

    UniPathwayi UPA00770 ; UER00756 .
    BioCyci MetaCyc:YGR060W-MONOMER.
    YEAST:YGR060W-MONOMER.

    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

    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: October 1, 2014
    This is version 124 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