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P39954

- SAHH_YEAST

UniProt

P39954 - SAHH_YEAST

Protein

Adenosylhomocysteinase

Gene

SAH1

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 125 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.By similarity

    Catalytic activityi

    S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.

    Cofactori

    Binds 1 NAD per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei58 – 581SubstrateBy similarity
    Binding sitei134 – 1341SubstrateBy similarity
    Binding sitei159 – 1591SubstrateBy similarity
    Binding sitei189 – 1891SubstrateBy similarity
    Binding sitei193 – 1931SubstrateBy similarity
    Binding sitei194 – 1941NADBy similarity
    Binding sitei246 – 2461NADBy similarity
    Binding sitei349 – 3491NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi160 – 1623NADBy similarity
    Nucleotide bindingi223 – 2286NADBy similarity
    Nucleotide bindingi302 – 3043NADBy similarity

    GO - Molecular functioni

    1. adenosylhomocysteinase activity Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. methionine metabolic process Source: SGD
    2. one-carbon metabolic process Source: UniProtKB-KW
    3. phosphatidylcholine biosynthetic process Source: SGD
    4. S-adenosylhomocysteine catabolic process Source: SGD
    5. triglyceride metabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciYEAST:YER043C-MONOMER.
    ReactomeiREACT_188464. Sulfur amino acid metabolism.
    UniPathwayiUPA00314; UER00076.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenosylhomocysteinase (EC:3.3.1.1)
    Short name:
    AdoHcyase
    Alternative name(s):
    S-adenosyl-L-homocysteine hydrolase
    Gene namesi
    Name:SAH1
    Ordered Locus Names:YER043C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER043c.
    SGDiS000000845. SAH1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 449448AdenosylhomocysteinasePRO_0000116937Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei393 – 3931Phosphothreonine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP39954.
    PaxDbiP39954.
    PeptideAtlasiP39954.
    PRIDEiP39954.

    Expressioni

    Gene expression databases

    GenevestigatoriP39954.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAF16P435693EBI-16451,EBI-22808

    Protein-protein interaction databases

    BioGridi36779. 36 interactions.
    DIPiDIP-5184N.
    IntActiP39954. 6 interactions.
    MINTiMINT-538156.
    STRINGi4932.YER043C.

    Structurei

    3D structure databases

    ProteinModelPortaliP39954.
    SMRiP39954. Positions 8-449.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the adenosylhomocysteinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0499.
    GeneTreeiENSGT00390000003626.
    HOGENOMiHOG000227987.
    KOiK01251.
    OMAiTRVNIKP.
    OrthoDBiEOG7FZ07M.

    Family and domain databases

    HAMAPiMF_00563. AdoHcyase.
    InterProiIPR000043. Adenosylhomocysteinase.
    IPR015878. Ado_hCys_hydrolase_NAD-bd.
    IPR020082. S-Ado-L-homoCys_hydrolase_CS.
    [Graphical view]
    PANTHERiPTHR23420. PTHR23420. 1 hit.
    PfamiPF05221. AdoHcyase. 1 hit.
    PF00670. AdoHcyase_NAD. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
    SMARTiSM00996. AdoHcyase. 1 hit.
    SM00997. AdoHcyase_NAD. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00936. ahcY. 1 hit.
    PROSITEiPS00738. ADOHCYASE_1. 1 hit.
    PS00739. ADOHCYASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P39954-1 [UniParc]FASTAAdd to Basket

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    MSAPAQNYKI ADISLAAFGR KEIELAEHEM PGLMAIRKAY GDVQPLKGAR    50
    IAGCLHMTIQ TAVLIETLVA LGAEVTWSSC NIYSTQDHAA AAIAASGVPV 100
    FAWKGETEEE YLWCIEQQLF AFKDNKKLNL ILDDGGDLTT LVHEKHPEML 150
    EDCFGLSEET TTGVHHLYRM VKEGKLKVPA INVNDSVTKS KFDNLYGCRE 200
    SLVDGIKRAT DVMLAGKVAV VAGYGDVGKG CAAALRGMGA RVLVTEIDPI 250
    NALQAAMEGY QVVTMEDASH IGQVFVTTTG CRDIINGEHF INMPEDAIVC 300
    NIGHFDIEID VAWLKANAKE CINIKPQVDR YLLSSGRHVI LLANGRLVNL 350
    GCATGHSSFV MSCSFSNQVL AQIALFKSND KSFREKHIEF QKTGPFEVGV 400
    HVLPKILDEA VAKFHLGNLG VRLTKLSKVQ SEYLGIPEEG PFKADHYRY 449
    Length:449
    Mass (Da):49,126
    Last modified:February 1, 1995 - v1
    Checksum:iD98D9DD329374F5B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18796 Genomic DNA. Translation: AAB64578.1.
    AY692801 Genomic DNA. Translation: AAT92820.1.
    BK006939 Genomic DNA. Translation: DAA07697.1.
    PIRiS50546.
    RefSeqiNP_010961.3. NM_001178934.3.

    Genome annotation databases

    EnsemblFungiiYER043C; YER043C; YER043C.
    GeneIDi856766.
    KEGGisce:YER043C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18796 Genomic DNA. Translation: AAB64578.1 .
    AY692801 Genomic DNA. Translation: AAT92820.1 .
    BK006939 Genomic DNA. Translation: DAA07697.1 .
    PIRi S50546.
    RefSeqi NP_010961.3. NM_001178934.3.

    3D structure databases

    ProteinModelPortali P39954.
    SMRi P39954. Positions 8-449.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36779. 36 interactions.
    DIPi DIP-5184N.
    IntActi P39954. 6 interactions.
    MINTi MINT-538156.
    STRINGi 4932.YER043C.

    Proteomic databases

    MaxQBi P39954.
    PaxDbi P39954.
    PeptideAtlasi P39954.
    PRIDEi P39954.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER043C ; YER043C ; YER043C .
    GeneIDi 856766.
    KEGGi sce:YER043C.

    Organism-specific databases

    CYGDi YER043c.
    SGDi S000000845. SAH1.

    Phylogenomic databases

    eggNOGi COG0499.
    GeneTreei ENSGT00390000003626.
    HOGENOMi HOG000227987.
    KOi K01251.
    OMAi TRVNIKP.
    OrthoDBi EOG7FZ07M.

    Enzyme and pathway databases

    UniPathwayi UPA00314 ; UER00076 .
    BioCyci YEAST:YER043C-MONOMER.
    Reactomei REACT_188464. Sulfur amino acid metabolism.

    Miscellaneous databases

    NextBioi 982947.
    PROi P39954.

    Gene expression databases

    Genevestigatori P39954.

    Family and domain databases

    HAMAPi MF_00563. AdoHcyase.
    InterProi IPR000043. Adenosylhomocysteinase.
    IPR015878. Ado_hCys_hydrolase_NAD-bd.
    IPR020082. S-Ado-L-homoCys_hydrolase_CS.
    [Graphical view ]
    PANTHERi PTHR23420. PTHR23420. 1 hit.
    Pfami PF05221. AdoHcyase. 1 hit.
    PF00670. AdoHcyase_NAD. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001109. Ad_hcy_hydrolase. 1 hit.
    SMARTi SM00996. AdoHcyase. 1 hit.
    SM00997. AdoHcyase_NAD. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00936. ahcY. 1 hit.
    PROSITEi PS00738. ADOHCYASE_1. 1 hit.
    PS00739. ADOHCYASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "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-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    5. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "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 nameiSAHH_YEAST
    AccessioniPrimary (citable) accession number: P39954
    Secondary accession number(s): D3DLU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3