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P15274

- AMPD_YEAST

UniProt

P15274 - AMPD_YEAST

Protein

AMP deaminase

Gene

AMD1

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 137 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    AMP deaminase plays a critical role in energy metabolism.

    Catalytic activityi

    AMP + H2O = IMP + NH3.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi362 – 3621Zinc; catalyticBy similarity
    Metal bindingi364 – 3641Zinc; catalyticBy similarity
    Binding sitei364 – 3641SubstrateBy similarity
    Metal bindingi630 – 6301Zinc; catalyticBy similarity
    Binding sitei633 – 6331SubstrateBy similarity
    Active sitei652 – 6521Proton acceptorPROSITE-ProRule annotation
    Metal bindingi707 – 7071Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. AMP deaminase activity Source: SGD
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. guanine salvage Source: SGD
    2. IMP salvage Source: UniProtKB-UniPathway
    3. purine nucleotide metabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:YML035C-MONOMER.
    UniPathwayiUPA00591; UER00663.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AMP deaminase (EC:3.5.4.6)
    Alternative name(s):
    Myoadenylate deaminase
    Gene namesi
    Name:AMD1
    Synonyms:AMD
    Ordered Locus Names:YML035C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYML035c.
    SGDiS000004498. AMD1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 810810AMP deaminasePRO_0000194414Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphoserine2 Publications
    Modified residuei58 – 581Phosphoserine3 Publications
    Modified residuei61 – 611Phosphoserine3 Publications
    Modified residuei138 – 1381Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP15274.
    PaxDbiP15274.
    PeptideAtlasiP15274.

    Expressioni

    Gene expression databases

    GenevestigatoriP15274.

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRP40P332032EBI-2548,EBI-701

    Protein-protein interaction databases

    BioGridi35135. 83 interactions.
    DIPiDIP-1949N.
    IntActiP15274. 10 interactions.
    MINTiMINT-408221.
    STRINGi4932.YML035C.

    Structurei

    3D structure databases

    ProteinModelPortaliP15274.
    SMRiP15274. Positions 299-797.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni433 – 4386Substrate bindingBy similarity
    Regioni708 – 7114Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1816.
    GeneTreeiENSGT00390000008190.
    HOGENOMiHOG000092200.
    KOiK01490.
    OMAiPRDIPHR.
    OrthoDBiEOG7N63W7.

    Family and domain databases

    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view]
    PANTHERiPTHR11359. PTHR11359. 1 hit.
    PfamiPF00962. A_deaminase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
    TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
    PROSITEiPS00485. A_DEAMINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P15274-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNQATQRLN DLSLEPAPSH DEQDGSGLVI DIDQRKIGDE QAGVVVDDET    50
    PPLEQQDSHE SLAADSRNAN FSYHENQQLL ENGTKQLALD EHDSHSAILE 100
    QPSHSTNCSS SNIAAMNKGH DSADHASQNS GGKPRTLSAS AQHILPETLK 150
    SFAGAPVVNK QVRTSASYKM GMLADDASQQ FLDDPSSELI DLYSKVAECR 200
    NLRAKYQTIS VQNDDQNPKN KPGWVVYPPP PKPSYNSDTK TVVPVTNKPD 250
    AEVFDFTKCE IPGEDPDWEF TLNDDDSYVV HRSGKTDELI AQIPTLRDYY 300
    LDLEKMISIS SDGPAKSFAY RRLQYLEARW NLYYLLNEYQ ETSVSKRNPH 350
    RDFYNVRKVD THVHHSACMN QKHLLRFIKH KLRHSKDEKV IFRDGKLLTL 400
    DEVFRSLHLT GYDLSIDTLD MHAHKDTFHR FDKFNLKYNP IGESRLREIF 450
    LKTNNYIKGT YLADITKQVI FDLENSKYQN CEYRISVYGR SLDEWDKLAS 500
    WVIDNKVISH NVRWLVQIPR LYDIYKKTGI VQSFQDICKN LFQPLFEVTK 550
    NPQSHPKLHV FLQRVIGFDS VDDESKVDRR FHRKYPKPSL WEAPQNPPYS 600
    YYLYYLYSNV ASLNQWRAKR GFNTLVLRPH CGEAGDPEHL VSAYLLAHGI 650
    SHGILLRKVP FVQYLYYLDQ VGIAMSPLSN NALFLTYDKN PFPRYFKRGL 700
    NVSLSTDDPL QFSYTREPLI EEYSVAAQIY KLSNVDMCEL ARNSVLQSGW 750
    EAQIKKHWIG KDFDKSGVEG NDVVRTNVPD IRINYRYDTL STELELVNHF 800
    ANFKRTIEEK 810
    Length:810
    Mass (Da):93,302
    Last modified:February 1, 1996 - v2
    Checksum:i7A6DCB43B9B45C93
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti568 – 5681F → C in AAA34420. (PubMed:2690949)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30449 Genomic DNA. Translation: AAA34420.1.
    Z46659 Genomic DNA. Translation: CAA86620.1.
    BK006946 Genomic DNA. Translation: DAA09864.1.
    PIRiS49744.
    RefSeqiNP_013677.1. NM_001182392.1.

    Genome annotation databases

    EnsemblFungiiYML035C; YML035C; YML035C.
    GeneIDi854973.
    KEGGisce:YML035C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30449 Genomic DNA. Translation: AAA34420.1 .
    Z46659 Genomic DNA. Translation: CAA86620.1 .
    BK006946 Genomic DNA. Translation: DAA09864.1 .
    PIRi S49744.
    RefSeqi NP_013677.1. NM_001182392.1.

    3D structure databases

    ProteinModelPortali P15274.
    SMRi P15274. Positions 299-797.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35135. 83 interactions.
    DIPi DIP-1949N.
    IntActi P15274. 10 interactions.
    MINTi MINT-408221.
    STRINGi 4932.YML035C.

    Proteomic databases

    MaxQBi P15274.
    PaxDbi P15274.
    PeptideAtlasi P15274.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YML035C ; YML035C ; YML035C .
    GeneIDi 854973.
    KEGGi sce:YML035C.

    Organism-specific databases

    CYGDi YML035c.
    SGDi S000004498. AMD1.

    Phylogenomic databases

    eggNOGi COG1816.
    GeneTreei ENSGT00390000008190.
    HOGENOMi HOG000092200.
    KOi K01490.
    OMAi PRDIPHR.
    OrthoDBi EOG7N63W7.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00663 .
    BioCyci YEAST:YML035C-MONOMER.

    Miscellaneous databases

    NextBioi 978079.

    Gene expression databases

    Genevestigatori P15274.

    Family and domain databases

    InterProi IPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view ]
    PANTHERi PTHR11359. PTHR11359. 1 hit.
    Pfami PF00962. A_deaminase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001251. AMP_deaminase_met. 1 hit.
    TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
    PROSITEi PS00485. A_DEAMINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of AMD, the AMP deaminase gene in yeast. Production of amd strain, cloning, nucleotide sequence, and properties of the protein."
      Meyer S.L., Kvalnes-Krick K.L., Schramm V.L.
      Biochemistry 28:8734-8743(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    6. "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 SER-58; SER-61 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "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 SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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 SER-19; SER-58 AND SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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 SER-19; SER-58 AND SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAMPD_YEAST
    AccessioniPrimary (citable) accession number: P15274
    Secondary accession number(s): D6VZE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 3910 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3