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P50998

- AMPD_SCHPO

UniProt

P50998 - AMPD_SCHPO

Protein

AMP deaminase

Gene

ada1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 3 (11 Jul 2012)
      Previous versions | rss
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    Functioni

    AMP deaminase plays a critical role in energy metabolism.

    Catalytic activityi

    AMP + H2O = IMP + NH3.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi319 – 3191Zinc; catalyticBy similarity
    Metal bindingi321 – 3211Zinc; catalyticBy similarity
    Binding sitei321 – 3211SubstrateBy similarity
    Metal bindingi587 – 5871Zinc; catalyticBy similarity
    Binding sitei590 – 5901SubstrateBy similarity
    Active sitei609 – 6091Proton acceptorPROSITE-ProRule annotation
    Metal bindingi664 – 6641Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. AMP deaminase activity Source: PomBase
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. IMP salvage Source: UniProtKB-UniPathway
    2. regulation of transcription from RNA polymerase II promoter Source: PomBase

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00591; UER00663.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AMP deaminase (EC:3.5.4.6)
    Alternative name(s):
    Myoadenylate deaminase
    Gene namesi
    Name:ada1
    ORF Names:SPBC106.04
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC106.04.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. cytosol Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 831831AMP deaminasePRO_0000194413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791Phosphoserine1 Publication
    Modified residuei84 – 841Phosphoserine1 Publication
    Modified residuei758 – 7581Phosphoserine1 Publication
    Modified residuei776 – 7761Phosphoserine1 Publication
    Modified residuei780 – 7801Phosphoserine1 Publication
    Modified residuei782 – 7821Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP50998.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi276642. 73 interactions.
    MINTiMINT-4690806.
    STRINGi4896.SPBC106.04-1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni390 – 3956Substrate bindingBy similarity
    Regioni665 – 6684Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1816.
    HOGENOMiHOG000092200.
    KOiK01490.
    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.

    P50998-1 [UniParc]FASTAAdd to Basket

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    MNMEQEDDQV PAVAAETVPL KRYVTNPGAN RDEEVAAAPS SQDTPYFDYA    50
    YERSLRHQDA KFLAMNGTQN GRDGLPSKSP RRPSVSASTV RNSDDVNHSK 100
    AGPGSGKLLN DTLQSKISSI HMPHVQQGDN AVVSSVGGPE TDPGNMETTD 150
    PLFSDELAEI YLSIHKCMDM RHKYIRVSLQ GELDNPIDDD SWIIYPDCKE 200
    GEDDTGLFNF ADCKIPGIEN EMEYHMDHQG IFQVYENDSA YIAGTPSFHI 250
    PTIRDYYIDL EFLLSASSDG PSKSFSFRRL QYLEGRWNMY MLLNEYQELA 300
    DTKKVPHRDF YNVRKVDTHV HHSALANQKH LLRFIKAKLR KCPNEKVIWR 350
    DGKFLTLQEV FDSLKLTSYD LSIDTLDMHA HTDTFHRFDK FNLKYNPIGE 400
    SRLRTIFLKT DNDINGRYLA ELTKEVFTDL RTQKYQMAEY RISIYGRNRE 450
    EWDKLAAWII DNELFSPNVR WLIQVPRLYD VYKKSGIVET FEEVVRNVFE 500
    PLFEVTKDPR THPKLHVFLQ RVIGFDSVDD ESKPERRTFR KFPYPKHWDI 550
    NLNPPYSYWL YYMYANMTSL NSWRKIRGFN TFVLRPHCGE AGDTDHLASA 600
    FLLSHGINHG ILLRKVPFLQ YLWYLDQIPI AMSPLSNNAL FLAYDKNPFL 650
    TYFKRGLNVS LSTDDPLQFA FTREPLIEEY AVAAQIYKLS AVDMCELARN 700
    SVLQSGFERQ LKERWLGVDF QDIDRTNVPI IRLAYRALTL TQEIALVNKH 750
    VQPSKHPSNH DLEELIHKYD AMTGTSDPLS ASPRTNDATI SSRLSLHDGH 800
    DHGAFFPGLS VISERRRRKD SMASSSQDLK D 831
    Length:831
    Mass (Da):95,887
    Last modified:July 11, 2012 - v3
    Checksum:iF027B33C7AD0C63D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti468 – 50538NVRWL…PLFEV → TFVGLFKYLVCMMCIRSPVL LRLLKRSSEMSLNHCSKF in CAA62797. 1 PublicationCuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91498 Genomic DNA. Translation: CAA62797.1. Sequence problems.
    CU329671 Genomic DNA. Translation: CAB53720.2.
    PIRiT39261.
    RefSeqiNP_595153.2. NM_001021062.2.

    Genome annotation databases

    EnsemblFungiiSPBC106.04.1; SPBC106.04.1:pep; SPBC106.04.
    GeneIDi2540105.
    KEGGispo:SPBC106.04.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91498 Genomic DNA. Translation: CAA62797.1 . Sequence problems.
    CU329671 Genomic DNA. Translation: CAB53720.2 .
    PIRi T39261.
    RefSeqi NP_595153.2. NM_001021062.2.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276642. 73 interactions.
    MINTi MINT-4690806.
    STRINGi 4896.SPBC106.04-1.

    Proteomic databases

    MaxQBi P50998.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC106.04.1 ; SPBC106.04.1:pep ; SPBC106.04 .
    GeneIDi 2540105.
    KEGGi spo:SPBC106.04.

    Organism-specific databases

    PomBasei SPBC106.04.

    Phylogenomic databases

    eggNOGi COG1816.
    HOGENOMi HOG000092200.
    KOi K01490.
    OrthoDBi EOG7N63W7.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00663 .

    Miscellaneous databases

    NextBioi 20801241.

    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. Rochet M., Levesque H., Gaillardin C.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. "Comparative functional genomics of the fission yeasts."
      Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
      , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
      Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVISION OF GENE MODEL.
    4. "Yeast AMP deaminase. Catalytic activity in Schizosaccharomyces pombe and chromosomal location in Saccharomyces cerevisiae."
      Sollitti P., Merkler D.J., Estupinan B., Schramm V.L.
      J. Biol. Chem. 268:4549-4555(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    5. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
      Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
      Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-84; SER-758; SER-776; SER-780 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiAMPD_SCHPO
    AccessioniPrimary (citable) accession number: P50998
    Secondary accession number(s): Q9URV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 11, 2012
    Last modified: October 1, 2014
    This is version 102 of the entry and version 3 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. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3