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Q8U4Q8

- MTAP_PYRFU

UniProt

Q8U4Q8 - MTAP_PYRFU

Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.3 PublicationsUniRule annotation

    Catalytic activityi

    S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation

    Kineticsi

    1. KM=147 µM for S-methyl-5'-thioadenosine1 Publication
    2. KM=109 µM for adenosine1 Publication
    3. KM=963 µM for inosine1 Publication
    4. KM=916 µM for guanosine1 Publication

    pH dependencei

    Optimum pH is 7.4. Active from pH 5 to 10.1 Publication

    Temperature dependencei

    Optimum temperature is 125 degrees Celsius. Thermostable up to 137 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101PhosphateUniRule annotation
    Sitei163 – 1631Important for substrate specificityUniRule annotation
    Binding sitei180 – 1801Substrate; via amide nitrogenUniRule annotation
    Binding sitei181 – 1811PhosphateUniRule annotation
    Sitei215 – 2151Important for substrate specificityUniRule annotation

    GO - Molecular functioni

    1. phosphorylase activity Source: InterPro
    2. S-methyl-5-thioadenosine phosphorylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB-HAMAP
    2. purine ribonucleoside salvage Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Enzyme and pathway databases

    SABIO-RKQ8U4Q8.
    UniPathwayiUPA00904; UER00873.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-methyl-5'-thioadenosine phosphorylaseUniRule annotation (EC:2.4.2.28UniRule annotation)
    Alternative name(s):
    5'-methylthioadenosine phosphorylaseUniRule annotation
    Short name:
    MTA phosphorylaseUniRule annotation
    Short name:
    MTAPUniRule annotation
    Short name:
    PfMTAP
    Gene namesi
    Name:mtnPUniRule annotation
    Ordered Locus Names:PF0016
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000001013: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 257257S-methyl-5'-thioadenosine phosphorylasePRO_0000415107Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi130 ↔ 1951 Publication
    Disulfide bondi246 ↔ 2481 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ8U4Q8.

    Interactioni

    Subunit structurei

    Homohexamer. Dimer of a homotrimer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi186497.PF0016.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8U4Q8.
    SMRiQ8U4Q8. Positions 4-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 512Phosphate bindingUniRule annotation
    Regioni204 – 2063Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000228987.
    KOiK00772.
    OMAiDYTFYNG.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    HAMAPiMF_01963. MTAP.
    InterProiIPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01694. MTAP. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8U4Q8-1 [UniParc]FASTAAdd to Basket

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    MPKIGIIGGS GVYGIFEPKE TVKVHTPYGR PSAPVEIGEI EGVEVAFIPR    50
    HGKYHEFPPH EVPYRANIWA LHELGVERVI AVNAVGSLKE EYKPGDIVII 100
    DQFIDFTKKR EYTFYNGPRV AHISMADPFC PELRRIFIET AKELNLPVHE 150
    KGTYICIEGP RFSTRAESRM FRQFADVIGM TLVPEVNLAR ELGMCYVNIS 200
    TVTDYDVWAE KPVDAQEVLR VMKENEEKVQ KLLKRAIPKI PEERKCGCAD 250
    VLKTMFV 257
    Length:257
    Mass (Da):29,220
    Last modified:June 1, 2002 - v1
    Checksum:iA1B8194889A30AB8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80140.1.
    RefSeqiNP_577745.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL80140; AAL80140; PF0016.
    GeneIDi1467844.
    KEGGipfu:PF0016.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80140.1 .
    RefSeqi NP_577745.1. NC_003413.1.

    3D structure databases

    ProteinModelPortali Q8U4Q8.
    SMRi Q8U4Q8. Positions 4-243.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 186497.PF0016.

    Proteomic databases

    PRIDEi Q8U4Q8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL80140 ; AAL80140 ; PF0016 .
    GeneIDi 1467844.
    KEGGi pfu:PF0016.

    Phylogenomic databases

    eggNOGi COG0005.
    HOGENOMi HOG000228987.
    KOi K00772.
    OMAi DYTFYNG.

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00873 .
    SABIO-RK Q8U4Q8.

    Family and domain databases

    Gene3Di 3.40.50.1580. 1 hit.
    HAMAPi MF_01963. MTAP.
    InterProi IPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view ]
    PANTHERi PTHR11904. PTHR11904. 1 hit.
    Pfami PF01048. PNP_UDP_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53167. SSF53167. 1 hit.
    TIGRFAMsi TIGR01694. MTAP. 1 hit.
    PROSITEi PS01240. PNP_MTAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    2. "Purification and characterization of 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus: substrate specificity and primary structure analysis."
      Cacciapuoti G., Bertoldo C., Brio A., Zappia V., Porcelli M.
      Extremophiles 7:159-168(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-27, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    3. "Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds."
      Cacciapuoti G., Moretti M.A., Forte S., Brio A., Camardella L., Zappia V., Porcelli M.
      Eur. J. Biochem. 271:4834-4844(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISULFIDE BONDS.
    4. "Unraveling the structural and functional differences between purine nucleoside phosphorylase and 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus."
      Cacciapuoti G., Marabotti A., Fuccio F., Porcelli M.
      Biochim. Biophys. Acta 1814:1358-1366(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMTAP_PYRFU
    AccessioniPrimary (citable) accession number: Q8U4Q8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3