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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.UniRule annotation3 Publications

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

    Pathway:iL-methionine biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route).UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. S-methyl-5'-thioadenosine phosphorylase (mtnP)
    This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

    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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Enzyme and pathway databases

    BRENDAi2.4.2.28. 5243.
    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 Componenti: 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.UniRule annotation1 Publication

    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.
    OMAiHTPYGRP.

    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

    « Hide

            10         20         30         40         50
    MPKIGIIGGS GVYGIFEPKE TVKVHTPYGR PSAPVEIGEI EGVEVAFIPR
    60 70 80 90 100
    HGKYHEFPPH EVPYRANIWA LHELGVERVI AVNAVGSLKE EYKPGDIVII
    110 120 130 140 150
    DQFIDFTKKR EYTFYNGPRV AHISMADPFC PELRRIFIET AKELNLPVHE
    160 170 180 190 200
    KGTYICIEGP RFSTRAESRM FRQFADVIGM TLVPEVNLAR ELGMCYVNIS
    210 220 230 240 250
    TVTDYDVWAE KPVDAQEVLR VMKENEEKVQ KLLKRAIPKI PEERKCGCAD

    VLKTMFV
    Length:257
    Mass (Da):29,220
    Last modified:June 1, 2002 - v1
    Checksum:iA1B8194889A30AB8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80140.1.
    RefSeqiNP_577745.1. NC_003413.1.
    WP_011011128.1. NC_003413.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80140.1.
    RefSeqiNP_577745.1. NC_003413.1.
    WP_011011128.1. NC_003413.1.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi186497.PF0016.

    Proteomic databases

    PRIDEiQ8U4Q8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000228987.
    KOiK00772.
    OMAiHTPYGRP.

    Enzyme and pathway databases

    UniPathwayiUPA00904; UER00873.
    BRENDAi2.4.2.28. 5243.
    SABIO-RKQ8U4Q8.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: April 1, 2015
    This is version 70 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.