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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 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 annotation1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.7 mM for S-methyl-5'-thioadenosine1 Publication
  2. KM=270 µM for adenosine1 Publication

    Temperature dependencei

    Optimum temperature is 120 degrees Celsius. Highly thermostable.1 Publication

    Pathway: L-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 sitei16 – 161PhosphateUniRule annotation
    Sitei171 – 1711Important for substrate specificityUniRule annotation
    Binding sitei190 – 1901Substrate; via amide nitrogenUniRule annotation
    Binding sitei191 – 1911PhosphateUniRule annotation
    Sitei225 – 2251Important 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

    BioCyciSSOL273057:GCH2-2180-MONOMER.
    BRENDAi2.4.2.28. 6163.
    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:
    MTAPIIUniRule annotation
    Gene namesi
    Name:mtnPUniRule annotation
    Ordered Locus Names:SSO2343
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001974 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi259 – 2591C → S: Reduces thermostability of the enzyme; when associated with S-261. 1 Publication
    Mutagenesisi261 – 2611C → S: Reduces thermostability of the enzyme; when associated with S-259. 1 Publication
    Mutagenesisi262 – 2621C → S: Reduces thermostability of the enzyme. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 270270S-methyl-5'-thioadenosine phosphorylasePRO_0000415109Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi138 ↔ 2051 Publication
    Disulfide bondi200 ↔ 2621 Publication
    Disulfide bondi259 ↔ 2611 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homohexamer. Dimer of a homotrimer.UniRule annotation2 Publications

    Protein-protein interaction databases

    STRINGi273057.SSO2343.

    Structurei

    Secondary structure

    1
    270
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 146Combined sources
    Beta strandi25 – 306Combined sources
    Beta strandi43 – 486Combined sources
    Beta strandi51 – 577Combined sources
    Turni58 – 603Combined sources
    Helixi61 – 633Combined sources
    Helixi67 – 693Combined sources
    Helixi72 – 8110Combined sources
    Beta strandi86 – 9712Combined sources
    Beta strandi110 – 1145Combined sources
    Beta strandi125 – 1273Combined sources
    Helixi139 – 15214Combined sources
    Beta strandi156 – 1583Combined sources
    Beta strandi161 – 1655Combined sources
    Helixi173 – 1819Combined sources
    Beta strandi187 – 1915Combined sources
    Helixi192 – 20110Combined sources
    Beta strandi205 – 21410Combined sources
    Beta strandi218 – 2214Combined sources
    Helixi225 – 23410Combined sources
    Helixi236 – 24914Combined sources
    Helixi256 – 2583Combined sources
    Turni260 – 2634Combined sources
    Helixi266 – 2683Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A8YX-ray1.45A/B/C/D/E/F/G/H/I/J/K/L1-270[»]
    3T94X-ray1.45A/B/C/D/E/F1-270[»]
    ProteinModelPortaliQ97W94.
    SMRiQ97W94. Positions 1-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ97W94.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 592Phosphate bindingUniRule annotation
    Regioni91 – 922Phosphate bindingUniRule annotation
    Regioni214 – 2163Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000228986.
    InParanoidiQ97W94.
    KOiK00772.
    OMAiMTNHTEA.

    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.

    Q97W94-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIEQNEKASI GIIGGSGLYD PGIFSESKEI KVYTPYGQPS DFITIGKIGN
    60 70 80 90 100
    KSVAFLPRHG RGHRIPPHKI NYRANIWALK ELGVRWVISV SAVGSLRMDY
    110 120 130 140 150
    KLGDFVIPDQ FIDMTKNREY SFFDGPVVAH VSMADPFCNS LRKLAIETAK
    160 170 180 190 200
    ELNIKTHESG TYICIEGPRF STRAESRTWR EVYKADIIGM TLVPEVNLAC
    210 220 230 240 250
    EAQMCYATIA MVTDYDVFAE IPVTAEEVTR VMAENTEKAK KLLYALIQKL
    260 270
    PEKPEEGSCS CCNSLKTALV
    Length:270
    Mass (Da):30,141
    Last modified:October 1, 2001 - v1
    Checksum:i682A166698935A88
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006641 Genomic DNA. Translation: AAK42494.1.
    PIRiG90404.
    RefSeqiNP_343704.1. NC_002754.1.
    WP_009989516.1. NC_002754.1.

    Genome annotation databases

    EnsemblBacteriaiAAK42494; AAK42494; SSO2343.
    GeneIDi1453821.
    KEGGisso:SSO2343.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006641 Genomic DNA. Translation: AAK42494.1.
    PIRiG90404.
    RefSeqiNP_343704.1. NC_002754.1.
    WP_009989516.1. NC_002754.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A8YX-ray1.45A/B/C/D/E/F/G/H/I/J/K/L1-270[»]
    3T94X-ray1.45A/B/C/D/E/F1-270[»]
    ProteinModelPortaliQ97W94.
    SMRiQ97W94. Positions 1-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273057.SSO2343.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK42494; AAK42494; SSO2343.
    GeneIDi1453821.
    KEGGisso:SSO2343.

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000228986.
    InParanoidiQ97W94.
    KOiK00772.
    OMAiMTNHTEA.

    Enzyme and pathway databases

    UniPathwayiUPA00904; UER00873.
    BioCyciSSOL273057:GCH2-2180-MONOMER.
    BRENDAi2.4.2.28. 6163.

    Miscellaneous databases

    EvolutionaryTraceiQ97W94.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    2. "A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus."
      Cacciapuoti G., Forte S., Moretti M.A., Brio A., Zappia V., Porcelli M.
      FEBS J. 272:1886-1899(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-259; CYS-261 AND CYS-262, SUBUNIT.
    3. "The crystal structure of 5'-deoxy-5'-methylthioadenosine phosphorylase II from Sulfolobus solfataricus, a thermophilic enzyme stabilized by intramolecular disulfide bonds."
      Zhang Y., Porcelli M., Cacciapuoti G., Ealick S.E.
      J. Mol. Biol. 357:252-262(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, DISULFIDE BONDS.

    Entry informationi

    Entry nameiMTAP_SULSO
    AccessioniPrimary (citable) accession number: Q97W94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: October 1, 2001
    Last modified: May 27, 2015
    This is version 75 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.