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Q9YAQ8

- MTAP_AERPE

UniProt

Q9YAQ8 - MTAP_AERPE

Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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.UniRule annotation

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei20 – 201PhosphateUniRule annotation
    Sitei176 – 1761Important for substrate specificityUniRule annotation
    Binding sitei195 – 1951Substrate; via amide nitrogenUniRule annotation
    Binding sitei196 – 1961PhosphateUniRule annotation
    Sitei230 – 2301Important 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

    BioCyciAPER272557:GJD6-1277-MONOMER.
    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
    Gene namesi
    Name:mtnPUniRule annotation
    Ordered Locus Names:APE_1885
    OrganismiAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
    Taxonomic identifieri272557 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum
    ProteomesiUP000002518: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 275275S-methyl-5'-thioadenosine phosphorylasePRO_0000415102Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi143 ↔ 210
    Disulfide bondi205 ↔ 266
    Disulfide bondi264 ↔ 267

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homohexamer. Dimer of a homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272557.APE_1885.

    Structurei

    Secondary structure

    1
    275
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Beta strandi13 – 186
    Helixi20 – 223
    Turni25 – 273
    Beta strandi29 – 368
    Beta strandi47 – 526
    Beta strandi55 – 617
    Turni62 – 676
    Helixi71 – 733
    Helixi76 – 8611
    Beta strandi90 – 10112
    Beta strandi114 – 1185
    Beta strandi130 – 1323
    Helixi144 – 15714
    Beta strandi161 – 1633
    Beta strandi166 – 1705
    Helixi178 – 1869
    Beta strandi191 – 1966
    Helixi197 – 20610
    Beta strandi210 – 21910
    Beta strandi223 – 2264
    Helixi230 – 25122
    Helixi252 – 2543
    Helixi261 – 2633
    Turni265 – 2684
    Helixi269 – 2713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WTAX-ray1.78A1-275[»]
    ProteinModelPortaliQ9YAQ8.
    SMRiQ9YAQ8. Positions 3-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9YAQ8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni62 – 632Phosphate bindingUniRule annotation
    Regioni95 – 962Phosphate bindingUniRule annotation
    Regioni219 – 2213Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000228987.
    KOiK00772.
    OMAiCEAQLCY.

    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.

    Q9YAQ8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFEITRPPGV RAHVGVIGGS GLYDPGIVEN PVEVKVSTPY GNPSDFIVVG    50
    DVAGVKVAFL PRHGRGHRIP PHAINYRANI WALKALGVKW VISVSAVGSL 100
    REDYRPGDFV VPDQFIDMTK NRRHYTFYDG PVTVHVSMAD PFCEDLRQRL 150
    IDSGRRLGYT VHERGTYVCI EGPRFSTRAE SRVWKDVFKA DIIGMTLVPE 200
    INLACEAQLC YATLAMVTDY DVWADRPVTA EEVERVMISN VERARRMLYD 250
    VIPKLAGEPE LERCSCCRAL DTAAI 275
    Length:275
    Mass (Da):30,737
    Last modified:November 1, 1999 - v1
    Checksum:i86CC11C1FB2DB091
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000002 Genomic DNA. Translation: BAA80890.1.
    PIRiE72575.
    RefSeqiNP_148238.1. NC_000854.2.

    Genome annotation databases

    EnsemblBacteriaiBAA80890; BAA80890; APE_1885.
    GeneIDi1446318.
    KEGGiape:APE_1885.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000002 Genomic DNA. Translation: BAA80890.1 .
    PIRi E72575.
    RefSeqi NP_148238.1. NC_000854.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WTA X-ray 1.78 A 1-275 [» ]
    ProteinModelPortali Q9YAQ8.
    SMRi Q9YAQ8. Positions 3-275.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272557.APE_1885.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA80890 ; BAA80890 ; APE_1885 .
    GeneIDi 1446318.
    KEGGi ape:APE_1885.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00873 .
    BioCyci APER272557:GJD6-1277-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9YAQ8.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
    2. "Crystal structure of 5'-deoxy-5'-methylthioadenosine from Aeropyrum pernix (R32 form)."
      Tsunoda M., Murakami Y., Nakamura K.T.
      Submitted (NOV-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.

    Entry informationi

    Entry nameiMTAP_AERPE
    AccessioniPrimary (citable) accession number: Q9YAQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 79 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