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O06401

- MTAP_MYCTU

UniProt

O06401 - MTAP_MYCTU

Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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. Prefers MTA, with 2% activity on adenosine, 0.8% activity on S-adenosyl-L-homocysteine and no activity on other tested nucleosides.

    Catalytic activityi

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

    Enzyme regulationi

    Not inhibited by adenosine, potently inhibited by MT-DADMe-immucillin A.1 Publication

    Kineticsi

    1. KM=9 µM for S-methyl-5'-thioadenosine1 Publication
    2. KM=260 µM for phosphate1 Publication
    3. KM=1700 µM for adenosine1 Publication

    pH dependencei

    Optimum pH is 7-7.5.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei14 – 141PhosphateUniRule annotation
    Sitei162 – 1621Important for substrate specificityUniRule annotation
    Binding sitei180 – 1801Substrate; via amide nitrogenUniRule annotation
    Binding sitei181 – 1811PhosphateUniRule annotation
    Sitei217 – 2171Important 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

    BioCyciMTBRV:RV0535-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:Rv0535
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001584: Chromosome

    Organism-specific databases

    TubercuListiRv0535.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 264264S-methyl-5'-thioadenosine phosphorylasePRO_0000415096Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi83332.Rv0535.

    Structurei

    3D structure databases

    ProteinModelPortaliO06401.
    SMRiO06401. Positions 2-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni55 – 562Phosphate bindingUniRule annotation
    Regioni204 – 2063Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000228987.
    KOiK00772.
    OMAiCEAQLCY.
    OrthoDBiEOG6KHFXC.
    PhylomeDBiO06401.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    HAMAPiMF_01963. MTAP.
    InterProiIPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01694. MTAP. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O06401-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHNNGRMLGV IGGSGFYTFF GSDTRTVNSD TPYGQPSAPI TIGTIGVHDV    50
    AFLPRHGAHH QYSAHAVPYR ANMWALRALG VRRVFGPCAV GSLDPELEPG 100
    AVVVPDQLVD RTSGRADTYF DFGGVHAAFA DPYCPTLRAA VTGLPGVVDG 150
    GTMVVIQGPR FSTRAESQWF AAAGCNLVNM TGYPEAVLAR ELELCYAAIA 200
    LVTDVDAGVA AGDGVKAADV FAAFGENIEL LKRLVRAAID RVADERTCTH 250
    CQHHAGVPLP FELP 264
    Length:264
    Mass (Da):27,964
    Last modified:July 1, 1997 - v1
    Checksum:i3A850EA1B1873662
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP43273.1.
    PIRiB70546.
    RefSeqiNP_215049.1. NC_000962.3.
    YP_006513868.1. NC_018143.2.

    Genome annotation databases

    EnsemblBacteriaiCCP43273; CCP43273; Rv0535.
    GeneIDi13318409.
    887430.
    KEGGimtu:Rv0535.
    mtv:RVBD_0535.
    PATRICi18149684. VBIMycTub87468_0594.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP43273.1 .
    PIRi B70546.
    RefSeqi NP_215049.1. NC_000962.3.
    YP_006513868.1. NC_018143.2.

    3D structure databases

    ProteinModelPortali O06401.
    SMRi O06401. Positions 2-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 83332.Rv0535.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCP43273 ; CCP43273 ; Rv0535 .
    GeneIDi 13318409.
    887430.
    KEGGi mtu:Rv0535.
    mtv:RVBD_0535.
    PATRICi 18149684. VBIMycTub87468_0594.

    Organism-specific databases

    TubercuListi Rv0535.

    Phylogenomic databases

    HOGENOMi HOG000228987.
    KOi K00772.
    OMAi CEAQLCY.
    OrthoDBi EOG6KHFXC.
    PhylomeDBi O06401.

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00873 .
    BioCyci MTBRV:RV0535-MONOMER.

    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.
    [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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25618 / H37Rv.
    2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 25618 / H37Rv.
    3. "Identification of Rv0535 as methylthioadenosine phosphorylase from Mycobacterium tuberculosis."
      Buckoreelall K., Sun Y., Hobrath J.V., Wilson L., Parker W.B.
      Tuberculosis 92:139-147(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
      Strain: ATCC 25618 / H37Rv.

    Entry informationi

    Entry nameiMTAP_MYCTU
    AccessioniPrimary (citable) accession number: O06401
    Secondary accession number(s): L0T6S7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 81 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, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3