Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 3 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 annotation

Catalytic activityi

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

Kineticsi

  1. KM=1.6 µM for S-methyl-5'-thioadenosine1 Publication
  2. KM=310 µM for adenosine1 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), 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 sitei9 – 91PhosphateUniRule annotation
    Sitei157 – 1571Important for substrate specificityUniRule annotation
    Binding sitei175 – 1751Substrate; via amide nitrogenUniRule annotation
    Binding sitei176 – 1761PhosphateUniRule annotation
    Sitei212 – 2121Important 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

    BioCyciMSME246196:GJ4Y-990-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
    Synonyms:pnp
    Ordered Locus Names:MSMEG_0990, MSMEI_0963
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
    ProteomesiUP000006158 Componenti: Chromosome UP000000757 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 259259S-methyl-5'-thioadenosine phosphorylasePRO_0000415095Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer. Dimer of a homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi246196.MSMEG_0990.

    Structurei

    3D structure databases

    ProteinModelPortaliA0QR54.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 512Phosphate bindingUniRule annotation
    Regioni199 – 2013Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000228987.
    KOiK00772.
    OMAiIDYRANI.
    OrthoDBiEOG6KHFXC.

    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.

    A0QR54-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMLGVIGGSG FYTFFGSDAR AVSVETPYGP PSAPITVGTV GDHEVAFLPR
    60 70 80 90 100
    HGVKHEFSPH TVPYRANLWA LRSLGVRRVF APCAVGSLTP DLGPGSIVVP
    110 120 130 140 150
    DQLVDRTSGR DDTYFDSGGI HVAFADPYCP TLRAAATGLP GVVDGGTMVV
    160 170 180 190 200
    IQGPRFSTRA ESRWFASQGF TLVNMTGYPE AVLARELEMC YAAVALVTDL
    210 220 230 240 250
    DAGIEVGSGV RAVDVFAEFE RNMPPFKKLV FEALEAVEVE RTCTHCLTHS

    GVQLPFELP
    Length:259
    Mass (Da):27,723
    Last modified:January 9, 2007 - v1
    Checksum:i8D379609536F84FF
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000480 Genomic DNA. Translation: ABK70512.1.
    CP001663 Genomic DNA. Translation: AFP37443.1.
    RefSeqiWP_011727338.1. NC_018289.1.
    YP_006565738.1. NC_018289.1.
    YP_885392.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK70512; ABK70512; MSMEG_0990.
    AFP37443; AFP37443; MSMEI_0963.
    GeneIDi4532080.
    KEGGimsm:MSMEG_0990.
    PATRICi18074434. VBIMycSme59918_0978.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000480 Genomic DNA. Translation: ABK70512.1.
    CP001663 Genomic DNA. Translation: AFP37443.1.
    RefSeqiWP_011727338.1. NC_018289.1.
    YP_006565738.1. NC_018289.1.
    YP_885392.1. NC_008596.1.

    3D structure databases

    ProteinModelPortaliA0QR54.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi246196.MSMEG_0990.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABK70512; ABK70512; MSMEG_0990.
    AFP37443; AFP37443; MSMEI_0963.
    GeneIDi4532080.
    KEGGimsm:MSMEG_0990.
    PATRICi18074434. VBIMycSme59918_0978.

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000228987.
    KOiK00772.
    OMAiIDYRANI.
    OrthoDBiEOG6KHFXC.

    Enzyme and pathway databases

    UniPathwayiUPA00904; UER00873.
    BioCyciMSME246196:GJ4Y-990-MONOMER.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
      Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
      Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
      Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
      Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    4. "Identification and characterization of two adenosine phosphorylase activities in Mycobacterium smegmatis."
      Buckoreelall K., Wilson L., Parker W.B.
      J. Bacteriol. 193:5668-5674(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 700084 / mc(2)155.

    Entry informationi

    Entry nameiMTAP_MYCS2
    AccessioniPrimary (citable) accession number: A0QR54
    Secondary accession number(s): I7FF12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: January 9, 2007
    Last modified: June 24, 2015
    This is version 64 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. 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.