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P0DJF9

- MTAP_SYNYG

UniProt

P0DJF9 - MTAP_SYNYG

Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Synechocystis sp. (strain PCC 6803 / GT-S)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 17 (01 Oct 2014)
      Sequence version 1 (21 Mar 2012)
      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 sitei44 – 441PhosphateUniRule annotation
    Sitei202 – 2021Important for substrate specificityUniRule annotation
    Binding sitei220 – 2201Substrate; via amide nitrogenUniRule annotation
    Binding sitei221 – 2211PhosphateUniRule annotation
    Sitei257 – 2571Important 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

    BioCyciSSP1148:GJOT-2026-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:SYNGTS_1998
    OrganismiSynechocystis sp. (strain PCC 6803 / GT-S)
    Taxonomic identifieri1111707 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    ProteomesiUP000008187: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 326326S-methyl-5'-thioadenosine phosphorylasePRO_0000416437Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer. Dimer of a homotrimer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP0DJF9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni86 – 872Phosphate bindingUniRule annotation
    Regioni119 – 1202Phosphate bindingUniRule annotation
    Regioni244 – 2463Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK00772.

    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.

    P0DJF9-1 [UniParc]FASTAAdd to Basket

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    MGMIISMAMT AVTIWTKTKP GRVSCFIRKN STMVNAPIGI IGGSGLYQME    50
    ALKNVEEVTL DTPFGAPSDS FIVGELAGVR VAFLARHGRG HHLLPSEIPF 100
    RANIHGMKQL GVKYLISASA VGSLQAEAKP LDMVVPDQFI DRTRQRISTF 150
    FGEGIVAHIG FGNPICPQLA QCLSTAIAGL ELEGVTLHDR GTYVSMEGPA 200
    FSTIAESNLY RSWGGTVIGM TNLPEAKLAR EAEIAYATLA LVTDYDCWHP 250
    DHDHVTVEMV IGNLQKNAVN AQQVILETVK QLAANPFESI AHRALQYAVL 300
    TPPDKFPAAT YEKLSLLLGK YYPPAP 326
    Length:326
    Mass (Da):35,319
    Last modified:March 21, 2012 - v1
    Checksum:i06F7D98E67A7BCD8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012205 Genomic DNA. Translation: BAK50746.1.
    RefSeqiNP_441892.1. NC_000911.1.
    YP_005651951.1. NC_017277.1.
    YP_007451772.1. NC_020286.1.

    Genome annotation databases

    EnsemblBacteriaiBAK50746; BAK50746; SYNGTS_1998.
    GeneIDi952850.
    KEGGisyn:sll0135.
    syy:SYNGTS_1998.
    syz:MYO_120170.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012205 Genomic DNA. Translation: BAK50746.1 .
    RefSeqi NP_441892.1. NC_000911.1.
    YP_005651951.1. NC_017277.1.
    YP_007451772.1. NC_020286.1.

    3D structure databases

    ProteinModelPortali P0DJF9.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAK50746 ; BAK50746 ; SYNGTS_1998 .
    GeneIDi 952850.
    KEGGi syn:sll0135.
    syy:SYNGTS_1998.
    syz:MYO_120170.

    Phylogenomic databases

    KOi K00772.

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00873 .
    BioCyci SSP1148:GJOT-2026-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. "Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 strain GT-S."
      Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K., Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.
      DNA Res. 18:393-399(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 6803 / GT-S.

    Entry informationi

    Entry nameiMTAP_SYNYG
    AccessioniPrimary (citable) accession number: P0DJF9
    Secondary accession number(s): P74469
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2012
    Last sequence update: March 21, 2012
    Last modified: October 1, 2014
    This is version 17 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3