Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8K9E5

- METK_BUCAP

UniProt

Q8K9E5 - METK_BUCAP

Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.UniRule annotation

    Catalytic activityi

    ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.UniRule annotation

    Cofactori

    Binds 2 divalent ions per subunit. Magnesium or cobalt.UniRule annotation
    Binds 1 potassium ion per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi17 – 171MagnesiumUniRule annotation
    Metal bindingi43 – 431PotassiumUniRule annotation
    Metal bindingi264 – 2641PotassiumUniRule annotation
    Metal bindingi272 – 2721MagnesiumUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi260 – 2678ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. magnesium ion binding Source: UniProtKB-HAMAP
    3. methionine adenosyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. one-carbon metabolic process Source: UniProtKB-HAMAP
    2. S-adenosylmethionine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

    Enzyme and pathway databases

    BioCyciBAPH198804:GHMG-413-MONOMER.
    UniPathwayiUPA00315; UER00080.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine synthaseUniRule annotation (EC:2.5.1.6UniRule annotation)
    Short name:
    AdoMet synthaseUniRule annotation
    Alternative name(s):
    MATUniRule annotation
    Methionine adenosyltransferaseUniRule annotation
    Gene namesi
    Name:metKUniRule annotation
    Ordered Locus Names:BUsg_393
    OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
    Taxonomic identifieri198804 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000000416: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 379379S-adenosylmethionine synthasePRO_0000174503Add
    BLAST

    Proteomic databases

    PRIDEiQ8K9E5.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi198804.BUsg393.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K9E5.
    SMRiQ8K9E5. Positions 3-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AdoMet synthase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0192.
    KOiK00789.
    OMAiGYVNSEM.
    OrthoDBiEOG68WR6M.

    Family and domain databases

    HAMAPiMF_00086. S_AdoMet_synth1.
    InterProiIPR022631. ADOMET_SYNTHASE_CS.
    IPR022630. S-AdoMet_synt_C.
    IPR022629. S-AdoMet_synt_central.
    IPR022628. S-AdoMet_synt_N.
    IPR002133. S-AdoMet_synthetase.
    IPR022636. S-AdoMet_synthetase_sfam.
    [Graphical view]
    PANTHERiPTHR11964. PTHR11964. 1 hit.
    PfamiPF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000497. MAT. 1 hit.
    SUPFAMiSSF55973. SSF55973. 3 hits.
    TIGRFAMsiTIGR01034. metK. 1 hit.
    PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8K9E5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEYLFTSES VSEGHPDKIA DQISDALLDE IIKQDLKARV ACETYVKTGM    50
    VLIGGEITTT AWVDVEEITR NTINNIGYIN SETGFDANSC AVLSTIGKQS 100
    PDITQGVDRC NPLEQGAGDQ GIIFGYATNE TEVLMPAPIT YAHLLVKKQS 150
    ELRKKNILHW LRPDAKSQVT FKYKNGRIIG IDTVVFSTQH KESITQDVLK 200
    EAVMEEIIKP VLPNKWLTKN TKFFINPTGR FVIGGPMGDC GLTGRKIIVD 250
    TYGGMSRHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQLS 300
    YAIGIAEPTS IMIETFRTGK ISNKSLINLV RNIFDLRPYG LIEMLDLLRP 350
    IYLNTAVYGH FGREEFPWEK LDKVDELLQ 379
    Length:379
    Mass (Da):42,003
    Last modified:October 1, 2002 - v1
    Checksum:i8D5576799F7DAFE7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013218 Genomic DNA. Translation: AAM67945.1.
    RefSeqiNP_660734.1. NC_004061.1.

    Genome annotation databases

    EnsemblBacteriaiAAM67945; AAM67945; BUsg_393.
    GeneIDi1005765.
    KEGGibas:BUsg393.
    PATRICi21247606. VBIBucAph100086_0406.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013218 Genomic DNA. Translation: AAM67945.1 .
    RefSeqi NP_660734.1. NC_004061.1.

    3D structure databases

    ProteinModelPortali Q8K9E5.
    SMRi Q8K9E5. Positions 3-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198804.BUsg393.

    Proteomic databases

    PRIDEi Q8K9E5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM67945 ; AAM67945 ; BUsg_393 .
    GeneIDi 1005765.
    KEGGi bas:BUsg393.
    PATRICi 21247606. VBIBucAph100086_0406.

    Phylogenomic databases

    eggNOGi COG0192.
    KOi K00789.
    OMAi GYVNSEM.
    OrthoDBi EOG68WR6M.

    Enzyme and pathway databases

    UniPathwayi UPA00315 ; UER00080 .
    BioCyci BAPH198804:GHMG-413-MONOMER.

    Family and domain databases

    HAMAPi MF_00086. S_AdoMet_synth1.
    InterProi IPR022631. ADOMET_SYNTHASE_CS.
    IPR022630. S-AdoMet_synt_C.
    IPR022629. S-AdoMet_synt_central.
    IPR022628. S-AdoMet_synt_N.
    IPR002133. S-AdoMet_synthetase.
    IPR022636. S-AdoMet_synthetase_sfam.
    [Graphical view ]
    PANTHERi PTHR11964. PTHR11964. 1 hit.
    Pfami PF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000497. MAT. 1 hit.
    SUPFAMi SSF55973. SSF55973. 3 hits.
    TIGRFAMsi TIGR01034. metK. 1 hit.
    PROSITEi PS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sg.

    Entry informationi

    Entry nameiMETK_BUCAP
    AccessioniPrimary (citable) accession number: Q8K9E5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 84 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. Buchnera aphidicola (subsp. Schizaphis graminum)
      Buchnera aphidicola (subsp. Schizaphis graminum): 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