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Q17YQ7

- METK_HELAH

UniProt

Q17YQ7 - METK_HELAH

Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Helicobacter acinonychis (strain Sheeba)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (25 Jul 2006)
      Previous versions | rss
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    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 bindingi18 – 181MagnesiumUniRule annotation
    Metal bindingi44 – 441PotassiumUniRule 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

    BioCyciHACI382638:GJAU-361-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:Hac_0382
    OrganismiHelicobacter acinonychis (strain Sheeba)
    Taxonomic identifieri382638 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
    ProteomesiUP000000775: 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 – 385385S-adenosylmethionine synthasePRO_0000302922Add
    BLAST

    Proteomic databases

    PRIDEiQ17YQ7.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi382638.Hac_0382.

    Structurei

    3D structure databases

    ProteinModelPortaliQ17YQ7.
    SMRiQ17YQ7. Positions 6-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AdoMet synthase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0192.
    HOGENOMiHOG000245710.
    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.

    Q17YQ7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKDSFLFTSE SVTEGHPDKM ADQISDAVLD YIIERDKKAK VACETLVSNG    50
    FCVITGELKT SIYAPMQEIA REVVKKIGYT DALYGFDYRS AAVLNGIGEQ 100
    SPDINQGVDR EDGEIGAGDQ GLVFGYACKE TQMLMPLPIH LAHQLTFALA 150
    QKRKDNTLPF LRPDGKSQVS VRYENNKPIS IDTIVISTQH SPEVSQKHLK 200
    EAVIEEIVYK VLPKEYLHDN IKFFVNPTGK FVIGGPQGDA GLTGRKIIVD 250
    TYGGSCPHGG GAFSGKDPSK VDRSAAYAAR YVAKNLVASG VCDRATVQLA 300
    YAIGVVEPVS IYVNTHNTSK YSSAELEKCV KLVFKLTPKG IIESLDLLRP 350
    IYSLTSSYGH FGRELEAFTW EKTNKAEEIK AFFKH 385
    Length:385
    Mass (Da):42,358
    Last modified:July 25, 2006 - v1
    Checksum:iFA68A27F9790647A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM260522 Genomic DNA. Translation: CAJ99219.1.
    RefSeqiYP_664218.1. NC_008229.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ99219; CAJ99219; Hac_0382.
    GeneIDi4176762.
    KEGGihac:Hac_0382.
    PATRICi20584697. VBIHelAci71660_0374.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM260522 Genomic DNA. Translation: CAJ99219.1 .
    RefSeqi YP_664218.1. NC_008229.1.

    3D structure databases

    ProteinModelPortali Q17YQ7.
    SMRi Q17YQ7. Positions 6-380.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 382638.Hac_0382.

    Proteomic databases

    PRIDEi Q17YQ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ99219 ; CAJ99219 ; Hac_0382 .
    GeneIDi 4176762.
    KEGGi hac:Hac_0382.
    PATRICi 20584697. VBIHelAci71660_0374.

    Phylogenomic databases

    eggNOGi COG0192.
    HOGENOMi HOG000245710.
    KOi K00789.
    OMAi GYVNSEM.
    OrthoDBi EOG68WR6M.

    Enzyme and pathway databases

    UniPathwayi UPA00315 ; UER00080 .
    BioCyci HACI382638:GJAU-361-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. "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
      Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
      PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sheeba.

    Entry informationi

    Entry nameiMETK_HELAH
    AccessioniPrimary (citable) accession number: Q17YQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: July 25, 2006
    Last modified: October 1, 2014
    This is version 61 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