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P56878

- METK_RICPR

UniProt

P56878 - METK_RICPR

Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Rickettsia prowazekii (strain Madrid E)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (30 May 2000)
      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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.By similarity
    Binds 1 potassium ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi17 – 171MagnesiumBy similarity
    Metal bindingi43 – 431PotassiumBy similarity
    Metal bindingi264 – 2641PotassiumBy similarity
    Metal bindingi272 – 2721MagnesiumBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi260 – 2678ATPSequence Analysis

    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

    UniPathwayiUPA00315; UER00080.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine synthase (EC:2.5.1.6)
    Short name:
    AdoMet synthase
    Alternative name(s):
    MAT
    Methionine adenosyltransferase
    Gene namesi
    Name:metK
    Ordered Locus Names:RP777
    OrganismiRickettsia prowazekii (strain Madrid E)
    Taxonomic identifieri272947 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
    ProteomesiUP000002480: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 380380S-adenosylmethionine synthasePRO_0000174578Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP56878.
    SMRiP56878. Positions 5-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AdoMet synthase family.Curated

    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.

    P56878-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNFVFTSES VSEGHPDKIA DQISDAVLDE ILKHDPNGRV ACETFVTTGL    50
    VLVGGEITTN TYVDIEQVVR NKIQEIGYNN PNYGFDGSCC AVISSIIKQS 100
    PDIAMGIDNE NEEEIGAGDQ GMVFGYACNE TKSLMPAPIY YAHLLMKRQA 150
    YLRKQNILSW LRPDAKSQVT LRYENNKPIV IDSVVLSTQH HPEIQQKDLI 200
    EAVIEEIIKP TLPTNLLHKD TKYLINPTGR FVIGGPVADC GLTGRKIIVD 250
    SYGGMAKHGG GCFSGKDPTK IDRSAAYMAR YIAKNIVGAG LADRCEIQIS 300
    YAIGVADPVS VYAETFGTSK LSNEQTTKLI TEHFDMRPGK IIKNLKLHTQ 350
    CYQKTATYGH FGREDENFTW EQLDKVDIFK 380
    Length:380
    Mass (Da):42,149
    Last modified:May 30, 2000 - v1
    Checksum:iD1B29BB64481FBCA
    GO

    Sequence cautioni

    The sequence AJ235273 differs from that shown. Reason: Erroneous termination at position 141. Translated as Tyr.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ235273 Genomic DNA. No translation available.
    AJ238756 Genomic DNA. Translation: CAB56090.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ235273 Genomic DNA. No translation available.
    AJ238756 Genomic DNA. Translation: CAB56090.1 .

    3D structure databases

    ProteinModelPortali P56878.
    SMRi P56878. Positions 5-380.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00315 ; UER00080 .

    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: Madrid E.
    2. "Genome degradation is an ongoing process in Rickettsia."
      Andersson J.O., Andersson S.G.E.
      Mol. Biol. Evol. 16:1178-1191(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: B.

    Entry informationi

    Entry nameiMETK_RICPR
    AccessioniPrimary (citable) accession number: P56878
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    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

    Caution

    Non-functional in strain Madrid E.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Rickettsia prowazekii
      Rickettsia prowazekii (strain Madrid E): entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3