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P58620

- GMSS_ECO57

UniProt

P58620 - GMSS_ECO57

Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
  1. Functioni

    Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).UniRule annotation

    Catalytic activityi

    L-threo-3-methylaspartate = L-glutamate.UniRule annotation

    Cofactori

    Adenosylcobalamin.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi16 – 161Cobalt (cobalamin axial ligand)UniRule annotation

    GO - Molecular functioni

    1. cobalamin binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. methylaspartate mutase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. anaerobic glutamate catabolic process Source: UniProtKB-HAMAP
    2. glutamate catabolic process via L-citramalate Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Cobalamin, Cobalt, Metal-binding

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-759-MONOMER.
    UniPathwayiUPA00561; UER00617.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate mutase sigma subunitUniRule annotation (EC:5.4.99.1UniRule annotation)
    Alternative name(s):
    Glutamate mutase S chainUniRule annotation
    Glutamate mutase small subunitUniRule annotation
    Methylaspartate mutaseUniRule annotation
    Gene namesi
    Name:glmSUniRule annotation
    Ordered Locus Names:Z0895, ECs0764
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 149149Glutamate mutase sigma subunitPRO_0000216446Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi155864.Z0895.

    Structurei

    3D structure databases

    ProteinModelPortaliP58620.
    SMRiP58620. Positions 1-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 140138B12-bindingUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni13 – 175Adenosylcobalamin bindingUniRule annotation
    Regioni61 – 633Adenosylcobalamin bindingUniRule annotation
    Regioni93 – 975Adenosylcobalamin bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the methylaspartate mutase GlmS subunit family.UniRule annotation
    Contains 1 B12-binding domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG2185.
    HOGENOMiHOG000011065.
    KOiK01846.
    OMAiMGFNRVF.
    OrthoDBiEOG6CP428.

    Family and domain databases

    Gene3Di3.40.50.280. 1 hit.
    HAMAPiMF_00526. Me_Asp_mutase_S.
    InterProiIPR006158. Cobalamin-bd.
    IPR006394. Me_Asp_mutase.
    [Graphical view]
    PfamiPF02310. B12-binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF52242. SSF52242. 1 hit.
    TIGRFAMsiTIGR01501. MthylAspMutase. 1 hit.
    PROSITEiPS51332. B12_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P58620-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKATLVIGV IGADCHAVGN KVLDRVFSNH DFRVINLGVM VSQDEYIDAA    50
    IETGADAIVV SSIYGHGDID CLGMRERCIE RGLGDILLYV GGNLVVGKHD 100
    FADVETKFKE MGFDRVFAPS HDLEDVCQLM AHDINQRHDV DTRILEEAI 149
    Length:149
    Mass (Da):16,430
    Last modified:January 23, 2002 - v1
    Checksum:iB785DAE49F27D9D0
    GO

    Sequence cautioni

    The sequence AAG55064.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG55064.1. Different initiation.
    BA000007 Genomic DNA. Translation: BAB34187.1.
    PIRiD85575.
    D90724.
    RefSeqiNP_286456.1. NC_002655.2.
    NP_308791.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG55064; AAG55064; Z0895.
    BAB34187; BAB34187; BAB34187.
    GeneIDi917503.
    957856.
    KEGGiece:Z0895.
    ecs:ECs0764.
    PATRICi18350552. VBIEscCol44059_0787.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG55064.1 . Different initiation.
    BA000007 Genomic DNA. Translation: BAB34187.1 .
    PIRi D85575.
    D90724.
    RefSeqi NP_286456.1. NC_002655.2.
    NP_308791.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P58620.
    SMRi P58620. Positions 1-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z0895.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG55064 ; AAG55064 ; Z0895 .
    BAB34187 ; BAB34187 ; BAB34187 .
    GeneIDi 917503.
    957856.
    KEGGi ece:Z0895.
    ecs:ECs0764.
    PATRICi 18350552. VBIEscCol44059_0787.

    Phylogenomic databases

    eggNOGi COG2185.
    HOGENOMi HOG000011065.
    KOi K01846.
    OMAi MGFNRVF.
    OrthoDBi EOG6CP428.

    Enzyme and pathway databases

    UniPathwayi UPA00561 ; UER00617 .
    BioCyci ECOL386585:GJFA-759-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.280. 1 hit.
    HAMAPi MF_00526. Me_Asp_mutase_S.
    InterProi IPR006158. Cobalamin-bd.
    IPR006394. Me_Asp_mutase.
    [Graphical view ]
    Pfami PF02310. B12-binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52242. SSF52242. 1 hit.
    TIGRFAMsi TIGR01501. MthylAspMutase. 1 hit.
    PROSITEi PS51332. B12_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiGMSS_ECO57
    AccessioniPrimary (citable) accession number: P58620
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 77 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