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Q890S0

- GMSS_CLOTE

UniProt

Q890S0 - GMSS_CLOTE

Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Clostridium tetani (strain Massachusetts / E88)
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

    BioCyciCTET212717:GJAM-2372-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
    Synonyms:mutS
    Ordered Locus Names:CTC_02568
    OrganismiClostridium tetani (strain Massachusetts / E88)
    Taxonomic identifieri212717 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000001412: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 137137Glutamate mutase sigma subunitPRO_0000216444Add
    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

    STRINGi212717.CTC02568.

    Structurei

    3D structure databases

    ProteinModelPortaliQ890S0.
    SMRiQ890S0. Positions 1-137.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 137135B12-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.
    KOiK01846.
    OMAiTSQEEFA.
    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.

    Q890S0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKKTIVLGV IGSDCHAVGN KILDHSFTAA GFNVVNIGVL SPQEDFINAA    50
    IETKADAILV SSLYGQGEID CKGLRQKCDE AGLEGILLYV GGNIVVGKQH 100
    WPDVEKRFKD MGYDRVYAPG TPPEVGIADL KEDLNIK 137
    Length:137
    Mass (Da):14,773
    Last modified:May 30, 2003 - v1
    Checksum:i9BDE133E7A8D0035
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015927 Genomic DNA. Translation: AAO37025.1.
    RefSeqiNP_783088.1. NC_004557.1.

    Genome annotation databases

    EnsemblBacteriaiAAO37025; AAO37025; CTC_02568.
    GeneIDi1060139.
    KEGGictc:CTC02568.
    PATRICi19513251. VBICloTet101274_2656.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015927 Genomic DNA. Translation: AAO37025.1 .
    RefSeqi NP_783088.1. NC_004557.1.

    3D structure databases

    ProteinModelPortali Q890S0.
    SMRi Q890S0. Positions 1-137.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 212717.CTC02568.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO37025 ; AAO37025 ; CTC_02568 .
    GeneIDi 1060139.
    KEGGi ctc:CTC02568.
    PATRICi 19513251. VBICloTet101274_2656.

    Phylogenomic databases

    eggNOGi COG2185.
    KOi K01846.
    OMAi TSQEEFA.
    OrthoDBi EOG6CP428.

    Enzyme and pathway databases

    UniPathwayi UPA00561 ; UER00617 .
    BioCyci CTET212717:GJAM-2372-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: Massachusetts / E88.

    Entry informationi

    Entry nameiGMSS_CLOTE
    AccessioniPrimary (citable) accession number: Q890S0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2003
    Last sequence update: May 30, 2003
    Last modified: October 1, 2014
    This is version 76 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, Reference proteome

    Documents

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

    External Data

    Dasty 3