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Q05488

- GMSS_CLOTT

UniProt

Q05488 - GMSS_CLOTT

Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Clostridium tetanomorphum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).1 PublicationUniRule annotation

    Catalytic activityi

    L-threo-3-methylaspartate = L-glutamate.1 PublicationUniRule annotation

    Cofactori

    Adenosylcobalamin.1 PublicationUniRule annotation

    Kineticsi

    Kcat is 20.6 sec(-1) for mutase activity with L-glutamate.

    1. KM=18 µM for adenosylcobalamin1 Publication
    2. KM=1.09 mM for L-glutamate1 Publication

    Vmax=22.8 µmol/min/mg enzyme1 Publication

    Pathwayi

    Sites

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

    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

    SABIO-RKQ05488.
    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
    OrganismiClostridium tetanomorphum
    Taxonomic identifieri1553 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 137137Glutamate mutase sigma subunitPRO_0000216445Add
    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.1 PublicationUniRule annotation

    Structurei

    Secondary structure

    1
    137
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Beta strandi13 – 164
    Beta strandi20 – 223
    Beta strandi25 – 284
    Turni29 – 313
    Beta strandi33 – 408
    Helixi45 – 528
    Beta strandi56 – 6611
    Helixi67 – 715
    Helixi75 – 784
    Beta strandi87 – 926
    Beta strandi94 – 963
    Helixi104 – 1118
    Beta strandi114 – 1163
    Turni123 – 1286
    Helixi129 – 1324

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BE1NMR-A1-137[»]
    1FMFNMR-A1-137[»]
    1ID8NMR-A1-137[»]
    ProteinModelPortaliQ05488.
    SMRiQ05488. Positions 1-137.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05488.

    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

    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.

    Q05488-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKKTIVLGV IGSDCHAVGN KILDHSFTNA GFNVVNIGVL SSQEDFINAA    50
    IETKADLICV SSLYGQGEID CKGLREKCDE AGLKGIKLFV GGNIVVGKQN 100
    WPDVEQRFKA MGFDRVYPPG TSPETTIADM KEVLGVE 137
    Length:137
    Mass (Da):14,748
    Last modified:February 1, 1995 - v1
    Checksum:iE71FE55BA8CE3DB3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70499 Genomic DNA. Translation: CAA49908.1.
    X68570 Genomic DNA. Translation: CAA48567.1.
    PIRiS29502.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70499 Genomic DNA. Translation: CAA49908.1 .
    X68570 Genomic DNA. Translation: CAA48567.1 .
    PIRi S29502.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BE1 NMR - A 1-137 [» ]
    1FMF NMR - A 1-137 [» ]
    1ID8 NMR - A 1-137 [» ]
    ProteinModelPortali Q05488.
    SMRi Q05488. Positions 1-137.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00561 ; UER00617 .
    SABIO-RK Q05488.

    Miscellaneous databases

    EvolutionaryTracei Q05488.

    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. "Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes."
      Marsh E.N.G., Holloway D.E.
      FEBS Lett. 310:167-170(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-33.
      Strain: NCIMB 11547.
    2. "Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum."
      Brecht M., Kellermann J., Plueckthun A.
      FEBS Lett. 319:84-89(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-24.
      Strain: ATCC 15920 / DSM 528 / H1.
    3. "Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme."
      Holloway D.E., Marsh E.N.
      J. Biol. Chem. 269:20425-20430(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
    4. "How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum."
      Tollinger M., Konrat R., Hilbert B.H., Marsh E.N.G., Kraeutler B.
      Structure 6:1021-1033(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
      Strain: ATCC 15920 / DSM 528 / H1.
    5. "A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum."
      Hoffmann B., Tollinger M., Konrat R., Huhta M., Marsh E.N., Krautler B.
      ChemBioChem 2:643-655(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    6. "The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12)."
      Tollinger M., Eichmuller C., Konrat R., Huhta M.S., Marsh E.N., Krautler B.
      J. Mol. Biol. 309:777-791(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiGMSS_CLOTT
    AccessioniPrimary (citable) accession number: Q05488
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 81 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

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3