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P80078

- GMSS_CLOCO

UniProt

P80078 - GMSS_CLOCO

Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Clostridium cochlearium
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).3 PublicationsUniRule annotation

    Catalytic activityi

    L-threo-3-methylaspartate = L-glutamate.2 PublicationsUniRule annotation

    Cofactori

    Adenosylcobalamin.5 PublicationsUniRule annotation

    Enzyme regulationi

    Competitively inhibited by (2S,4S)-4-fluoroglutamate, 2-methyleneglutarate, (2R,3RS)-3-fluoroglutamate and (S)-3-methylitaconate.2 Publications

    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
    4. protein binding Source: IntAct

    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-RKP80078.
    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
    OrganismiClostridium cochlearium
    Taxonomic identifieri1494 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 137137Glutamate mutase sigma subunitPRO_0000216443Add
    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.5 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    glmEP800772EBI-1028147,EBI-1028142

    Protein-protein interaction databases

    IntActiP80078. 1 interaction.

    Structurei

    Secondary structure

    1
    137
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Helixi18 – 2912
    Beta strandi33 – 419
    Helixi43 – 5311
    Beta strandi56 – 627
    Helixi67 – 715
    Helixi74 – 807
    Beta strandi87 – 937
    Beta strandi95 – 984
    Helixi101 – 11010
    Beta strandi114 – 1163
    Helixi123 – 13412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B1ANMR-A1-137[»]
    1CB7X-ray2.00A/C1-137[»]
    1CCWX-ray1.60A/C1-137[»]
    1I9CX-ray1.90A/C1-137[»]
    ProteinModelPortaliP80078.
    SMRiP80078. Positions 1-137.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80078.

    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 binding
    Regioni61 – 633Adenosylcobalamin binding
    Regioni93 – 975Adenosylcobalamin binding

    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.

    P80078-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKKTIVLGV IGSDCHAVGN KILDHAFTNA GFNVVNIGVL SPQEVFIKAA    50
    IETKADAILL SSLYGQGEID CKGLRQKCDE AGLEGILLYV GGNIVVGKQH 100
    WPDVEKRFKD MGYDRVYAPG TPPEVGIADL KKDLNIE 137
    Length:137
    Mass (Da):14,812
    Last modified:December 13, 2001 - v2
    Checksum:iD9C5BF8DE5D1E878
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80997 Genomic DNA. Translation: CAA56921.1.
    X75890 Genomic DNA. Translation: CAA53484.1.
    PIRiI40658.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80997 Genomic DNA. Translation: CAA56921.1 .
    X75890 Genomic DNA. Translation: CAA53484.1 .
    PIRi I40658.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B1A NMR - A 1-137 [» ]
    1CB7 X-ray 2.00 A/C 1-137 [» ]
    1CCW X-ray 1.60 A/C 1-137 [» ]
    1I9C X-ray 1.90 A/C 1-137 [» ]
    ProteinModelPortali P80078.
    SMRi P80078. Positions 1-137.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P80078. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00561 ; UER00617 .
    SABIO-RK P80078.

    Miscellaneous databases

    EvolutionaryTracei P80078.

    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. "Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli."
      Zelder O., Beatrix B., Leutbecher U., Buckel W.
      Eur. J. Biochem. 226:577-585(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, SUBUNIT.
      Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
    2. "Cloning, sequencing and expression in Escherichia coli of the gene encoding component S of the coenzyme B12-dependent glutamate mutase from Clostridium cochlearium."
      Zelder O., Beatrix B., Buckel W.
      FEMS Microbiol. Lett. 118:15-21(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
      Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
    3. "Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors."
      Leutbecher U., Boecher R., Linder D., Buckel W.
      Eur. J. Biochem. 205:759-765(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-23, FUNCTION, ENZYME REGULATION, COFACTOR, SUBUNIT.
      Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
    4. "Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium."
      Hoffmann B., Konrat R., Bothe H., Buckel W., Krautler B.
      Eur. J. Biochem. 263:178-188(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    5. "Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights."
      Reitzer R., Gruber K., Jogl G., Wagner U.G., Bothe H., Buckel W., Kratky C.
      Structure 7:891-902(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS, COFACTOR, SUBUNIT.
      Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
    6. "Radical shuttling in a protein: ribose pseudorotation controls alkyl-radical transfer in the coenzyme B(12) dependent enzyme glutamate mutase."
      Gruber K., Reitzer R., Kratky C.
      Angew. Chem. Int. Ed. Engl. 40:3377-3380(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS AND SUBSTRATE, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiGMSS_CLOCO
    AccessioniPrimary (citable) accession number: P80078
    Secondary accession number(s): Q60144
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: December 13, 2001
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 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