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Q05509

- GLME_CLOTT

UniProt

Q05509 - GLME_CLOTT

Protein

Glutamate mutase epsilon subunit

Gene

glmE

Organism
Clostridium tetanomorphum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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
    Binding sitei66 – 661L-glutamateUniRule annotation
    Binding sitei68 – 681Adenosylcobalamin; via carbonyl oxygenUniRule annotation
    Binding sitei100 – 1001L-glutamateUniRule annotation
    Binding sitei123 – 1231AdenosylcobalaminUniRule annotation
    Binding sitei171 – 1711L-glutamateUniRule annotation
    Binding sitei177 – 1771L-glutamateUniRule annotation
    Binding sitei180 – 1801Adenosylcobalamin; via carbonyl oxygenUniRule annotation
    Binding sitei181 – 1811L-glutamateUniRule annotation
    Binding sitei297 – 2971Adenosylcobalamin; via amide nitrogenUniRule annotation
    Binding sitei326 – 3261AdenosylcobalaminUniRule annotation
    Binding sitei330 – 3301Adenosylcobalamin; via carbonyl oxygenUniRule annotation
    Binding sitei334 – 3341Adenosylcobalamin; via amide nitrogenUniRule annotation

    GO - Molecular functioni

    1. cobalamin binding Source: UniProtKB-KW
    2. methylaspartate mutase activity Source: UniProtKB-EC

    GO - Biological processi

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

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Cobalamin, Cobalt

    Enzyme and pathway databases

    SABIO-RKQ05509.
    UniPathwayiUPA00561; UER00617.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate mutase epsilon subunitUniRule annotation (EC:5.4.99.1UniRule annotation)
    Alternative name(s):
    Glutamate mutase E chainUniRule annotation
    Glutamate mutase large subunitUniRule annotation
    Methylaspartate mutaseUniRule annotation
    Gene namesi
    Name:glmEUniRule annotation
    Synonyms:mutE
    OrganismiClostridium tetanomorphum
    Taxonomic identifieri1553 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Glutamate mutase epsilon subunitPRO_0000087512Add
    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 Probable.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ05509.
    SMRiQ05509. Positions 1-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni149 – 1502L-glutamate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the methylaspartate mutase GlmE subunit family.UniRule annotation

    Family and domain databases

    Gene3Di3.20.20.240. 1 hit.
    3.90.970.10. 1 hit.
    HAMAPiMF_01923. Me_Asp_mutase_E.
    InterProiIPR016176. Cbl-dep_enz_cat.
    IPR014348. Cbl-dep_enz_cat-sub.
    IPR006396. Glu_mut_E.
    IPR014714. Glu_mut_E_C_dom.
    [Graphical view]
    PfamiPF06368. Met_asp_mut_E. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001495. Met_asp_mut_epsi. 1 hit.
    SUPFAMiSSF51703. SSF51703. 1 hit.
    TIGRFAMsiTIGR01503. MthylAspMut_E. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q05509-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELKNKKWTD EEFFKQREEV LKQWPTGKEV DLQEAVDYLK KVPTEKNFAD    50
    KLVRAKEAGI TLAQPRAGVA LLDEHINLLR YLQDEGGADL LPSTIDAYTR 100
    QNRYEECEIG IKESEKAGRS LLNGFPGVNH GVKGCRKVLE SVNLPLQARH 150
    GTPDSRLLAE IIHAGGWTSN EGGGISYNIP YAKSVPIDKC LKDWQYCDRL 200
    VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV 250
    GYGECGNMLQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD 300
    ESKAFGVIVT ATTIASLAGA TKVIVKTPHE AIGIPTKEAN ASGIKATKMA 350
    LNMLEGQRMP MSKELETEMA IIKAETKCIL DKMFELGKGD LAVGTVKAFE 400
    TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE ELKNYNRERL 450
    AERAKFEGRE VSFQMVIDDI FAVGKGRLIG RPENK 485
    Length:485
    Mass (Da):53,741
    Last modified:February 1, 1995 - v1
    Checksum:i131792A392CACCC0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81W → L AA sequence (PubMed:1397267)Curated
    Sequence conflicti12 – 121E → G AA sequence (PubMed:1397267)Curated
    Sequence conflicti17 – 171R → A AA sequence (PubMed:1397267)Curated
    Sequence conflicti19 – 191E → G AA sequence (PubMed:1397267)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70499 Genomic DNA. Translation: CAA49910.1.
    X70695 Genomic DNA. Translation: CAA50026.1.
    S48141 Genomic DNA. Translation: AAB24069.1.
    PIRiS32433.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70499 Genomic DNA. Translation: CAA49910.1 .
    X70695 Genomic DNA. Translation: CAA50026.1 .
    S48141 Genomic DNA. Translation: AAB24069.1 .
    PIRi S32433.

    3D structure databases

    ProteinModelPortali Q05509.
    SMRi Q05509. Positions 1-483.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00561 ; UER00617 .
    SABIO-RK Q05509.

    Family and domain databases

    Gene3Di 3.20.20.240. 1 hit.
    3.90.970.10. 1 hit.
    HAMAPi MF_01923. Me_Asp_mutase_E.
    InterProi IPR016176. Cbl-dep_enz_cat.
    IPR014348. Cbl-dep_enz_cat-sub.
    IPR006396. Glu_mut_E.
    IPR014714. Glu_mut_E_C_dom.
    [Graphical view ]
    Pfami PF06368. Met_asp_mut_E. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001495. Met_asp_mut_epsi. 1 hit.
    SUPFAMi SSF51703. SSF51703. 1 hit.
    TIGRFAMsi TIGR01503. MthylAspMut_E. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes."
      Holloway D.E., Marsh E.N.G.
      FEBS Lett. 317:44-48(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 15920 / DSM 528 / H1.
    3. "Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
      Goda S.K., Minton N.P., Botting N.P., Gani D.
      Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-485.
      Strain: ATCC 15920 / DSM 528 / H1.
    4. "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: PROTEIN SEQUENCE OF 1-20.
      Strain: NCIMB 11547.
    5. "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.

    Entry informationi

    Entry nameiGLME_CLOTT
    AccessioniPrimary (citable) accession number: Q05509
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 71 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

    Direct protein sequencing

    Documents

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

    External Data

    Dasty 3