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P80077

- GLME_CLOCO

UniProt

P80077 - GLME_CLOCO

Protein

Glutamate mutase epsilon subunit

Gene

glmE

Organism
Clostridium cochlearium
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      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).2 PublicationsUniRule annotation

    Catalytic activityi

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

    Cofactori

    Adenosylcobalamin.4 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
    Binding sitei66 – 661L-glutamate
    Binding sitei68 – 681Adenosylcobalamin; via carbonyl oxygen
    Binding sitei100 – 1001L-glutamate
    Binding sitei123 – 1231Adenosylcobalamin
    Binding sitei171 – 1711L-glutamate
    Binding sitei177 – 1771L-glutamate
    Binding sitei180 – 1801Adenosylcobalamin; via carbonyl oxygen
    Binding sitei181 – 1811L-glutamate
    Binding sitei297 – 2971Adenosylcobalamin; via amide nitrogen
    Binding sitei326 – 3261Adenosylcobalamin
    Binding sitei330 – 3301Adenosylcobalamin; via carbonyl oxygen
    Binding sitei334 – 3341Adenosylcobalamin; via amide nitrogen

    GO - Molecular functioni

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

    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

    BioCyciMetaCyc:MONOMER-1101.
    SABIO-RKP80077.
    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
    OrganismiClostridium cochlearium
    Taxonomic identifieri1494 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 483483Glutamate mutase epsilon subunitPRO_0000087511Add
    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.4 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    glmSP800782EBI-1028142,EBI-1028147

    Protein-protein interaction databases

    IntActiP80077. 1 interaction.

    Structurei

    Secondary structure

    1
    483
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2011
    Helixi21 – 233
    Helixi25 – 295
    Helixi32 – 409
    Helixi44 – 463
    Helixi48 – 5811
    Beta strandi62 – 643
    Helixi72 – 8413
    Beta strandi89 – 957
    Helixi99 – 1013
    Helixi104 – 11714
    Beta strandi122 – 1254
    Helixi127 – 14115
    Beta strandi146 – 1494
    Helixi156 – 1649
    Beta strandi169 – 1713
    Turni174 – 1818
    Helixi187 – 20620
    Beta strandi212 – 2143
    Turni217 – 2204
    Beta strandi221 – 2233
    Helixi226 – 24217
    Beta strandi247 – 2537
    Helixi258 – 27821
    Beta strandi285 – 2917
    Helixi301 – 31818
    Beta strandi321 – 3244
    Turni328 – 3325
    Helixi337 – 35317
    Turni354 – 3563
    Helixi363 – 38624
    Turni387 – 3893
    Helixi391 – 40010
    Beta strandi419 – 4224
    Beta strandi428 – 4325
    Helixi440 – 45718
    Helixi463 – 47210
    Turni473 – 4764
    Beta strandi477 – 4793

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CB7X-ray2.00B/D1-483[»]
    1CCWX-ray1.60B/D1-483[»]
    1I9CX-ray1.90B/D1-483[»]
    ProteinModelPortaliP80077.
    SMRiP80077. Positions 1-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80077.

    Family & Domainsi

    Region

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

    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.

    P80077-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELKNKKWTD EEFHKQREEV LQQWPTGKEV DLQEAVDYLK KIPAEKNFAE    50
    KLVLAKKKGI TMAQPRAGVA LLDEHIELLR YLQDEGGADF LPSTIDAYTR 100
    QNRYDECENG IKESEKAGRS LLNGFPGVNY GVKGCRKVLE AVNLPLQARH 150
    GTPDSRLLAE IIHAGGWTSN EGGGISYNVP YAKNVTIEKS LLDWQYCDRL 200
    VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV 250
    GYGECGNMIQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD 300
    ESKAFGVIVT ATTIAALAGA TKVIVKTPHE AIGIPTKEAN AAGIKATKMA 350
    LNMLEGQRMP MSKELETEMA VIKAETKCIL DKMFELGKGD LAIGTVKAFE 400
    TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE EIKNYNRERL 450
    QERAKFEGRD VSFQMVIDDI FAVGKGRLIG RPE 483
    Length:483
    Mass (Da):53,574
    Last modified:November 1, 1997 - v2
    Checksum:i0789965B945B3F5C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80997 Genomic DNA. Translation: CAA56923.1.
    PIRiI40662.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80997 Genomic DNA. Translation: CAA56923.1 .
    PIRi I40662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CB7 X-ray 2.00 B/D 1-483 [» ]
    1CCW X-ray 1.60 B/D 1-483 [» ]
    1I9C X-ray 1.90 B/D 1-483 [» ]
    ProteinModelPortali P80077.
    SMRi P80077. Positions 1-483.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P80077. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00561 ; UER00617 .
    BioCyci MetaCyc:MONOMER-1101.
    SABIO-RK P80077.

    Miscellaneous databases

    EvolutionaryTracei P80077.

    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. "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. "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 1-26, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, SUBUNIT.
      Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
    3. "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.
    4. "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 nameiGLME_CLOCO
    AccessioniPrimary (citable) accession number: P80077
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 85 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