AC   MF_01923;
DC   Protein; auto
TR   HAMAP; MF_01923; -; 1; level=0
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Names: Me_Asp_mutase_E
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ID   GLME
DE   RecName: Full=Glutamate mutase epsilon subunit;
DE            EC=5.4.99.1;
DE   AltName: Full=Glutamate mutase E chain;
DE   AltName: Full=Glutamate mutase large subunit;
DE   AltName: Full=Methylaspartate mutase;
GN   Name=glmE;
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CC   -!- FUNCTION: Catalyzes the carbon skeleton rearrangement of L-glutamate to
CC       L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3S)-3-methyl-L-aspartate = L-glutamate;
CC         Xref=Rhea:RHEA:12857, ChEBI:CHEBI:29985, ChEBI:CHEBI:58724;
CC         EC=5.4.99.1;
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC   -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via mesaconate
CC       pathway; acetate and pyruvate from L-glutamate: step 1/4.
CC   -!- SUBUNIT: Heterotetramer composed of 2 epsilon subunits (GlmE) and 2
CC       sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a
CC       monomer.
CC   -!- SIMILARITY: Belongs to the methylaspartate mutase GlmE subunit family.
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DR   Pfam; PF06368; Met_asp_mut_E; 1; trigger=no
DR   NCBIfam; TIGR01503; MthylAspMut_E; 1; trigger=no
DR   PIRSF; PIRSF001495; Met_asp_mut_epsi; 1; trigger=no
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KW   Cobalamin
KW   Cobalt
KW   Isomerase
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GO   GO:0050097; F:methylaspartate mutase activity
GO   GO:0019670; P:anaerobic glutamate catabolic process
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FT   From: GLME_CLOCO (P80077)
FT   BINDING         149..150
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   Optional; Condition: [RK]-H
FT   BINDING         66
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   Optional; Condition: R
FT   BINDING         68
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Optional; Condition: G
FT   BINDING         100
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   Optional; Condition: R
FT   BINDING         123
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Optional; Condition: N
FT   BINDING         171
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   Optional; Condition: [ED]
FT   BINDING         177
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   Optional; Condition: Y
FT   BINDING         180
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Optional; Condition: P
FT   BINDING         181
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   Optional; Condition: Y
FT   BINDING         297
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Optional; Condition: F
FT   BINDING         326
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Optional; Condition: K
FT   BINDING         330
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Optional; Condition: E
FT   BINDING         334
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT   Optional; Condition: I
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Size: 440-520;
Related: None;
Template: P80077; Q05509;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.9 2023/06/01
//