AC MF_00526; DC Protein; auto TR HAMAP; MF_00526; -; 1; level=0 XX Names: Me_Asp_mutase_S XX ID GMSS DE RecName: Full=Glutamate mutase sigma subunit; DE EC=5.4.99.1; DE AltName: Full=Glutamate mutase S chain; DE AltName: Full=Glutamate mutase small subunit; DE AltName: Full=Methylaspartate mutase; GN Name=glmS; XX 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 GlmS subunit family. XX DR Pfam; PF02310; B12-binding; 1; trigger=no DR PROSITE; PS51332; B12_BINDING; 1; trigger=yes DR NCBIfam; TIGR01501; MthylAspMutase; 1; trigger=no XX KW Cobalamin KW Cobalt KW Isomerase KW Metal-binding XX GO GO:0050097; F:methylaspartate mutase activity GO GO:0019670; P:anaerobic glutamate catabolic process XX FT From: GMSS_CLOCO (P80078) FT BINDING 13..17 FT /ligand="adenosylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:18408" FT Optional; Condition: [SA]-D-[CVA]-H-[ATV] FT BINDING 61..63 FT /ligand="adenosylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:18408" FT Optional; Condition: S-S-[LI] FT BINDING 93..97 FT /ligand="adenosylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:18408" FT Optional; Condition: N-[LI]-[VGA]-[VI]-[G] FT BINDING 16 FT /ligand="adenosylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:18408" FT /ligand_part="Co" FT /ligand_part_id="ChEBI:CHEBI:27638" FT /note="axial binding residue" FT Condition: H XX Size: 130-175; Related: None; Template: P80078; Q05488; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in HALMA Plasmid: None Comments: None XX # Revision 1.33 2023/06/01 //