P80078 · GMSS_CLOCO
- ProteinGlutamate mutase sigma subunit
- GeneglmS
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids137 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
Catalytic activity
- (2S,3S)-3-methyl-L-aspartate = L-glutamate
Cofactor
Activity regulation
Competitively inhibited by (2S,4S)-4-fluoroglutamate, 2-methyleneglutarate, (2R,3RS)-3-fluoroglutamate and (S)-3-methylitaconate.
Pathway
Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 1/4.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 13-17 | adenosylcob(III)alamin (UniProtKB | ChEBI) | ||||
Sequence: SDCHA | ||||||
Binding site | 16 | Co (UniProtKB | ChEBI) of adenosylcob(III)alamin (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 61-63 | adenosylcob(III)alamin (UniProtKB | ChEBI) | ||||
Sequence: SSL | ||||||
Binding site | 93-97 | adenosylcob(III)alamin (UniProtKB | ChEBI) | ||||
Sequence: NIVVG |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | cobalamin binding | |
Molecular Function | metal ion binding | |
Molecular Function | methylaspartate mutase activity | |
Biological Process | anaerobic glutamate catabolic process | |
Biological Process | glutamate catabolic process via L-citramalate |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamate mutase sigma subunit
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionP80078
- Secondary accessions
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000216443 | 1-137 | Glutamate mutase sigma subunit | |||
Sequence: MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQEVFIKAAIETKADAILLSSLYGQGEIDCKGLRQKCDEAGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE |
Interaction
Subunit
Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P80078 | glmE P80077 | 2 | EBI-1028147, EBI-1028142 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-137 | B12-binding | ||||
Sequence: KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQEVFIKAAIETKADAILLSSLYGQGEIDCKGLRQKCDEAGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE |
Sequence similarities
Belongs to the methylaspartate mutase GlmS subunit family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length137
- Mass (Da)14,812
- Last updated2001-12-13 v2
- ChecksumD9C5BF8DE5D1E878
Keywords
- Technical term