Q24SG7 · GMSS_DESHY
- ProteinGlutamate mutase sigma subunit
- GeneglmS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids136 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
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: ADVHA | ||||||
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: NLVVG |
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
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Desulfitobacteriaceae > Desulfitobacterium
Accessions
- Primary accessionQ24SG7
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000264142 | 1-136 | Glutamate mutase sigma subunit | |||
Sequence: MEGKTLVLGVIGADVHAVGNRILDYAFTQAGFKVINIGVLASQEEFIRAAIETAASVIMVSSLYGHGELDCRGLREKCQESGIGDILLYVGGNLVVGKQEFSEVEKRFLAMGFNRVYPPGTMPEAAIEDLRKDLEL |
Interaction
Subunit
Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-136 | B12-binding | ||||
Sequence: GKTLVLGVIGADVHAVGNRILDYAFTQAGFKVINIGVLASQEEFIRAAIETAASVIMVSSLYGHGELDCRGLREKCQESGIGDILLYVGGNLVVGKQEFSEVEKRFLAMGFNRVYPPGTMPEAAIEDLRKDLEL |
Sequence similarities
Belongs to the methylaspartate mutase GlmS subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length136
- Mass (Da)14,748
- Last updated2006-04-18 v1
- Checksum051735403943D06C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP008230 EMBL· GenBank· DDBJ | BAE85025.1 EMBL· GenBank· DDBJ | Genomic DNA |