E6MX53 · E6MX53_NEIMH
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids492 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Catalytic activity
- UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate + ADP + phosphate + H+
Cofactor
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 30 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 114-120 | ATP (UniProtKB | ChEBI) | |||
Binding site | 156-157 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 183 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 189 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 191 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 389 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 413-416 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 462 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 466 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity | |
Biological Process | cell division | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Neisseriales > Neisseriaceae > Neisseria
Accessions
- Primary accessionE6MX53
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 223 | N6-carboxylysine | |||
Post-translational modification
Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 28-98 | Mur ligase N-terminal catalytic | |||
Domain | 112-315 | Mur ligase central | |||
Domain | 338-464 | Mur ligase C-terminal | |||
Motif | 413-416 | Meso-diaminopimelate recognition motif | |||
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length492
- Mass (Da)53,045
- Last updated2011-03-08 v1
- ChecksumB772F358CA32919E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AEQZ01000020 EMBL· GenBank· DDBJ | EFV63877.1 EMBL· GenBank· DDBJ | Genomic DNA |