A0A0Q9P4C4 · A0A0Q9P4C4_9GAMM
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids520 (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 | 34 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 36 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 137-143 | ATP (UniProtKB | ChEBI) | |||
Binding site | 179-180 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 206 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 212 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 214 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 410 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 434-437 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 485 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 489 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Rhodanobacteraceae > Rhodanobacter
Accessions
- Primary accessionA0A0Q9P4C4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 246 | N6-carboxylysine | |||
Post-translational modification
Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 29-123 | Mur ligase N-terminal catalytic | |||
Domain | 135-337 | Mur ligase central | |||
Domain | 360-487 | Mur ligase C-terminal | |||
Motif | 434-437 | Meso-diaminopimelate recognition motif | |||
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length520
- Mass (Da)54,534
- Last updated2016-01-20 v1
- Checksum7254C471822E6A43
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LMSK01000002 EMBL· GenBank· DDBJ | KRE85498.1 EMBL· GenBank· DDBJ | Genomic DNA |