A0A1D2SAW4 · A0A1D2SAW4_9BURK
- ProteinMultifunctional fusion protein
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids975 (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.
Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic activity
- UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate + D-alanyl-D-alanine + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + ADP + phosphate + H+
Cofactor
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 28 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 111-117 | ATP (UniProtKB | ChEBI) | |||
Binding site | 160-161 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 187 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 195 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 392 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 416-419 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 467 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 471 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 614-620 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity | |
Molecular Function | UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity | |
Molecular Function | UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine 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 nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- EC number
- Alternative names
- Recommended nameUDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Comamonas
Accessions
- Primary accessionA0A1D2SAW4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 227 | 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, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 24-68 | Mur ligase N-terminal catalytic | |||
Domain | 109-317 | Mur ligase central | |||
Domain | 340-469 | Mur ligase C-terminal | |||
Motif | 416-419 | Meso-diaminopimelate recognition motif | |||
Domain | 532-600 | Mur ligase N-terminal catalytic | |||
Domain | 612-815 | Mur ligase central | |||
Region | 750-772 | Disordered | |||
Domain | 846-959 | Mur ligase C-terminal | |||
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Belongs to the MurCDEF family. MurF subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length975
- Mass (Da)102,308
- Last updated2016-11-30 v1
- MD5 ChecksumDE14FC1D6EB0AF98259DB24D11056827
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MEDS01000005 EMBL· GenBank· DDBJ | ODS93273.1 EMBL· GenBank· DDBJ | Genomic DNA |