A0A935MWE9 · A0A935MWE9_UNCIG
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids489 (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 | 31 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 117-123 | ATP (UniProtKB | ChEBI) | |||
Binding site | 159-160 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 186 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 194 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 387 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 411-414 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 461 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 465 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | tetrahydrofolylpolyglutamate synthase activity | |
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 > Ignavibacteriota > Ignavibacteria > Ignavibacteriales
Accessions
- Primary accessionA0A935MWE9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 226 | 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 | 27-103 | Mur ligase N-terminal catalytic | |||
Domain | 115-315 | Mur ligase central | |||
Domain | 337-463 | Mur ligase C-terminal | |||
Motif | 411-414 | Meso-diaminopimelate recognition motif | |||
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length489
- Mass (Da)53,831
- Last updated2023-02-22 v1
- MD5 ChecksumED7F89ED3A8BD52730EB9B0CC3C14F92
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JADJIH010000003 EMBL· GenBank· DDBJ | MBK7498627.1 EMBL· GenBank· DDBJ | Genomic DNA |