A0A0E3YVK4 · A0A0E3YVK4_9BACT
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids542 (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
- ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H+ + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
Cofactor
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 75 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 156-162 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTNGKTT | ||||||
Binding site | 197-198 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 224 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 230 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 232 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 428 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 452-455 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: DNPR | ||||||
Binding site | 503 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 507 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: E |
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 > Verrucomicrobiota
Accessions
- Primary accessionA0A0E3YVK4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 264 | N6-carboxylysine | ||||
Sequence: K |
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 | 68-141 | Mur ligase N-terminal catalytic | ||||
Sequence: ISGLVMDSRRVVPGNVFFALSGLRTDGAVFVAEALSRGAVAIVSAAAPAAAPAKVTYVQVADPRGALARAARRI | ||||||
Domain | 154-357 | Mur ligase central | ||||
Sequence: VTGTNGKTTVGHLIKHFLEDGPRVGLLGTISYDLGARIVPSFKTTPEAPDIFGMLAQMRDAGCREAVMEVSSHGIDQQRVDGLEFAAAVFTNLTQDHLDYHQTLEAYFSVKTRLFTGGSGRPPPVAVINIDDNYGRRLLAMLPASVRPVSFGESADASVRAEDVELGFKETVFNLVWPEGRVRVRCSLLGRYNVSNVLAAAATA | ||||||
Domain | 379-505 | Mur ligase C-terminal | ||||
Sequence: GRMERIEEGQSYNVLVDYAHTDDALRNALGMLRAITPGRVLCVFGCGGNRDRAKRPLMTRAVEDYADIALPTADNPRNESVVRIFEDMRAGVTQPSKFTWIEDRRRAISLALDMCRPGDCLLVAGKG | ||||||
Motif | 452-455 | Meso-diaminopimelate recognition motif | ||||
Sequence: DNPR |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length542
- Mass (Da)58,843
- Last updated2015-06-24 v1
- ChecksumF92DD8944635EEE2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP011265 EMBL· GenBank· DDBJ | AKC81942.1 EMBL· GenBank· DDBJ | Genomic DNA |