C0E4M8 · C0E4M8_9CORY
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids497 (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 | 33 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 35 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 117-123 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTSGKTT | ||||||
Binding site | 159-160 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 186 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 194 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 390 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 414-417 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: DNPR | ||||||
Binding site | 466 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 470 | 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 > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium
Accessions
- Primary accessionC0E4M8
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 226 | N6-carboxylysine | ||||
Sequence: K |
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 | 28-101 | Mur ligase N-terminal catalytic | ||||
Sequence: ITEVGLNSAELPAGALFAAVPGTRVHGARFAADTAAAAILTDEAGWGLLSAAGETRPVLVVDDVRSVLGVAAAA | ||||||
Domain | 115-320 | Mur ligase central | ||||
Sequence: ITGTSGKTTTSYMLEAGLLAAGYRVGLIGTTGTQINGRPVPTSLTTPEAPTLQALFVQMLAEGVTHVVMEVSSHALMLGRVLGVKFDVAGFTNLSQDHLDFHATMAEYFDAKALFFRPGSPTRAARAVVCVDDEWGEKMASVFGSGVRTLATRGQAGDYTVSAVQTVERGGQEFQLAAPSGSVVAATVPLPGRFNVANAALALALA | ||||||
Domain | 341-468 | Mur ligase C-terminal | ||||
Sequence: GRMEVVDCGQDFLAVVDYAHKPAAIKAVLATVRGQITGRIGLVVGAGGDRDHSKRPIMGAEAAAGADYVVVTDDNPRNEDPAAIRAQVLAGTAAGSAEVVEIGDRRAAIRQVVAWAKPGDAVIIAGKG | ||||||
Motif | 414-417 | Meso-diaminopimelate recognition motif | ||||
Sequence: DNPR |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length497
- Mass (Da)50,965
- Last updated2009-05-05 v1
- Checksum6FCB535DF39DFB2E