C1A0Y0 · C1A0Y0_RHOE4
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids544 (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 | 57 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 148-154 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTSGKTT | ||||||
Binding site | 190-191 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 217 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 225 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 425 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 449-452 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: DNPR | ||||||
Binding site | 505 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 509 | 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 > Nocardiaceae > Rhodococcus > Rhodococcus erythropolis group
Accessions
- Primary accessionC1A0Y0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 257 | 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 region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MPNRLQSSNSDGAPGTRPTQ | ||||||
Domain | 52-132 | Mur ligase N-terminal catalytic | ||||
Sequence: VKGVDLRAQGIVADDLFAALPGARTHGAQFAVDALGRGATAILTDEAGLELIEAAGKAPDRSVPVLVHPNPRDVLGEISAE | ||||||
Domain | 146-354 | Mur ligase central | ||||
Sequence: ITGTSGKTTTSYLLEAAIAGAGRKPGLVGTIETRIDGRRVPSALTTPEAPQLHALFAVMAEQGIDTVVMEVSSHALALGRVDGIRFDIGAFTNLSQDHLDFHRDFEEYFQAKARLFDPESTVRAEHAVVCVDDVWGRRMAELAATDESDAVTTVSTSTAEAEWKVGAVEVAEDGSQTFELVGPDGQSWPVSLRLPGRYNVANAALALTV | ||||||
Domain | 376-507 | Mur ligase C-terminal | ||||
Sequence: GRVQRIDRGQSFLAVVDYAHKPAALEAVIATLRNQVPGRVAVVVGAGGDRDAGKRTLMGEAGARGADLLIVTDDNPRTEDPAKIRASVMQGAIDVPESERGEIREVGDRALAIEQAVRWAQPGDVVLVAGKG | ||||||
Motif | 449-452 | Meso-diaminopimelate recognition motif | ||||
Sequence: DNPR |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length544
- Mass (Da)57,195
- Last updated2009-05-26 v1
- Checksum02C57687F164A449
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP008957 EMBL· GenBank· DDBJ | BAH34265.1 EMBL· GenBank· DDBJ | Genomic DNA |