N9VMT5 · N9VMT5_9GAMM
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids493 (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 | 26 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 28 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 43-45 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: HQV | ||||||
Binding site | 111-117 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTNGKST | ||||||
Binding site | 152 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 153-154 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 180 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 186 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 188 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 384 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 408-411 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: DNPR | ||||||
Binding site | 459 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 463 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Aeromonadales > Aeromonadaceae > Aeromonas
Accessions
- Primary accessionN9VMT5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 220 | 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 | 21-97 | Mur ligase N-terminal catalytic | ||||
Sequence: LTGITLDSREVRQGFLFVAVKGHQVDGRRFIEQAVAQGAAAVLFEADEGYVAPAVGVPCVGIPDLSAHLSTLAGRFY | ||||||
Domain | 109-312 | Mur ligase central | ||||
Sequence: VTGTNGKSTTALLVANWRTLLGGRAGVMGTVGNGLFGELVEAANTTGSAIEVQGTLRALRDQGADLVAMEVSSHGLVQHRVAGVRFAAAAYTNLSRDHLDYHGTMEAYGEAKERLLDLVAERCAVINGDDELGRQWLARRPAAVAYSMEGGVTGHQGPQLLASELEFHQQGFRARITSPWGNGVLSAPLLGRFNVANVLAAMGV | ||||||
Domain | 335-461 | Mur ligase C-terminal | ||||
Sequence: GRMECFGGQGKPLAVVDYAHTPDALEKALAALRVHCHGRLWCLVGCGGDRDRGKRPMMAAMAERHADRVILTDDNPRTEEPRQIMADMVAGLSQPETVQIEHDRVTAIRLALTQAGPQDIVLVAGKG | ||||||
Motif | 408-411 | Meso-diaminopimelate recognition motif | ||||
Sequence: DNPR |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length493
- Mass (Da)52,807
- Last updated2013-06-26 v1
- Checksum0C06C934E165E7C5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
APVG01000010 EMBL· GenBank· DDBJ | ENY72903.1 EMBL· GenBank· DDBJ | Genomic DNA |