A0A5D0S2S0 · A0A5D0S2S0_9RHOB
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids499 (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 | 35 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 120-126 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTNGKTS | ||||||
Binding site | 161-162 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 188 | 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: Q | ||||||
Binding site | 196 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 393 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 417-420 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: DNPR | ||||||
Binding site | 465 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 469 | 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 > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Oceaniovalibus
Accessions
- Primary accessionA0A5D0S2S0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 228 | 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 | 28-104 | Mur ligase N-terminal catalytic | ||||
Sequence: ITGLAVDSRDVVEGTLFAALPGGRVHGGDFIGFALRMGASAILTDREGARRAADDLASSSVALVVAEDPRQTLALAA | ||||||
Domain | 119-320 | Mur ligase central | ||||
Sequence: TGTNGKTSVATFTRQIWMALGHVAVNLGTTGVEGAYSAPLKHTTPEPVTLHRMLAKLANAGITHAAMEASSHGLDQRRLDGVHLSAAAFTNMTQDHLDYHATFADYFKAKAGLFSRVLSEDAIAVINIDGAYASEMAQAAELRGQDVLRVGRSGDASLRILNQRFDATGQDLRFSFNGRVDQVRLNLIGGFQAENVLVAAGL | ||||||
Domain | 343-467 | Mur ligase C-terminal | ||||
Sequence: GRMQLAATRDNGAAVFVDYAHTPDALATALSNLRPHVMGRLIVVYGAGGDRDTSKRPLMGAAAAKHADVRIVTDDNPRSEEPAVIRSQILQSDPEASEVGDRAEAILRGIDALEPGDALLIAGKG | ||||||
Motif | 417-420 | Meso-diaminopimelate recognition motif | ||||
Sequence: DNPR |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length499
- Mass (Da)52,474
- Last updated2019-11-13 v1
- ChecksumF5EFBD6DDE8CF619
Keywords
- Technical term