A0A0M9X5X4 · A0A0M9X5X4_9ACTN
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids564 (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 | 100 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 183-189 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTSGKTT | ||||||
Binding site | 224-225 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 251 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 259 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 453 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 477-480 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: DNPR | ||||||
Binding site | 533 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 537 | 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 > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A0M9X5X4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 291 | 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, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-68 | Disordered | ||||
Sequence: MTRTEHRATRNHPVTTITPDPGNQNASRPSLGPPTGAPGTLTAVPHADQSQTTQKGHPVTYPGPPRPV | ||||||
Compositional bias | 11-31 | Polar residues | ||||
Sequence: NHPVTTITPDPGNQNASRPSL | ||||||
Compositional bias | 44-58 | Polar residues | ||||
Sequence: VPHADQSQTTQKGHP | ||||||
Domain | 92-167 | Mur ligase N-terminal catalytic | ||||
Sequence: EVTGITHDSRAVRPGDLYAALPGARAHGADFVTQAAGLGAVAVLTDPSGAERVAAAGLPALVVDDPRARMGELAAT | ||||||
Domain | 181-381 | Mur ligase central | ||||
Sequence: ITGTSGKTTTAYLVEGGLKTVHSTGLIGTVEMRIGDERIKSERTTPEATDLQALFAVMRERGTDAVAMEVSSHALVLGRVDGCVFDIAVFTNLSPEHMEFHSGMEDYFRAKAQLFTPERSRLGVVNVDDEYGRRLVKEAGVPVVTYSAEGHPDADWRAEDVTVGPMDSTFTVIGPGGERIGAKSPLPGPFNVANTLAAIVA | ||||||
Domain | 404-535 | Mur ligase C-terminal | ||||
Sequence: GRLERVDAGQPYLAVVDYAHKTDAVESVLRALRKVTEGRVHVVLGCGGDRDTTKRMPMGAAAARLADTAVLTSDNPRSEDPLSILAAMLHGAASVPAHERGEVQVFEDRAAAIAAAVARARPGDTVLVAGKG | ||||||
Motif | 477-480 | Meso-diaminopimelate recognition motif | ||||
Sequence: DNPR |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length564
- Mass (Da)58,736
- Last updated2015-12-09 v1
- Checksum395F6C58EC2DA83D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-31 | Polar residues | ||||
Sequence: NHPVTTITPDPGNQNASRPSL | ||||||
Compositional bias | 44-58 | Polar residues | ||||
Sequence: VPHADQSQTTQKGHP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LGCN01000251 EMBL· GenBank· DDBJ | KOT29175.1 EMBL· GenBank· DDBJ | Genomic DNA |