A0A9D5RKK9 · A0A9D5RKK9_9FIRM
- ProteinMultifunctional fusion protein
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids769 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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.
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic activity
- (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Cofactor
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 30 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 110-116 | ATP (UniProtKB | ChEBI) | |||
Binding site | 151 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 152-153 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 179 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 187 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 380 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 404-407 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 456 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 460 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 496 | substrate | |||
Binding site | 551 | substrate | |||
Active site | 560 | ||||
Active site | 560 | Proton donor | |||
Binding site | 561-562 | substrate | |||
Binding site | 652 | substrate | |||
Site | 654 | Could be important to modulate the pK values of the two catalytic cysteine residues | |||
Binding site | 685 | substrate | |||
Site | 703 | Could be important to modulate the pK values of the two catalytic cysteine residues | |||
Binding site | 703-704 | substrate | |||
Active site | 712 | Proton acceptor | |||
Binding site | 713-714 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | diaminopimelate epimerase activity | |
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 | lysine biosynthetic process via diaminopimelate | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- EC number
- Alternative names
- Recommended nameDiaminopimelate epimerase
- EC number
- Short namesDAP epimerase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae
Accessions
- Primary accessionA0A9D5RKK9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 221 | N6-carboxylysine | |||
Post-translational modification
Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 23-95 | Mur ligase N-terminal catalytic | |||
Domain | 108-309 | Mur ligase central | |||
Domain | 331-458 | Mur ligase C-terminal | |||
Motif | 404-407 | Meso-diaminopimelate recognition motif | |||
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Belongs to the diaminopimelate epimerase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length769
- Mass (Da)84,898
- Last updated2023-05-03 v1
- ChecksumEFCA6B02CCDA00B2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SVEO01000001 EMBL· GenBank· DDBJ | MBE5921199.1 EMBL· GenBank· DDBJ | Genomic DNA |