A0A1T1AR44 · A0A1T1AR44_RHOFE
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids504 (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: S | ||||||
Binding site | 109-115 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTNGKTS | ||||||
Binding site | 155-156 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 182 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 190 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 391 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 415-418 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: DNPR | ||||||
Binding site | 466 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 470 | 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 > Betaproteobacteria > Burkholderiales > Comamonadaceae > Rhodoferax
Accessions
- Primary accessionA0A1T1AR44
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 222 | N6-carboxylysine | ||||
Sequence: K |
Post-translational modification
Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 107-316 | Mur ligase central | ||||
Sequence: VTGTNGKTSTAWWLAQALSNLKQAAPIPCGLVGTLGIGVPPDVVSTGLTTPDPVALQSAFARFVAQGFGACAIEASSIGIEEHRLDGTQIHTAILTNLTQDHLDYHGSMEAYWQAKSKLFAWPGLCAAVVNVDDAYGADLAHTLAGSALDLWSVSMLPGVGNGARLQAQAIDYSQGGTRCTVVEAEQALPLATGLIGDYNVANLLGVIAT | ||||||
Domain | 339-468 | Mur ligase C-terminal | ||||
Sequence: GRMECVNQPGQPLVAVDYAHTPDALAKALDALKPVAAQRGGQLWCVFGCGGDRDTSKRPLMGAVAASHADRVLVTSDNPRSEAPDAIICQILLGLSGVPGVMVEPDRARAISQAITQAAAADVVLVAGKG | ||||||
Motif | 415-418 | Meso-diaminopimelate recognition motif | ||||
Sequence: DNPR |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length504
- Mass (Da)52,118
- Last updated2017-05-10 v1
- ChecksumF90758D49E438B0F
Keywords
- Technical term