A0A174DZL9 · A0A174DZL9_PHOVU
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids484 (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 | 30 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 111-117 | ATP (UniProtKB | ChEBI) | |||
Binding site | 153-154 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 180 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 186 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 188 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 378 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 402-405 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 455 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 459 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
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
- Strains
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Phocaeicola
Accessions
- Primary accessionA0A174DZL9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 220 | N6-carboxylysine | |||
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 | 22-97 | Mur ligase N-terminal catalytic | |||
Domain | 109-305 | Mur ligase central | |||
Domain | 327-457 | Mur ligase C-terminal | |||
Motif | 402-405 | Meso-diaminopimelate recognition motif | |||
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length484
- Mass (Da)53,283
- Last updated2016-09-07 v1
- MD5 Checksum7C63D08726BB61521B20E1B0B939E9C2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CYZI01000007 EMBL· GenBank· DDBJ | CUO31001.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WCIF01000022 EMBL· GenBank· DDBJ | KAB5434820.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WDAY01000046 EMBL· GenBank· DDBJ | KAB6557591.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WDAX01000001 EMBL· GenBank· DDBJ | KAB6577339.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAHPYS010000039 EMBL· GenBank· DDBJ | MBU9140318.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAJCQG010000047 EMBL· GenBank· DDBJ | MCB7282230.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAKNGO010000047 EMBL· GenBank· DDBJ | MCG4690324.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAMOYI010000040 EMBL· GenBank· DDBJ | MCM1845919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAQKEI010000038 EMBL· GenBank· DDBJ | MDB0853878.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JABDSD010000059 EMBL· GenBank· DDBJ | NMX07305.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JABWDJ010000040 EMBL· GenBank· DDBJ | NVB74116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP043529 EMBL· GenBank· DDBJ | QEW38458.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QSPP01000072 EMBL· GenBank· DDBJ | RGJ82149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QSQC01000034 EMBL· GenBank· DDBJ | RGK10885.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QSSN01000007 EMBL· GenBank· DDBJ | RGL86880.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QSTG01000044 EMBL· GenBank· DDBJ | RGM40417.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QRXI01000016 EMBL· GenBank· DDBJ | RGT91816.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QRKA01000004 EMBL· GenBank· DDBJ | RHH82118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QRMN01000045 EMBL· GenBank· DDBJ | RHJ73849.1 EMBL· GenBank· DDBJ | Genomic DNA |