Reviewed,
UniProtKB/Swiss-Prot Q8A254 (MURE_BACTN)
Last modified
November 3, 2009.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase EC=6.3.2.13 Alternative name(s): UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase Meso-diaminopimelate-adding enzyme Meso-A2pm-adding enzyme UDP-N-acetylmuramyl-tripeptide synthetase UDP-MurNAc-tripeptide synthetase | ||||
| Gene names |
| ||||
| Organism | Bacteroides thetaiotaomicron [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 818 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides |
Protein attributes
| Sequence length | 482 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| 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 By similarity. |
| Catalytic activity | ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. HAMAP MF_00208 |
| Pathway | Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208 |
| Subcellular location | Cytoplasm By similarity. |
| Post-translational modification | Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. |
| Sequence similarities | Belongs to the murCDEF family. MurE subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell divisionInferred from electronic annotation. Source: UniProtKB-KW cell wall organizationInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: HAMAP regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 482 | 482 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208 | PRO_0000101867 | |||||
Regions | |||||||||
| Nucleotide binding | 111 – 117 | 7 | ATP Potential | ||||||
| Region | 153 – 154 | 2 | UDP-MurNAc-L-Ala-D-Glu binding By similarity | ||||||
| Region | 402 – 405 | 4 | Meso-diaminopimelate binding By similarity | ||||||
| Motif | 402 – 405 | 4 | Meso-diaminopimelate recognition motif HAMAP MF_00208 | ||||||
Sites | |||||||||
| Binding site | 30 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 180 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 186 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 188 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 378 | 1 | Meso-diaminopimelate By similarity | ||||||
| Binding site | 455 | 1 | Meso-diaminopimelate; via carbonyl oxygen By similarity | ||||||
| Binding site | 459 | 1 | Meso-diaminopimelate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 220 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis." Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I. Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482. |
Cross-references
Sequence databases | |
|---|---|
| AE015928 Genomic DNA. Translation: AAO78558.1. | |
| RefSeq | NP_812364.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1073969. |
| GenomeReviews | Gene locus BT_3452 in contig AE015928_GR. |
| KEGG | bth:BT_3452. |
| NMPDR | fig|226186.1.peg.3451. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8A254. |
| OMA | FPVIVDY. |
Enzyme and pathway databases | |
| BioCyc | BTHE226186:BT_3452-MON. |
| BRENDA | 6.3.2.13. 21018. |
Family and domain databases | |
| HAMAP | MF_00208. [Tree] |
| InterPro | IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view] |
| Gene3D | G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. |
| Pfam | PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01085. murE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MURE_BACTN | ||||||||
| Accession | Primary (citable) accession number: Q8A254 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


