Q732F6 (MURD_BACC1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 61.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: UDP-N-acetylmuramoylalanine--D-glutamate ligase EC=6.3.2.9 Alternative name(s): D-glutamic acid-adding enzyme UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | ||||
| Gene names |
| ||||
| Organism | Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 222523 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 450 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) By similarity. HAMAP MF_00639 |
| Catalytic activity | ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. HAMAP MF_00639 |
| Pathway | Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00639 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00639. |
| Sequence similarities | Belongs to the MurCDEF family. |
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 cellular cell wall organizationInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW UDP-N-acetylmuramoylalanine-D-glutamate 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 – 450 | 450 | UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639 | PRO_0000108960 | |||||
Regions | |||||||||
| Nucleotide binding | 119 – 125 | 7 | ATP Potential | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017194 Genomic DNA. Translation: AAS42861.1. |
| RefSeq | NP_980253.1. NC_003909.8. |
3D structure databases | |
| ProteinModelPortal | Q732F6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q732F6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000027120; EBBACP00000026470; EBBACG00000027111. |
| GeneID | 2750493. |
| GenomeReviews | Gene locus BCE_3958 in contig AE017194_GR. |
| KEGG | bca:BCE_3958. |
| NMPDR | fig|222523.1.peg.3925. |
| PATRIC | 18856570. VBIBacCer118379_3784. |
| TIGR | BCE_3958. |
Phylogenomic databases | |
| eggNOG | COG0771. |
| GeneTree | EBGT00070000032130. |
| HOGENOM | HBG750024. |
| OMA | ACASWDM. |
| ProtClustDB | PRK02472. |
Enzyme and pathway databases | |
| BioCyc | BCER405917:BCE_3958-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00639. MurD. [Tree] |
| InterPro | IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR016040. NAD(P)-bd_dom. IPR005762. UDP-N-AcMur-Glu_ligase. [Graphical view] |
| Gene3D | G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K01925. |
| PANTHER | PTHR23135:SF2. PTHR23135:SF2. 1 hit. |
| Pfam | PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view] |
| SUPFAM | SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit. |
| TIGRFAMs | TIGR01087. MurD. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MURD_BACC1 | ||||||||
| Accession | Primary (citable) accession number: Q732F6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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