A5VI51 (ALR_LACRD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 31.
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: Alanine racemase EC=5.1.1.1 | ||||
| Gene names |
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| Organism | Lactobacillus reuteri (strain DSM 20016) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 557436 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus |
Protein attributes
| Sequence length | 375 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Provides the D-alanine required for cell wall biosynthesis By similarity. HAMAP MF_01201 |
| Catalytic activity | L-alanine = D-alanine. HAMAP MF_01201 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP MF_01201 |
| Pathway | Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP MF_01201 Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_01201 |
| Sequence similarities | Belongs to the alanine racemase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Isomerase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | alanine metabolic process Inferred from electronic annotation. Source: InterPro 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 |
| Molecular function | alanine racemase activity Inferred 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 – 375 | 375 | Alanine racemase HAMAP MF_01201 | PRO_1000066002 | |||||
Sites | |||||||||
| Active site | 40 | 1 | Proton acceptor; specific for D-alanine By similarity | ||||||
| Active site | 268 | 1 | Proton acceptor; specific for L-alanine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 40 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri." Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L. Walter J.PLoS Genet. 7:E1001314-E1001314(2011) [PubMed: 21379339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 20016. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000705 Genomic DNA. Translation: ABQ82525.1. |
| RefSeq | YP_001270862.1. NC_009513.1. |
3D structure databases | |
| ProteinModelPortal | A5VI51. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A5VI51. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5189698. |
| GenomeReviews | Gene locus Lreu_0255 in contig CP000705_GR. |
| KEGG | lre:Lreu_0255. |
| PATRIC | 22253592. VBILacReu87937_0264. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG712172. |
| OMA | HYEIACN. |
| ProtClustDB | CLSK2326072. |
Enzyme and pathway databases | |
| BioCyc | LREU557436:LREU_0255-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01201. Ala_racemase. [Tree] |
| InterPro | IPR000821. Ala_racemase. IPR009006. Ala_racemase/Decarboxylase_C. IPR011079. Ala_racemase_C. IPR001608. Ala_racemase_N. IPR020622. Ala_racemase_pyridoxalP-BS. [Graphical view] |
| Gene3D | G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit. |
| KO | K01775. |
| Pfam | PF00842. Ala_racemase_C. 1 hit. PF01168. Ala_racemase_N. 1 hit. [Graphical view] |
| PRINTS | PR00992. ALARACEMASE. |
| SMART | SM01005. Ala_racemase_C. 1 hit. [Graphical view] |
| SUPFAM | SSF50621. Racem_decarbox_C. 1 hit. |
| TIGRFAMs | TIGR00492. Alr. 1 hit. |
| PROSITE | PS00395. ALANINE_RACEMASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ALR_LACRD | ||||||||
| Accession | Primary (citable) accession number: A5VI51 | ||||||||
| 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 |

Clusters with