Reviewed,
UniProtKB/Swiss-Prot P0A1A3 (ALR1_SALTY)
Last modified
February 9, 2010.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alanine racemase, biosynthetic EC=5.1.1.1 | ||||
| Gene names |
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| Organism | Salmonella typhimurium [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 90371 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 359 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Provides the D-alanine required for cell wall biosynthesis. HAMAP MF_01201 |
| Catalytic activity | L-alanine = D-alanine. HAMAP MF_01201 |
| Cofactor | Pyridoxal phosphate. 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 |
| Subunit structure | Monomer. HAMAP MF_01201 |
| Sequence similarities | Belongs to the alanine racemase family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 8.5. HAMAP MF_01201 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Isomerase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | alanine metabolic process Inferred from electronic annotation. Source: HAMAP cellular 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 |
| Molecular function | alanine racemase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 359 | 359 | Alanine racemase, biosynthetic HAMAP MF_01201 | PRO_0000114559 | |||||
Sites | |||||||||
| Active site | 34 | 1 | Proton acceptor; specific for D-alanine By similarity | ||||||
| Active site | 255 | 1 | Proton acceptor; specific for L-alanine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 34 | 1 | N6-(pyridoxal phosphate)lysine HAMAP MF_01201 | ||||||
Experimental info | |||||||||
| Sequence conflict | 5 | 1 | T → S AA sequence Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Biosynthetic alr alanine racemase from Salmonella typhimurium: DNA and protein sequence determination." Galakatos N.G., Daub E., Botstein D., Walsh C.T. Biochemistry 25:3255-3260(1986) [PubMed: 3524676] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K.Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720. |
| [3] | "Biosynthetic alanine racemase of Salmonella typhimurium: purification and characterization of the enzyme encoded by the alr gene." Esaki N., Walsh C.T. Biochemistry 25:3261-3267(1986) [PubMed: 3524677] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-9 AND 29-46, CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M12847 Genomic DNA. Translation: AAA27022.1. AE006468 Genomic DNA. Translation: AAL23071.1. |
| PIR | A24102. |
| RefSeq | NP_463112.1. |
3D structure databases | |
| SMR | P0A1A3. Positions 1-359. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0A1A3. |
Genome annotation databases | |
| GeneID | 1255773. |
| GenomeReviews | Gene locus STM4247 in contig AE006468_GR. |
| KEGG | stm:STM4247. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG712172. |
| OMA | EGTPVWV. |
Enzyme and pathway databases | |
| BioCyc | STYP99287:STM4247-MONOMER. |
| BRENDA | 5.1.1.1. 2. |
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] |
| Pfam | PF00842. Ala_racemase_C. 1 hit. PF01168. Ala_racemase_N. 1 hit. [Graphical view] |
| PRINTS | PR00992. ALARACEMASE. |
| TIGRFAMs | TIGR00492. alr. 1 hit. |
| PROSITE | PS00395. ALANINE_RACEMASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ALR1_SALTY | ||||||||
| Accession | Primary (citable) accession number: P0A1A3 Secondary accession number(s): P06655 | ||||||||
| 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 |

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