Q9S5V6 (ALR_BACPS) 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: Alanine racemase EC=5.1.1.1 | ||
| Gene names |
| ||
| Organism | Bacillus psychrosaccharolyticus | ||
| Taxonomic identifier | 1407 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 383 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. |
| 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 | Homodimer. |
| Sequence similarities | Belongs to the alanine racemase family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 8-10. HAMAP MF_01201 Temperature dependence: Highly active at low temperatures, even at 0 degree Celsius. Thermolabile. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Isomerase |
| Technical term | Direct protein sequencing |
| 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 – 383 | 383 | Alanine racemase HAMAP MF_01201 | PRO_0000114498 | |||||
Sites | |||||||||
| Active site | 41 | 1 | Proton acceptor; specific for D-alanine By similarity | ||||||
| Active site | 266 | 1 | Proton acceptor; specific for L-alanine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 41 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Characterization of psychrophilic alanine racemase from Bacillus psychrosaccharolyticus." Okubo Y., Yokoigawa K., Esaki N., Soda K., Kawai H. Biochem. Biophys. Res. Commun. 256:333-340(1999) [PubMed: 10080917] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-50. |
| [2] | "Alanine racemase gene fragments as probes for detecting Bacillus stearothermophilus and Bacillus psychrosaccharolyticus in foods." Okubo Y., Yokoigawa K., Kawai H. J. Ferment. Bioeng. 85:559-563(1998) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-166. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB021683 Genomic DNA. Translation: BAA76373.1. AB011668 Genomic DNA. Translation: BAA31255.1. |
3D structure databases | |
| ProteinModelPortal | Q9S5V6. |
| SMR | Q9S5V6. Positions 5-382. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| BRENDA | 5.1.1.1. 7181. |
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. |
| 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_BACPS | ||||||||
| Accession | Primary (citable) accession number: Q9S5V6 Secondary accession number(s): O82941 | ||||||||
| 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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