P10725 (ALR1_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 110.
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 1 EC=5.1.1.1 | ||||||
| Gene names |
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| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 389 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity. |
| Catalytic activity | L-alanine = D-alanine. HAMAP-Rule MF_01201 |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201 |
| Sequence similarities | Belongs to the alanine racemase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Isomerase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | D-alanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway peptidoglycan biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway 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 – 389 | 389 | Alanine racemase 1 HAMAP-Rule MF_01201 | PRO_0000114500 | |||||
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 | ||||||
| Binding site | 137 | 1 | Substrate By similarity | ||||||
| Binding site | 313 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 41 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 40 | 1 | V → E in AAA22378. Ref.1 | ||||||
| Sequence conflict | 66 | 1 | V → M in AAA22378. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation of an alanine racemase gene from Bacillus subtilis and its use for plasmid maintenance in B. subtilis." Ferrari E., Henner D.J., Yang M.Y. Biotechnology (N.Y.) 3:1003-1007(1985) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus subtilis genome." Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [3] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M16207 Genomic DNA. Translation: AAA22378.1. AB001488 Genomic DNA. Translation: BAA19301.1. AL009126 Genomic DNA. Translation: CAB12271.1. |
| PIR | JS0443. |
| RefSeq | NP_388345.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P10725. |
| SMR | P10725. Positions 4-382. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU04640. |
Proteomic databases | |
| PaxDb | P10725. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB12271; CAB12271; BSU04640. |
| GeneID | 939942. |
| KEGG | bsu:BSU04640. |
| PATRIC | 18972512. VBIBacSub10457_0484. |
Organism-specific databases | |
| GenoList | BSU04640. [Micado] |
Phylogenomic databases | |
| eggNOG | COG0787. |
| HOGENOM | HOG000031444. |
| KO | K01775. |
| OMA | IRLPKAY. |
| ProtClustDB | CLSK886745. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU04640-MONOMER. |
| SABIO-RK | P10725. |
| UniPathway | UPA00042; UER00497. |
Family and domain databases | |
| Gene3D | 2.40.37.10. 1 hit. |
| HAMAP | MF_01201. Ala_racemase. |
| 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. |
| 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 | ALR1_BACSU | ||||||||
| Accession | Primary (citable) accession number: P10725 Secondary accession number(s): P96620 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
