C6AHR9 (C6AHR9_BIFAS) Unreviewed, UniProtKB/TrEMBL
Last modified
May 29, 2013.
Version 31.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Alanine racemase HAMAP-Rule MF_01201 RuleBase RU000608 EC=5.1.1.1 HAMAP-Rule MF_01201 RuleBase RU000608 | ||
| Gene names |
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| Organism | Bifidobacterium animalis subsp. lactis (strain DSM 10140 / JCM 10602 / LMG 18314) [Complete proteome] [HAMAP] EMBL ACS47526.1 | ||
| Taxonomic identifier | 555970 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium › ![]() |
Protein attributes
| Sequence length | 455 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. HAMAP-Rule MF_01201 |
| Catalytic activity | L-alanine = D-alanine. HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622 |
| Pathway | Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201 RuleBase RU004247 SAAS SAAS020622 |
| Sequence similarities | Belongs to the alanine racemase family. HAMAP-Rule MF_01201 RuleBase RU004188 |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622 |
| Molecular function | Isomerase HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | D-alanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 66 | 1 | Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201 | ||||||
| Active site | 306 | 1 | Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201 | ||||||
| Binding site | 168 | 1 | Substrate By similarity HAMAP-Rule MF_01201 | ||||||
| Binding site | 370 | 1 | Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 66 | 1 | N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201 | ||||||
Sequences
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References
| [1] | "Comparison of the complete genome sequences of Bifidobacterium animalis subsp. lactis DSM 10140 and Bl-04." Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., Richards M., Horvath P., Coute-Monvoisin A.-C., Leyer G., Rendulic S., Steele J.L., Broadbent J.R., Oberg T., Dudley E.G., Schuster S., Romero D.A., Roberts R.F. J. Bacteriol. 191:4144-4151(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 10140 / JCM 10602 / LMG 18314. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001606 Genomic DNA. Translation: ACS47526.1. |
| RefSeq | YP_002969588.1. NC_012815.1. |
3D structure databases | |
| ProteinModelPortal | C6AHR9. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 555970.Balat_0584. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACS47526; ACS47526; Balat_0584. |
| GeneID | 8010206. |
| KEGG | blt:Balat_0584. |
| PATRIC | 21110740. VBIBifAni93544_0592. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0787. |
| HOGENOM | HOG000031444. |
| KO | K01775. |
| OMA | GQWQDIA. |
| ProtClustDB | CLSK572926. |
Enzyme and pathway databases | |
| BioCyc | BANI555970:GJ22-584-MONOMER. |
| 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 | C6AHR9_BIFAS | ||||||||
| Accession | Primary (citable) accession number: C6AHR9 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
