J7RFV2 (J7RFV2_BORP1) Unreviewed, UniProtKB/TrEMBL
Last modified
May 29, 2013.
Version 7.
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 |
| ||||
| Organism | Bordetella pertussis (strain ATCC 9797 / DSM 5571 / NCTC 10739 / 18323) [Complete proteome] [HAMAP] EMBL CCJ62265.1 | ||||
| Taxonomic identifier | 568706 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › ![]() |
Protein attributes
| Sequence length | 387 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 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 EMBL CCJ62265.1 |
| 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 | 49 | 1 | Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201 | ||||||
| Active site | 272 | 1 | Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201 | ||||||
| Binding site | 144 | 1 | Substrate By similarity HAMAP-Rule MF_01201 | ||||||
| Binding site | 320 | 1 | Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 49 | 1 | N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Comparative genomics of the classical Bordetella subspecies: the evolution and exchange of virulence-associated diversity amongst closely related pathogens." Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M., Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T. BMC Genomics 13:545-545(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9797 / DSM 5571 / NCTC 10739 / 18323. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | HE965805 Genomic DNA. Translation: CCJ62265.1. |
| RefSeq | YP_006625550.1. NC_018518.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CCJ62265; CCJ62265; BN118_0840. |
| GeneID | 13801130. |
| KEGG | bper:BN118_0840. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| KO | K01775. |
Enzyme and pathway databases | |
| 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 | J7RFV2_BORP1 | ||||||||
| Accession | Primary (citable) accession number: J7RFV2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
