B7J192 (ALR_BORBZ) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 22.
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 | Borrelia burgdorferi (strain ZS7) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 445985 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group |
Protein attributes
| Sequence length | 372 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Provides the D-alanine required for cell wall biosynthesis By similarity. HAMAP MF_01201 |
| Catalytic activity | L-alanine = D-alanine. HAMAP MF_01201 |
| Cofactor | Pyridoxal phosphate By similarity. 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 |
| Sequence similarities | Belongs to the alanine racemase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Isomerase |
| Technical term | Complete proteome |
| 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 – 372 | 372 | Alanine racemase HAMAP MF_01201 | PRO_1000138581 | |||||
Sites | |||||||||
| Active site | 41 | 1 | Proton acceptor; specific for D-alanine By similarity | ||||||
| Active site | 268 | 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] | "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi." Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J., Mongodin E.F., Luft B.J. J. Bacteriol. 193:1018-1020(2011) [PubMed: 20935092] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ZS7. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001205 Genomic DNA. Translation: ACK74425.1. |
| RefSeq | YP_002374687.1. NC_011728.1. |
3D structure databases | |
| ProteinModelPortal | B7J192. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B7J192. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBORT00000003305; EBBORP00000003044; EBBORG00000003305. |
| GeneID | 7106791. |
| GenomeReviews | Gene locus BbuZS7_0159 in contig CP001205_GR. |
| KEGG | bbz:BbuZS7_0159. |
| PATRIC | 20559755. VBIBorBur54821_0301. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000007269. |
| HOGENOM | HBG712172. |
| OMA | KKIKVHL. |
| ProtClustDB | CLSK507396. |
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. |
| KO | K01775. |
| 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_BORBZ | ||||||||
| Accession | Primary (citable) accession number: B7J192 | ||||||||
| 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 |

Clusters with