A8FA65 (A8FA65_BACP2) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 34.
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 1 HAMAP MF_01201 EC=5.1.1.1 HAMAP MF_01201 | ||||||
| Gene names |
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| Organism | Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 315750 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 392 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 RuleBase RU000608 SAAS SAAS009006 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP MF_01201 RuleBase RU000608 SAAS SAAS009006 |
| Pathway | Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP MF_01201 SAAS SAAS009006 RuleBase RU004247 Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_01201 |
| Sequence similarities | Belongs to the alanine racemase family. HAMAP MF_01201 RuleBase RU004188 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation HAMAP MF_01201 Peptidoglycan synthesis HAMAP MF_01201 |
| Ligand | Pyridoxal phosphate HAMAP MF_01201 RuleBase RU000608 SAAS SAAS009006 |
| Molecular function | Isomerase SAAS SAAS009006 HAMAP MF_01201 RuleBase RU000608 EMBL ABV61132.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | alanine metabolic process Inferred from electronic annotation. Source: HAMAP cellular cell wall organizationInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: HAMAP regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | alanine racemase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 41 | 1 | Proton acceptor; specific for D-alanine By similarity HAMAP MF_01201 | ||||||
| Active site | 269 | 1 | Proton acceptor; specific for L-alanine By similarity HAMAP MF_01201 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 41 | 1 | N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01201 | ||||||
Sequences
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References
| [1] | "Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. Weinstock G.M.PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000813 Genomic DNA. Translation: ABV61132.1. |
| RefSeq | YP_001485692.1. NC_009848.1. |
3D structure databases | |
| ProteinModelPortal | A8FA65. |
| SMR | A8FA65. Positions 4-385. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A8FA65. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000066426; EBBACP00000064759; EBBACG00000066417. |
| GeneID | 5619664. |
| GenomeReviews | Gene locus BPUM_0437 in contig CP000813_GR. |
| KEGG | bpu:BPUM_0437. |
| PATRIC | 18964625. VBIBacPum16546_0448. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0787. |
| GeneTree | EBGT00050000001615. |
| HOGENOM | HBG712172. |
| OMA | HYEIACN. |
| ProtClustDB | CLSK886745. |
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 | A8FA65_BACP2 | ||||||||
| Accession | Primary (citable) accession number: A8FA65 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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