Q1JF94 (ALR_STRPD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 41.
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 |
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| Organism | Streptococcus pyogenes serotype M2 (strain MGAS10270) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 370552 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 366 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 – 366 | 366 | Alanine racemase HAMAP MF_01201 | PRO_1000066048 | |||||
Sites | |||||||||
| Active site | 40 | 1 | Proton acceptor; specific for D-alanine By similarity | ||||||
| Active site | 263 | 1 | Proton acceptor; specific for L-alanine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 40 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus." Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., Musser J.M. Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006) [PubMed: 16636287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MGAS10270. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000260 Genomic DNA. Translation: ABF34665.1. |
| RefSeq | YP_599209.1. NC_008022.1. |
3D structure databases | |
| ProteinModelPortal | Q1JF94. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1JF94. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTRT00000040281; EBSTRP00000038765; EBSTRG00000040278. |
| GeneID | 4063656. |
| GenomeReviews | Gene locus alr in contig CP000260_GR. |
| KEGG | sph:MGAS10270_Spy1600. |
| PATRIC | 19721174. VBIStrPyo120482_1631. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0787. |
| GeneTree | EBGT00050000028408. |
| HOGENOM | HBG712172. |
| OMA | TRKEDAN. |
| ProtClustDB | PRK00053. |
Enzyme and pathway databases | |
| BioCyc | SPYO370552:MGAS10270_SPY1600-MONOMER. |
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_STRPD | ||||||||
| Accession | Primary (citable) accession number: Q1JF94 | ||||||||
| 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