Q8X4I9 (ALR2_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 84.
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, catabolic EC=5.1.1.1 | ||||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83334 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 356 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA By similarity. HAMAP-Rule MF_01201 |
| Catalytic activity | L-alanine = D-alanine. HAMAP-Rule MF_01201 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 |
| Sequence similarities | Belongs to the alanine racemase family. |
| Sequence caution | The sequence BAB35108.1 differs from that shown. Reason: Frameshift at position 321. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Isomerase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | alanine metabolic process Inferred from electronic annotation. Source: InterPro |
| 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 – 356 | 356 | Alanine racemase, catabolic HAMAP-Rule MF_01201 | PRO_0000114519 | |||||
Sites | |||||||||
| Active site | 35 | 1 | Proton acceptor; specific for D-alanine By similarity | ||||||
| Active site | 253 | 1 | Proton acceptor; specific for L-alanine By similarity | ||||||
| Binding site | 130 | 1 | Substrate By similarity | ||||||
| Binding site | 301 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 35 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 314 – 315 | 2 | AG → RD in BAB35108. Ref.2 | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG56041.1. BA000007 Genomic DNA. Translation: BAB35108.1. Frameshift. |
| PIR | E85697. E90839. |
| RefSeq | NP_287429.1. NC_002655.2. NP_309712.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | Q8X4I9. |
| SMR | Q8X4I9. Positions 3-356. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 155864.Z1953. |
Proteomic databases | |
| PRIDE | Q8X4I9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAG56041; AAG56041; Z1953. BAB35108; BAB35108; BAB35108. |
| GeneID | 913184. 960219. |
| KEGG | ece:Z1953. ecs:ECs1685. |
| PATRIC | 18352622. VBIEscCol44059_1536. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0787. |
| HOGENOM | HOG000031446. |
| KO | K01775. |
| OMA | GQWQDIA. |
| ProtClustDB | PRK03646. |
Enzyme and pathway databases | |
| BioCyc | ECOL386585:GJFA-1667-MONOMER. |
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 | ALR2_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8X4I9 Secondary accession number(s): Q8X2W4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
