F2JMR3 (F2JMR3_CELLD) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 16.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Submitted name: Alanine racemase EMBL ADZ84714.1 EC=5.1.1.1 EMBL ADZ84714.1 | ||
| Gene names |
| ||
| Organism | Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5) (Clostridium lentocellum) [Complete proteome] [HAMAP] EMBL ADZ84714.1 | ||
| Taxonomic identifier | 642492 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Lachnospiraceae › Cellulosilyticum › ![]() |
Protein attributes
| Sequence length | 377 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | L-alanine = D-alanine. RuleBase RU000608 SAAS SAAS020622 |
| Cofactor | Pyridoxal phosphate By similarity. RuleBase RU000608 SAAS SAAS020622 |
| Pathway | Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. SAAS SAAS020622 RuleBase RU004247 |
| Sequence similarities | Belongs to the alanine racemase family. RuleBase RU004188 |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate SAAS SAAS020622 RuleBase RU000608 |
| Molecular function | Isomerase RuleBase RU000608 SAAS SAAS020622 EMBL ADZ84714.1 |
| 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... | |
Sequences
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References
| [1] | "Complete genome sequence of the cellulose-degrading bacterium Cellulosilyticum lentocellum." US DOE Joint Genome Institute Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C., Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S., Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G., Angert E.R., Currie C.R. J. Bacteriol. 193:2357-2358(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP002582 Genomic DNA. Translation: ADZ84714.1. |
| RefSeq | YP_004309912.1. NC_015275.1. |
3D structure databases | |
| ProteinModelPortal | F2JMR3. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADZ84714; ADZ84714; Clole_3017. |
| GeneID | 10332753. |
| KEGG | cle:Clole_3017. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| KO | K01775. |
Enzyme and pathway databases | |
| BioCyc | CCLO642492:GIWK-3142-MONOMER. |
| 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 | F2JMR3_CELLD | ||||||||
| Accession | Primary (citable) accession number: F2JMR3 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
