Reviewed,
UniProtKB/Swiss-Prot Q8XNE2 (NADB_CLOPE)
Last modified
November 25, 2008.
Version 37.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: L-aspartate oxidase Short name=LASPO EC=1.4.3.16 Alternative name(s): Quinolinate synthetase B | ||||
| Gene names |
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| Organism | Clostridium perfringens [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1502 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 439 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the oxidation of L-aspartate to iminoaspartate. |
| Catalytic activity | L-aspartate + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2). |
| Cofactor | FAD. |
| Pathway | |
| Subcellular location | CytoplasmBy similarity. |
| Sequence similarities | Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily. |
Ontologies
Keywords | |
|---|---|
| Biological process | Pyridine nucleotide biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridine nucleotide biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-aspartate oxidase activity Inferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater." Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H. Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed: 11792842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 13 / Type A. |
Cross-references
Sequence databases | |
|---|---|
| BA000016 Genomic DNA. Translation: BAB80101.1. | |
| RefSeq | NP_561311.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CHU based on UniProtKB P10902. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 988648. |
| GenomeReviews | Gene locus CPE0395 in contig BA000016_GR. |
| KEGG | cpe:CPE0395. |
| NMPDR | fig|195102.1.peg.458. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8XNE2. |
Enzyme and pathway databases | |
| BioCyc | CPER195102:CPE0395-MON. |
Family and domain databases | |
| InterPro | IPR003953. FAD_bind2_N. [Graphical view] |
| Pfam | PF00890. FAD_binding_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NADB_CLOPE | ||||||||
| Accession | Primary (citable) accession number: Q8XNE2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


