Reviewed,
UniProtKB/Swiss-Prot Q929Z2 (NADB_LISIN)
Last modified
November 3, 2009.
Version 45.
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 | Listeria innocua [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1642 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria |
Protein attributes
| Sequence length | 484 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 + O2 = iminosuccinate + H2O2. |
| Cofactor | FAD. |
| Pathway | |
| Subcellular location | Cytoplasm By 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 | NAD biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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] | "Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. Cossart P.Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIP 11262 / Serovar 6a. |
Cross-references
Sequence databases | |
|---|---|
| AL596171 Genomic DNA. Translation: CAC97361.1. | |
| PIR | AI1698. |
| RefSeq | NP_471465.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CHU based on UniProtKB P10902. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1130858. |
| GenomeReviews | Gene locus lin2131 in contig AL592022_GR. |
| KEGG | lin:lin2131. |
| NMPDR | fig|272626.1.peg.2118. |
Organism-specific databases | |
| ListiList | LIN02131. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q929Z2. |
| OMA | GAYIWNR. |
Enzyme and pathway databases | |
| BioCyc | LINN272626:LIN2131-MON. |
| BRENDA | 1.4.3.16. 270396. |
Family and domain databases | |
| InterPro | IPR003953. FAD_bind2_N. IPR005288. NadB. [Graphical view] |
| Pfam | PF00890. FAD_binding_2. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00551. nadB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | NADB_LISIN | ||||||||
| Accession | Primary (citable) accession number: Q929Z2 | ||||||||
| 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


