Reviewed,
UniProtKB/Swiss-Prot Q9JSX4 (NADB_NEIMA)
Last modified
February 9, 2010.
Version 52.
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 | Neisseria meningitidis serogroup A [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 65699 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 502 AA. |
| Sequence status | Complete. |
| 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] | "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491." Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S. Barrell B.G.Nature 404:502-506(2000) [PubMed: 10761919] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Z2491 / Serogroup A / Serotype 4A. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL157959 Genomic DNA. Translation: CAM09193.1. |
| PIR | E81780. |
| RefSeq | YP_002343347.1. |
3D structure databases | |
| SMR | Q9JSX4. Positions 3-502. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 907351. |
| GenomeReviews | Gene locus NMA2092 in contig AL157959_GR. |
| KEGG | nma:NMA2092. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG293998. |
| OMA | GAYIWNR. |
Enzyme and pathway databases | |
| BioCyc | NMEN122587:NMA2092-MONOMER. |
| BRENDA | 1.4.3.16. 292829. |
Family and domain databases | |
| InterPro | IPR003953. FAD_bind2_N. IPR015939. Fum_Rdtase/Succ_DH_flav-like_C. IPR004112. Fum_Rdtase/Succ_DH_flav_C. IPR005288. NadB. [Graphical view] |
| Pfam | PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00551. nadB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | NADB_NEIMA | ||||||||
| Accession | Primary (citable) accession number: Q9JSX4 Secondary accession number(s): A1ITS5 | ||||||||
| 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


