Reviewed,
UniProtKB/Swiss-Prot Q9PC57 (NADB_XYLFA)
Last modified
November 3, 2009.
Version 51.
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 |
| ||||
| Organism | Xylella fastidiosa [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2371 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella |
Protein attributes
| Sequence length | 512 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 | 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-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] | "The genome sequence of the plant pathogen Xylella fastidiosa." Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. Setubal J.C.Nature 406:151-159(2000) [PubMed: 10910347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9a5c. |
Cross-references
Sequence databases | |
|---|---|
| AE003849 Genomic DNA. Translation: AAF84730.1. | |
| PIR | A82621. |
| RefSeq | NP_299210.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CHU based on UniProtKB P10902. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1127475. |
| GenomeReviews | Gene locus XF_1924 in contig AE003849_GR. |
| KEGG | xfa:XF1924. |
| NMPDR | fig|160492.1.peg.1917. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9PC57. |
| OMA | GAYIWNR. |
Enzyme and pathway databases | |
| BioCyc | XFAS160492:XF1924-MON. |
| BRENDA | 1.4.3.16. 278708. |
Family and domain databases | |
| InterPro | IPR003953. FAD_bind2_N. IPR004112. Fum_Rdtase/Succ_DH_flav_C. [Graphical view] |
| Pfam | PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NADB_XYLFA | ||||||||
| Accession | Primary (citable) accession number: Q9PC57 | ||||||||
| 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


