GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
ECOLI:NADB
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | nadB (synonyms: nicB) | |
| Protein Name(s) | L-aspartate oxidase
LASPO Quinolinate synthase B | |
| External Links | ||
| UniProt | P10902 | |
| EMBL | X12714 D13169 D64044 U00096 AP009048 | |
| PIR | E65035 | |
| RefSeq | NP_417069.1 YP_490802.1 | |
| PDB | 1CHU 1KNP 1KNR | |
| PDBsum | 1CHU 1KNP 1KNR | |
| ProteinModelPortal | P10902 | |
| SMR | P10902 | |
| DIP | DIP-556N | |
| IntAct | P10902 | |
| STRING | 511145.b2574 | |
| DrugBank | DB03147 | |
| PaxDb | P10902 | |
| PRIDE | P10902 | |
| EnsemblBacteria | AAC75627 BAE76750 | |
| GeneID | 12934288 947049 | |
| KEGG | ecj:Y75_p2527 eco:b2574 | |
| PATRIC | 32120547 | |
| EchoBASE | EB0625 | |
| EcoGene | EG10631 | |
| eggNOG | COG0029 | |
| HOGENOM | HOG000160476 | |
| InParanoid | P10902 | |
| KO | K00278 | |
| OMA | FQHDVLV | |
| OrthoDB | EOG696BWH | |
| PhylomeDB | P10902 | |
| BioCyc | EcoCyc:L-ASPARTATE-OXID-MONOMER ECOL316407:JW2558-MONOMER MetaCyc:L-ASPARTATE-OXID-MONOMER | |
| UniPathway | UPA00253 | |
| EvolutionaryTrace | P10902 | |
| PRO | PR:P10902 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P10902 | |
| GO | GO:0005737 GO:0050660 GO:0008734 GO:0044318 GO:0034628 | |
| Gene3D | 1.20.58.100 3.90.700.10 | |
| InterPro | IPR003953 IPR013027 IPR015939 IPR005288 IPR027477 | |
| Pfam | PF00890 PF02910 | |
| PRINTS | PR00368 | |
| SUPFAM | SSF46977 SSF56425 | |
| TIGRFAMs | TIGR00551 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
involved_in |
GO:0034628 |
'de novo' NAD biosynthetic process from aspartate |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10631 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008734 |
L-aspartate oxidase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10631 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008734 |
L-aspartate oxidase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0050660 |
flavin adenine dinucleotide binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0044318 |
L-aspartate:fumarate oxidoreductase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0034628 |
'de novo' NAD biosynthetic process from aspartate |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008734 |
L-aspartate oxidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008734 |
L-aspartate oxidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009435 |
NAD biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0044318 |
L-aspartate:fumarate oxidoreductase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008734 |
L-aspartate oxidase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0019363 |
pyridine nucleotide biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009435 |
NAD biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniPathway:UPA00253 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Flachmann, R et al. (1988) Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB. Eur. J. Biochem. 175 221-8 PubMed GONUTS page
- ↑ 3.0 3.1 Mortarino, M et al. (1996) L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition. Eur. J. Biochem. 239 418-26 PubMed GONUTS page
- ↑ Tedeschi, G et al. (1996) L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: fumarate oxidoreductase activity. Eur. J. Biochem. 239 427-33 PubMed GONUTS page
- ↑ Kerr, TJ & Tritz, GJ (1973) Cross-feeding of Escherichia coli mutants defective in the biosynthesis of nicotinamide adenine dinucleotide. J. Bacteriol. 115 982-6 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
