UniProtKB - P10902 (NADB_ECOLI)
Protein
L-aspartate oxidase
Gene
nadB
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the oxidation of L-aspartate to iminoaspartate.
Catalytic activityi
- EC:1.4.3.16
Cofactori
: NAD(+) biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes iminoaspartate from L-aspartate (oxidase route).Proteins known to be involved in this subpathway in this organism are:
- L-aspartate oxidase (nadB), L-aspartate oxidase (nadB)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes iminoaspartate from L-aspartate (oxidase route), the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 244 | By similarity | 1 | |
Active sitei | 263 | By similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 12 – 26 | FADSequence analysisAdd BLAST | 15 |
GO - Molecular functioni
- flavin adenine dinucleotide binding Source: EcoCyc
- L-aspartate:fumarate oxidoreductase activity Source: EcoCyc
- L-aspartate oxidase activity Source: EcoCyc
GO - Biological processi
- 'de novo' NAD biosynthetic process from aspartate Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Pyridine nucleotide biosynthesis |
Ligand | FAD, Flavoprotein |
Enzyme and pathway databases
BioCyci | EcoCyc:L-ASPARTATE-OXID-MONOMER MetaCyc:L-ASPARTATE-OXID-MONOMER |
BRENDAi | 1.4.3.16, 2026 |
UniPathwayi | UPA00253;UER00326 |
Names & Taxonomyi
Protein namesi | Recommended name: L-aspartate oxidase (EC:1.4.3.16)Short name: LASPO Alternative name(s): Quinolinate synthase B |
Gene namesi | Name:nadB Synonyms:nicB Ordered Locus Names:b2574, JW2558 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
GO - Cellular componenti
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000184384 | 1 – 540 | L-aspartate oxidaseAdd BLAST | 540 |
Post-translational modificationi
Contains two disulfide bonds.
Keywords - PTMi
Disulfide bondProteomic databases
PaxDbi | P10902 |
PRIDEi | P10902 |
Interactioni
Subunit structurei
Monomer.
Protein-protein interaction databases
BioGRIDi | 4263282, 13 interactors 851387, 1 interactor |
DIPi | DIP-556N |
IntActi | P10902, 7 interactors |
STRINGi | 511145.b2574 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P10902 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P10902 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0029, Bacteria |
HOGENOMi | CLU_014312_3_0_6 |
InParanoidi | P10902 |
PhylomeDBi | P10902 |
Family and domain databases
Gene3Di | 3.50.50.60, 2 hits 3.90.700.10, 1 hit |
InterProi | View protein in InterPro IPR003953, FAD-binding_2 IPR036188, FAD/NAD-bd_sf IPR037099, Fum_R/Succ_DH_flav-like_C_sf IPR015939, Fum_Rdtase/Succ_DH_flav-like_C IPR005288, NadB IPR027477, Succ_DH/fumarate_Rdtase_cat_sf |
PANTHERi | PTHR42716, PTHR42716, 1 hit |
Pfami | View protein in Pfam PF00890, FAD_binding_2, 1 hit PF02910, Succ_DH_flav_C, 1 hit |
SUPFAMi | SSF46977, SSF46977, 1 hit SSF51905, SSF51905, 1 hit SSF56425, SSF56425, 1 hit |
TIGRFAMsi | TIGR00551, nadB, 1 hit |
i Sequence
Sequence statusi: Complete.
P10902-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNTLPEHSCD VLIIGSGAAG LSLALRLADQ HQVIVLSKGP VTEGSTFYAQ
60 70 80 90 100
GGIAAVFDET DSIDSHVEDT LIAGAGICDR HAVEFVASNA RSCVQWLIDQ
110 120 130 140 150
GVLFDTHIQP NGEESYHLTR EGGHSHRRIL HAADATGREV ETTLVSKALN
160 170 180 190 200
HPNIRVLERS NAVDLIVSDK IGLPGTRRVV GAWVWNRNKE TVETCHAKAV
210 220 230 240 250
VLATGGASKV YQYTTNPDIS SGDGIAMAWR AGCRVANLEF NQFHPTALYH
260 270 280 290 300
PQARNFLLTE ALRGEGAYLK RPDGTRFMPD FDERGELAPR DIVARAIDHE
310 320 330 340 350
MKRLGADCMF LDISHKPADF IRQHFPMIYE KLLGLGIDLT QEPVPIVPAA
360 370 380 390 400
HYTCGGVMVD DHGRTDVEGL YAIGEVSYTG LHGANRMASN SLLECLVYGW
410 420 430 440 450
SAAEDITRRM PYAHDISTLP PWDESRVENP DERVVIQHNW HELRLFMWDY
460 470 480 490 500
VGIVRTTKRL ERALRRITML QQEIDEYYAH FRVSNNLLEL RNLVQVAELI
510 520 530 540
VRCAMMRKES RGLHFTLDYP ELLTHSGPSI LSPGNHYINR
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 160 | S → T (PubMed:2841129).Curated | 1 | |
Sequence conflicti | 160 | S → T (Ref. 3) Curated | 1 | |
Sequence conflicti | 160 | S → T (Ref. 4) Curated | 1 | |
Sequence conflicti | 485 | N → D in CAA31217 (PubMed:2841129).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X12714 Genomic DNA Translation: CAA31217.1 D13169 Genomic DNA Translation: BAA02446.1 D64044 Genomic DNA Translation: BAA10921.1 U00096 Genomic DNA Translation: AAC75627.1 AP009048 Genomic DNA Translation: BAE76750.1 |
PIRi | E65035, OXECLD |
RefSeqi | NP_417069.1, NC_000913.3 WP_001094491.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC75627; AAC75627; b2574 BAE76750; BAE76750; BAE76750 |
GeneIDi | 947049 |
KEGGi | ecj:JW2558 eco:b2574 |
PATRICi | fig|1411691.4.peg.4160 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X12714 Genomic DNA Translation: CAA31217.1 D13169 Genomic DNA Translation: BAA02446.1 D64044 Genomic DNA Translation: BAA10921.1 U00096 Genomic DNA Translation: AAC75627.1 AP009048 Genomic DNA Translation: BAE76750.1 |
PIRi | E65035, OXECLD |
RefSeqi | NP_417069.1, NC_000913.3 WP_001094491.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1CHU | X-ray | 2.20 | A | 1-540 | [»] | |
1KNP | X-ray | 2.60 | A | 1-540 | [»] | |
1KNR | X-ray | 2.50 | A | 1-540 | [»] | |
SMRi | P10902 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263282, 13 interactors 851387, 1 interactor |
DIPi | DIP-556N |
IntActi | P10902, 7 interactors |
STRINGi | 511145.b2574 |
Chemistry databases
DrugBanki | DB03147, Flavin adenine dinucleotide |
Proteomic databases
PaxDbi | P10902 |
PRIDEi | P10902 |
Genome annotation databases
EnsemblBacteriai | AAC75627; AAC75627; b2574 BAE76750; BAE76750; BAE76750 |
GeneIDi | 947049 |
KEGGi | ecj:JW2558 eco:b2574 |
PATRICi | fig|1411691.4.peg.4160 |
Organism-specific databases
EchoBASEi | EB0625 |
Phylogenomic databases
eggNOGi | COG0029, Bacteria |
HOGENOMi | CLU_014312_3_0_6 |
InParanoidi | P10902 |
PhylomeDBi | P10902 |
Enzyme and pathway databases
UniPathwayi | UPA00253;UER00326 |
BioCyci | EcoCyc:L-ASPARTATE-OXID-MONOMER MetaCyc:L-ASPARTATE-OXID-MONOMER |
BRENDAi | 1.4.3.16, 2026 |
Miscellaneous databases
EvolutionaryTracei | P10902 |
PROi | PR:P10902 |
Family and domain databases
Gene3Di | 3.50.50.60, 2 hits 3.90.700.10, 1 hit |
InterProi | View protein in InterPro IPR003953, FAD-binding_2 IPR036188, FAD/NAD-bd_sf IPR037099, Fum_R/Succ_DH_flav-like_C_sf IPR015939, Fum_Rdtase/Succ_DH_flav-like_C IPR005288, NadB IPR027477, Succ_DH/fumarate_Rdtase_cat_sf |
PANTHERi | PTHR42716, PTHR42716, 1 hit |
Pfami | View protein in Pfam PF00890, FAD_binding_2, 1 hit PF02910, Succ_DH_flav_C, 1 hit |
SUPFAMi | SSF46977, SSF46977, 1 hit SSF51905, SSF51905, 1 hit SSF56425, SSF56425, 1 hit |
TIGRFAMsi | TIGR00551, nadB, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NADB_ECOLI | |
Accessioni | P10902Primary (citable) accession number: P10902 Secondary accession number(s): P78099, Q2MAF6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | August 29, 2003 | |
Last modified: | December 2, 2020 | |
This is version 180 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families