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Protein

L-aspartate oxidase

Gene

nadB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of L-aspartate to iminoaspartate.

Catalytic activityi

L-aspartate + O2 = iminosuccinate + H2O2.

Cofactori

Pathwayi: NAD(+) biosynthesis

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:
  1. L-aspartate oxidase (nadB)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
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 keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei244By similarity1
Active sitei263By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 26FADSequence analysisAdd BLAST15

GO - Molecular functioni

  • electron carrier activity Source: GO_Central
  • 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
  • anaerobic respiration Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:L-ASPARTATE-OXID-MONOMER.
ECOL316407:JW2558-MONOMER.
MetaCyc:L-ASPARTATE-OXID-MONOMER.
BRENDAi1.4.3.16. 2026.
UniPathwayiUPA00253; 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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10631. nadB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001843841 – 540L-aspartate oxidaseAdd BLAST540

Post-translational modificationi

Contains two disulfide bonds.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP10902.
PRIDEiP10902.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4263282. 13 interactors.
DIPiDIP-556N.
IntActiP10902. 7 interactors.
STRINGi511145.b2574.

Structurei

Secondary structure

1540
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Beta strandi10 – 14Combined sources5
Helixi18 – 27Combined sources10
Turni28 – 30Combined sources3
Beta strandi33 – 36Combined sources4
Beta strandi38 – 40Combined sources3
Helixi45 – 48Combined sources4
Helixi60 – 73Combined sources14
Turni74 – 76Combined sources3
Helixi80 – 99Combined sources20
Beta strandi110 – 113Combined sources4
Helixi145 – 150Combined sources6
Beta strandi154 – 157Combined sources4
Beta strandi159 – 167Combined sources9
Helixi168 – 170Combined sources3
Beta strandi178 – 186Combined sources9
Turni187 – 190Combined sources4
Beta strandi191 – 196Combined sources6
Beta strandi198 – 202Combined sources5
Helixi208 – 210Combined sources3
Beta strandi211 – 215Combined sources5
Helixi217 – 219Combined sources3
Helixi223 – 230Combined sources8
Beta strandi241 – 248Combined sources8
Helixi260 – 264Combined sources5
Beta strandi268 – 270Combined sources3
Helixi278 – 280Combined sources3
Helixi285 – 287Combined sources3
Helixi290 – 304Combined sources15
Beta strandi309 – 312Combined sources4
Helixi319 – 324Combined sources6
Helixi326 – 333Combined sources8
Turni334 – 336Combined sources3
Turni339 – 341Combined sources3
Beta strandi344 – 354Combined sources11
Beta strandi356 – 358Combined sources3
Beta strandi366 – 368Combined sources3
Beta strandi370 – 372Combined sources3
Helixi374 – 376Combined sources3
Beta strandi380 – 382Combined sources3
Helixi390 – 409Combined sources20
Helixi410 – 412Combined sources3
Helixi430 – 450Combined sources21
Beta strandi451 – 455Combined sources5
Helixi457 – 478Combined sources22
Helixi485 – 506Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CHUX-ray2.20A1-540[»]
1KNPX-ray2.60A1-540[»]
1KNRX-ray2.50A1-540[»]
ProteinModelPortaliP10902.
SMRiP10902.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10902.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108IYU. Bacteria.
COG0029. LUCA.
HOGENOMiHOG000160476.
InParanoidiP10902.
KOiK00278.
OMAiHCVQWLI.
PhylomeDBiP10902.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR005288. NadB.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR00551. nadB. 1 hit.

Sequencei

Sequence statusi: Complete.

P10902-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:540
Mass (Da):60,337
Last modified:August 29, 2003 - v4
Checksum:i7B6CFF633BD4AFEC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti160S → T (PubMed:2841129).Curated1
Sequence conflicti160S → T (Ref. 3) Curated1
Sequence conflicti160S → T (Ref. 4) Curated1
Sequence conflicti485N → D in CAA31217 (PubMed:2841129).Curated1

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.
PIRiE65035. OXECLD.
RefSeqiNP_417069.1. NC_000913.3.
WP_001094491.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75627; AAC75627; b2574.
BAE76750; BAE76750; BAE76750.
GeneIDi947049.
KEGGiecj:JW2558.
eco:b2574.
PATRICi32120547. VBIEscCol129921_2676.

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.
PIRiE65035. OXECLD.
RefSeqiNP_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 entryMethodResolution (Å)ChainPositionsPDBsum
1CHUX-ray2.20A1-540[»]
1KNPX-ray2.60A1-540[»]
1KNRX-ray2.50A1-540[»]
ProteinModelPortaliP10902.
SMRiP10902.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263282. 13 interactors.
DIPiDIP-556N.
IntActiP10902. 7 interactors.
STRINGi511145.b2574.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PaxDbiP10902.
PRIDEiP10902.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75627; AAC75627; b2574.
BAE76750; BAE76750; BAE76750.
GeneIDi947049.
KEGGiecj:JW2558.
eco:b2574.
PATRICi32120547. VBIEscCol129921_2676.

Organism-specific databases

EchoBASEiEB0625.
EcoGeneiEG10631. nadB.

Phylogenomic databases

eggNOGiENOG4108IYU. Bacteria.
COG0029. LUCA.
HOGENOMiHOG000160476.
InParanoidiP10902.
KOiK00278.
OMAiHCVQWLI.
PhylomeDBiP10902.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00326.
BioCyciEcoCyc:L-ASPARTATE-OXID-MONOMER.
ECOL316407:JW2558-MONOMER.
MetaCyc:L-ASPARTATE-OXID-MONOMER.
BRENDAi1.4.3.16. 2026.

Miscellaneous databases

EvolutionaryTraceiP10902.
PROiP10902.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR005288. NadB.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR00551. nadB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNADB_ECOLI
AccessioniPrimary (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: November 30, 2016
This is version 158 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.