Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-aspartate oxidase

Gene

nadB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

  • 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 functionOxidoreductase
Biological processPyridine nucleotide biosynthesis
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:L-ASPARTATE-OXID-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

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
STRINGi316385.ECDH10B_2742

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

Gene3Di3.50.50.60, 3 hits
3.90.700.10, 1 hit
InterProiView 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
PANTHERiPTHR42716:SF2 PTHR42716:SF2, 1 hit
PfamiView protein in Pfam
PF00890 FAD_binding_2, 1 hit
PF02910 Succ_DH_flav_C, 1 hit
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
PATRICifig|1411691.4.peg.4160

Similar proteinsi

Entry informationi

Entry nameiNADB_ECOLI
AccessioniPrimary (citable) accession number: P10902
Secondary accession number(s): P78099, Q2MAF6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 29, 2003
Last modified: March 28, 2018
This is version 167 of the entry and version 4 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health