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Reviewed, UniProtKB/Swiss-Prot P10902 (NADB_ECOLI)

Last modified February 9, 2010. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    L-aspartate oxidase
      Short name=LASPO
    EC=1.4.3.16
Alternative name(s):
    Quinolinate synthetase B
Gene names
Name: nadB
Synonyms: nicB
Ordered Locus Names: b2574, JW2558
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the oxidation of L-aspartate to iminoaspartate.

Catalytic activity

L-aspartate + O2 = iminosuccinate + H2O2.

Cofactor

FAD.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Post-translational modification

Contains two disulfide bonds.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.

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Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processde novo NAD biosynthetic process from aspartate

Inferred from mutant phenotype. Source: UniProtKB

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from direct assay. Source: UniProtKB

L-aspartate oxidase activity Ref.1

Inferred from direct assay. Source: UniProtKB

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540L-aspartate oxidase
PRO_0000184384

Regions

Nucleotide binding12 – 2615FAD Potential

Sites

Active site2441 By similarity
Active site2631 By similarity

Experimental info

Sequence conflict1601S → T Ref.1
Sequence conflict1601S → T Ref.3
Sequence conflict1601S → T Ref.4
Sequence conflict4851N → D in CAA31217. Ref.1

Secondary structure

1 ............................................................................. 540
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P10902-1 [UniParc].

Last modified August 29, 2003. Version 4.
Checksum: 7B6CFF633BD4AFEC

FASTA54060,337
        10         20         30         40         50         60 
MNTLPEHSCD VLIIGSGAAG LSLALRLADQ HQVIVLSKGP VTEGSTFYAQ GGIAAVFDET 

        70         80         90        100        110        120 
DSIDSHVEDT LIAGAGICDR HAVEFVASNA RSCVQWLIDQ GVLFDTHIQP NGEESYHLTR 

       130        140        150        160        170        180 
EGGHSHRRIL HAADATGREV ETTLVSKALN HPNIRVLERS NAVDLIVSDK IGLPGTRRVV 

       190        200        210        220        230        240 
GAWVWNRNKE TVETCHAKAV VLATGGASKV YQYTTNPDIS SGDGIAMAWR AGCRVANLEF 

       250        260        270        280        290        300 
NQFHPTALYH PQARNFLLTE ALRGEGAYLK RPDGTRFMPD FDERGELAPR DIVARAIDHE 

       310        320        330        340        350        360 
MKRLGADCMF LDISHKPADF IRQHFPMIYE KLLGLGIDLT QEPVPIVPAA HYTCGGVMVD 

       370        380        390        400        410        420 
DHGRTDVEGL YAIGEVSYTG LHGANRMASN SLLECLVYGW SAAEDITRRM PYAHDISTLP 

       430        440        450        460        470        480 
PWDESRVENP DERVVIQHNW HELRLFMWDY VGIVRTTKRL ERALRRITML QQEIDEYYAH 

       490        500        510        520        530        540 
FRVSNNLLEL RNLVQVAELI VRCAMMRKES RGLHFTLDYP ELLTHSGPSI LSPGNHYINR

« Hide

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References

« Hide 'large scale' references
[1]"Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB."
Flachmann R., Kunz N., Seifert J., Guetlich M., Wientjes F.-J., Laeufer A., Gassen H.G.
Eur. J. Biochem. 175:221-228(1988) [PubMed: 2841129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19.
[2]Kunz N.
Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia coli."
Nashimoto H.
(In) Nierhaus K.H. (eds.); The translational apparatus, pp.185-195, Plenum Press, New York (1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[4]Nashimoto H., Saito N.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase."
Seifert J., Kunz N., Flachmann R., Laeufer A., Jany K.-D., Gassen H.G.
Biol. Chem. Hoppe-Seyler 371:239-248(1990) [PubMed: 2187483] [Abstract]
Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
[8]"Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family."
Mattevi A., Tedeschi G., Bacchella L., Coda A., Negri A., Ronchi S.
Structure 7:745-756(1999) [PubMed: 10425677] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIROXECLD. E65035.
RefSeqAP_003160.1.
NP_417069.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CHUX-ray2.20A1-540[»]
1KNPX-ray2.60A1-540[»]
1KNRX-ray2.50A1-540[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-556N.
STRINGP10902.

Proteomic databases

PRIDEP10902.

Genome annotation databases

GeneID947049.
GenomeReviewsGene locus JW2558 in contig AP009048_GR.
Gene locus b2574 in contig U00096_GR.
KEGGecj:JW2558.
eco:b2574.

Organism-specific databases

EchoBASEEB0625.
EcoGeneEG10631. nadB.
CMRSearch...

Phylogenomic databases

eggNOGCOG0029.
HOGENOMHBG293998.
OMAGAYIWNR.

Enzyme and pathway databases

BioCycEcoCyc:L-ASPARTATE-OXID-MONOMER.
ECOL168927:B2574-MONOMER.
MetaCyc:L-ASPARTATE-OXID-MONOMER.

Gene expression databases

GenevestigatorP10902.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
IPR005288. NadB.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
TIGRFAMsTIGR00551. nadB. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameNADB_ECOLI
AccessionPrimary (citable) accession number: P10902
Secondary accession number(s): P78099, Q2MAF6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 29, 2003
Last modified: February 9, 2010
This is version 109 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents