[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19. PubMed=2841129 [NCBI, ExPASy, EBI, Israel, Japan] Flachmann R., Kunz N., Seifert J., Guetlich M., Wientjes F.-J., Laeufer A., Gassen H.G.; "Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB."; Eur. J. Biochem. 175:221-228(1988).
[2]	SEQUENCE REVISION. Kunz N.; Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; Nashimoto H.; "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia coli."; (In) Nierhaus K.H. (eds.); The translational apparatus, pp.185-195, Plenum Press, New York (1993).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; Nashimoto H., Saito N.; Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[7]	CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE. PubMed=2187483 [NCBI, ExPASy, EBI, Israel, Japan] Seifert J., Kunz N., Flachmann R., Laeufer A., Jany K.-D., Gassen H.G.; "Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase."; Biol. Chem. Hoppe-Seyler 371:239-248(1990).
[8]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1016/S0969-2126(99)80099-9; PubMed=10425677 [NCBI, ExPASy, EBI, Israel, Japan] Mattevi A., Tedeschi G., Bacchella L., Coda A., Negri A., Ronchi S.; "Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family."; Structure 7:745-756(1999).

Comments

FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate.
CATALYTIC ACTIVITY: L-aspartate + H₂O + O₂ = oxaloacetate + NH₃ + H₂O₂.
COFACTOR: FAD.
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1 .
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
PTM: Contains two disulfide bonds.
SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X12714; CAA31217.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D13169; BAA02446.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D64044; BAA10921.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75627.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76750.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E65035; OXECLD.

RefSeq

AP_003160.1; -.
NP_417069.1; -.

3D structure databases

PDB

1CHU; X-ray; 2.20 A; A=1-540.	[ExPASy / RCSB / EBI]
1KNP; X-ray; 2.60 A; A=1-540.	[ExPASy / RCSB / EBI]
1KNR; X-ray; 2.50 A; A=1-540.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1CHU; -.
1KNP; -.
1KNR; -.

ModBase

P10902.

Protein-protein interaction databases

DIP

DIP:556N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:L-ASPARTATE-OXID-MON; -.
MetaCyc:L-ASPARTATE-OXID-MON; -.

Organism-specific databases

EchoBASE

EB0625; -.

EcoGene

EG10631; nadB.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008734;	Molecular function: L-aspartate oxidase activity (inferred from electronic annotation from InterPro).
GO:0009435;	Biological process: NAD biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003953; FAD_bind2_N.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
IPR005288; NadB.
IPR001100; Pyr_nuc-diS_OxRdtase.
Graphical view of domain structure.

Pfam

PF00890; FAD_binding_2; 1.
PF02910; Succ_DH_flav_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.

TIGRFAMs

TIGR00551; nadB; 1.

Genome annotation databases

GeneID

947049; -.

GenomeReviews

AP009048_GR; JW2558.
U00096_GR; b2574.

KEGG

ecj:JW2558; -.
eco:b2574; -.

Phylogenomic databases

HOGENOM

P10902; -.

Genome annotation databases

CMR

P10902; b2574.

Other

ProtoNet

P10902.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Pyridine nucleotide biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 540`	`540`	`L-aspartate oxidase.`	`PRO_0000184384`
`NP_BIND`	`12 26`	`15`	`FAD (Potential).`
`ACT_SITE`	`244 244`		`By similarity.`
`ACT_SITE`	`263 263`		`By similarity.`
`CONFLICT`	`160 160`		`S -> T (in Ref. 1, 3 and 4).`
`CONFLICT`	`485 485`		`N -> D (in Ref. 1; CAA31217).`
`STRAND`	`6 8`	`3`
`STRAND`	`10 14`	`5`
`HELIX`	`18 27`	`10`
`TURN`	`28 30`	`3`
`STRAND`	`33 36`	`4`
`HELIX`	`60 73`	`14`
`TURN`	`74 76`	`3`
`HELIX`	`80 99`	`20`
`HELIX`	`145 150`	`6`
`STRAND`	`154 157`	`4`
`STRAND`	`159 167`	`9`
`HELIX`	`168 170`	`3`
`STRAND`	`178 186`	`9`
`TURN`	`187 190`	`4`
`STRAND`	`191 196`	`6`
`STRAND`	`198 202`	`5`
`HELIX`	`208 210`	`3`
`STRAND`	`211 215`	`5`
`HELIX`	`217 219`	`3`
`HELIX`	`223 230`	`8`
`STRAND`	`241 248`	`8`
`HELIX`	`260 264`	`5`
`STRAND`	`268 270`	`3`
`HELIX`	`278 280`	`3`
`HELIX`	`285 287`	`3`
`HELIX`	`290 304`	`15`
`STRAND`	`309 312`	`4`
`HELIX`	`319 324`	`6`
`HELIX`	`326 333`	`8`
`TURN`	`334 336`	`3`
`TURN`	`339 341`	`3`
`STRAND`	`344 354`	`11`
`STRAND`	`356 358`	`3`
`STRAND`	`366 368`	`3`
`STRAND`	`370 372`	`3`
`HELIX`	`374 376`	`3`
`STRAND`	`380 382`	`3`
`HELIX`	`390 409`	`20`
`HELIX`	`430 450`	`21`
`STRAND`	`451 455`	`5`
`HELIX`	`457 478`	`22`
`HELIX`	`485 506`	`22`

Sequence information

Length: 540 AA [This is the length of the unprocessed precursor]

Molecular weight: 60337 Da [This is the MW of the unprocessed precursor]

CRC64: 7B6CFF633BD4AFEC [This is a checksum on the sequence]

        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

P10902 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools