Reviewed, UniProtKB/Swiss-Prot Q8XA23 (NADB_ECO57)

Names and origin

Protein names

Recommended name:
    L-aspartate oxidase
      Short name=LASPO
    EC=1.4.3.16
Alternative name(s):
    Quinolinate synthetase B

Gene names

Name:	nadB
Ordered Locus Names:	Z3856, ECs3440

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	540 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-aspartate oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 540	540	L-aspartate oxidase		PRO_0000184385
Regions
	Nucleotide binding	12 – 26	15	FAD Potential
Sites
	Active site	244	1	By similarity
	Active site	263	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8XA23-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: C3E08141513492AC	FASTA	540	60,379
	10 20 30 40 50 60 MNTLLEHSCD 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 NAVDLIISDK IGLPGTRRVV 190 200 210 220 230 240 GAWVWNRNKE KVETCHAKAV VLATGGASKV YQYTTNPDIS SGDGIAMAWR AGCRVANLEF 250 260 270 280 290 300 NQFHPTALYH PQARNFLLTE ALRGEGAYLK RPDGTRFMPD FDVRGELAPR 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 DERVIIQHNW HELRLFMWDY VGIVRTTKRL ERALRRITML QQEIDEYYAH 490 500 510 520 530 540 FRVSNNLLEL RNLVQVAELI VRCAMMRKES RGLHFTLDYP ELLTHSGPSI LSPGNHYINR

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG57690.1. BA000007 Genomic DNA. Translation: BAB36863.1.
PIR	F85903. H91058.
RefSeq	NP_289132.1. NP_311467.1.
3D structure databases
HSSP	HSSP built from PDB template 1CHU based on UniProtKB P10902.
ModBase	Search...
Genome annotation databases
GeneID	914886. 957968.
GenomeReviews	Gene locus Z3856 in contig AE005174_GR. Gene locus ECs3440 in contig BA000007_GR.
KEGG	ece:Z3856. ecs:ECs3440.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8XA23.
OMA	GAYIWNR.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3440-MON.
Family and domain databases
InterPro	IPR003953. FAD_bind2_N. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004112. Fum_Rdtase/Succ_DH_flav_C. IPR005288. NadB. [Graphical view]
Pfam	PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
TIGRFAMs	TIGR00551. nadB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NADB_ECO57

Accession

Primary (citable) accession number: Q8XA23

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	March 1, 2002
Last modified:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)