L-aspartate oxidase - Escherichia coli (strain K12)

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P10902 (NADB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 134. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
L-aspartate oxidase
Short name=LASPO
EC=1.4.3.16

Alternative name(s):
Quinolinate synthase B

Gene names

Name:	nadB
Synonyms:	nicB
Ordered Locus Names:	b2574, JW2558

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	540 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	de novo NAD biosynthetic process from aspartate Inferred from mutant phenotype PubMed 4353874. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-aspartate oxidase activity Inferred from direct assay PubMed 8706749. Source: EcoCyc L-aspartate:fumarate oxidoreductase activity Inferred from direct assay PubMed 8706750. Source: EcoCyc flavin adenine dinucleotide binding Inferred from direct assay PubMed 8706749. Source: EcoCyc
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_0000184384

Regions

Nucleotide binding

12 – 26

FAD Potential

Sites

Active site

244

By similarity

Active site

263

By similarity

Experimental info

Sequence conflict

160

S → T Ref.1

Sequence conflict

160

S → T Ref.3

Sequence conflict

160

S → T Ref.4

Sequence conflict

485

N → D in CAA31217. Ref.1

Secondary structure

540

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P10902 [UniParc].

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

540

60,337

        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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

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.

PIR

OXECLD. E65035.

RefSeq

NP_417069.1. NC_000913.2.
YP_490802.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CHU	X-ray	2.20	A	1-540	[»]
1KNP	X-ray	2.60	A	1-540	[»]
1KNR	X-ray	2.50	A	1-540	[»]

ProteinModelPortal

P10902.

SMR

P10902. Positions 5-533.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-556N.

IntAct

P10902. 6 interactions.

STRING

511145.b2574.

Proteomic databases

PaxDb

P10902.

PRIDE

P10902.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75627; AAC75627; b2574.
BAE76750; BAE76750; BAE76750.

GeneID

12934288.
947049.

KEGG

ecj:Y75_p2527.
eco:b2574.

PATRIC

32120547. VBIEscCol129921_2676.

Organism-specific databases

EchoBASE

EB0625.

EcoGene

EG10631. nadB.

Phylogenomic databases

eggNOG

COG0029.

HOGENOM

HOG000160476.

K00278.

OMA

GERCLGA.

ProtClustDB

PRK09077.

Enzyme and pathway databases

BioCyc

EcoCyc:L-ASPARTATE-OXID-MONOMER.
ECOL316407:JW2558-MONOMER.
MetaCyc:L-ASPARTATE-OXID-MONOMER.

UniPathway

UPA00253; UER00326.

Gene expression databases

Genevestigator

P10902.

Family and domain databases

Gene3D

1.20.58.100. 1 hit.

InterPro

IPR003953. FAD_bind_dom.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR005288. NadB.
[Graphical view]

Pfam

PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

SUPFAM

SSF46977. Succ_DH_flav_C. 1 hit.

TIGRFAMs

TIGR00551. nadB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P10902.

Entry information

Entry name

NADB_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 134 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents