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Q8ZD80 (NADB_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-aspartate oxidase

Short name=LASPO
EC=1.4.3.16
Alternative name(s):
Quinolinate synthase B
Gene names
Name:nadB
Ordered Locus Names:YPO2710, y1289, YP_2514
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence caution

The sequence AAM84863.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAS62712.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAL21329.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-aspartate oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

L-aspartate:fumarate oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533L-aspartate oxidase
PRO_0000184406

Regions

Nucleotide binding12 – 2615FAD Potential

Sites

Active site2441 By similarity
Active site2631 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZD80 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 909E8BFEB15BD2BD

FASTA53359,294
        10         20         30         40         50         60 
MQSSSEHISD VLIIGSGAAG LSLALRLAPH CKVTVLSKGP LNEGATFYAQ GGIAAVFDET 

        70         80         90        100        110        120 
DSISSHVDDT LIAGAGLCDK EAVEFIASNA RSCVQWLIDQ GVLFDTETSA NGEERYHLTR 

       130        140        150        160        170        180 
EGGHSHRRIL HTADATGKEV ETTLVGKASN HPNISVKERC NAVDLITSNK IGLAGTKRVV 

       190        200        210        220        230        240 
GAYVWNRELE KVETFRAKAV VLATGGAAKV YQYTTNPDIS SGDGIAMAWR AGCRVANLEF 

       250        260        270        280        290        300 
NQFHPTCLFH PQARNFLLTE ALRGEGAYLK RPDGSRFMLD FDPRGELAPR DIVARAIDHE 

       310        320        330        340        350        360 
MKRLGADCMY LDISHKPTDF VMQHFPMIYE KLLSLGIDLT KEAIPIVPAA HYTCGGVMVD 

       370        380        390        400        410        420 
QHGRTDLDGL YAIGEVSYTG LHGANRMASN SLLECLVYGW SAAEDILTRL PTAKLAKHLP 

       430        440        450        460        470        480 
DWDESRVDNS DERVVIQHNW HELRLFMWDY VGIVRTTKRL ERALRRINTL QQEIDEYYAN 

       490        500        510        520        530 
FRISNNLLEL RNLVQVAELI VRCAMERKES RGLHYTLDYP DQIENPQPTI LHP 

« Hide

References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL21329.1. Different initiation.
AE009952 Genomic DNA. Translation: AAM84863.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS62712.1. Different initiation.
PIRAF0330.
RefSeqNP_668612.1. NC_004088.1.
NP_993835.1. NC_005810.1.
YP_002347657.1. NC_003143.1.

3D structure databases

ProteinModelPortalQ8ZD80.
SMRQ8ZD80. Positions 6-533.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING214092.YPO2710.

Proteomic databases

PRIDEQ8ZD80.

Protocols and materials databases

DNASU1146236.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM84863; AAM84863; y1289.
AAS62712; AAS62712; YP_2514.
GeneID1146236.
1175540.
2764388.
KEGGype:YPO2710.
ypk:y1289.
ypm:YP_2514.

Phylogenomic databases

eggNOGCOG0029.
HOGENOMHOG000160476.
KOK00278.
OMACGDGIAM.
OrthoDBEOG696BWH.
ProtClustDBPRK09077.

Enzyme and pathway databases

BioCycYPES214092:GKDD-2677-MONOMER.
UniPathwayUPA00253; UER00326.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR005288. NadB.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR00551. nadB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADB_YERPE
AccessionPrimary (citable) accession number: Q8ZD80
Secondary accession number(s): Q0WDI1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: August 30, 2002
Last modified: November 13, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways