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Reviewed, UniProtKB/Swiss-Prot Q9PC57 (NADB_XYLFA)

Last modified November 3, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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
Ordered Locus Names: XF_1924
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pyridine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512L-aspartate oxidase
PRO_0000184404

Regions

Nucleotide binding13 – 2715FAD Potential

Sites

Active site2331 By similarity
Active site2521 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PC57-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: DD2C9C15FC7A61C6

FASTA51253,965
        10         20         30         40         50         60 
MAEIVDCFAD RPIIVGSGLA GLIAALTMSP EPSVLVTRSA LGAETSSAWA QGGMSVSLSP 

        70         80         90        100        110        120 
DDNPSLHLAD TLAAGDGLCD AVAAESIILE ALDAFHVLQH FGIHFDQDSN GHLALGLEAA 

       130        140        150        160        170        180 
HSRRRIVHVG GDRSGTAIVQ ALTACVLNDP SITVLEGLEA RHILMADNVV CGLLLANPTS 

       190        200        210        220        230        240 
EIVLPSSRIL LATGGIGGLY DATTNPVSNF GQGIAMAARA GAVLADMEFV QFHPTALHCH 

       250        260        270        280        290        300 
NRPLALVSEA VRGEGAVLIN ERGERFMADI PGAELAARNI VAQAISAEIT RGGQVFLDAR 

       310        320        330        340        350        360 
QALGARFSTR FPTITALCHK VGIDPVHMPI PVCPAAHYHM GGIAIDHQGR SSIPGLWVAG 

       370        380        390        400        410        420 
EAASTGLHGA NRLASNSLLE AVVMGTRAAR DITFHNTPHP LGTIPITPKK PDTTLIRPIV 

       430        440        450        460        470        480 
SQCLGVLRHA ADMHRAIAAL LPFVEGEEES SDPAIVALLI AIFAYLRTES RGAHARTDFP 

       490        500        510 
LKHDTTQRRH MTLEDVLEIA HSCVAQRKEK IS 

« Hide

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. expand/collapse author list , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
Nature 406:151-159(2000) [PubMed: 10910347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.

Cross-references

Sequence databases

AE003849 Genomic DNA. Translation: AAF84730.1.
PIRA82621.
RefSeqNP_299210.1.

3D structure databases

HSSPHSSP built from PDB template 1CHU based on UniProtKB P10902.
ModBaseSearch...

Genome annotation databases

GeneID1127475.
GenomeReviewsGene locus XF_1924 in contig AE003849_GR.
KEGGxfa:XF1924.
NMPDRfig|160492.1.peg.1917.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9PC57.
OMAGAYIWNR.

Enzyme and pathway databases

BioCycXFAS160492:XF1924-MON.
BRENDA1.4.3.16. 278708.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNADB_XYLFA
AccessionPrimary (citable) accession number: Q9PC57
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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