Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8TZL4 (NADB_PYRFU)

Last modified June 16, 2009. Version 47. 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: PF1976
OrganismPyrococcus furiosus [Complete proteome] [HAMAP]
Taxonomic identifier2261 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length464 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 processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

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 – 464464L-aspartate oxidase
PRO_0000184409

Regions

Nucleotide binding4 – 1815FAD Potential

Sites

Active site2101 By similarity
Active site2271 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TZL4-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 413C23A61594A7B3

FASTA46451,710
        10         20         30         40         50         60 
MKVAVVGSGL AGLTAAMSLA KKGIEVTVFG PKPKESNSYL AQAGIAFPIS DGDSIISHVT 

        70         80         90        100        110        120 
DTIRGGKYLN DVTVVWNVIS KSTEAYHFLT SLGIEFTSRE LEGGHSFPRI FTIKNETGKY 

       130        140        150        160        170        180 
IIPVLEKHAK EMGVNFIRKF AEEVAIHNKK IVGVFVEGEL LYFDAVIIAS GGFSGLYKFT 

       190        200        210        220        230        240 
AGNPWNLGIP IGDLALKGVP LRDIEFIQFH PTGFIGKRTY LISEAVRGAG AKLVTGEGER 

       250        260        270        280        290        300 
FVNELETRDV VAREIYRKML EGKGVFLDAT GIEDFKRRFP YIYSFLRREG INPKRDLIPV 

       310        320        330        340        350        360 
TPVAHYTIGG ISVDIFYRTP IKGLYAIGEA ACNGFHGANR LASNSLLECI VSGIEVSRTV 

       370        380        390        400        410        420 
IREKPRGERK EAKYHGYEPG NVDEVRDIMW NHAGIIRREE SLRLGLKKLE KVEADPRVKI 

       430        440        450        460 
LAEAVLKCAL AREESRGAHY REDYPYSREE FRRPSIFRVE NCML 

« Hide

References

[1]"The complete sequence of the Pyrococcus furiosus genome."
Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

AE010291 Genomic DNA. Translation: AAL82100.1.
RefSeqNP_579705.1.

3D structure databases

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

Genome annotation databases

GeneID1469858.
GenomeReviewsGene locus PF1976 in contig AE009950_GR.
KEGGpfu:PF1976.
NMPDRfig|186497.1.peg.2028.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8TZL4.
OMAQ8TZL4. NENCETS.

Enzyme and pathway databases

BRENDA1.4.3.16. 321.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
IPR005288. NadB.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
TIGRFAMsTIGR00551. nadB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADB_PYRFU
AccessionPrimary (citable) accession number: Q8TZL4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: June 1, 2002
Last modified: June 16, 2009
This is version 47 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