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Reviewed, UniProtKB/Swiss-Prot Q972D2 (NADB_SULTO)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: ST1196
OrganismSulfolobus tokodaii [Complete proteome] [HAMAP]
Taxonomic identifier111955 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

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 term3D-structure
Complete 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 – 472472L-aspartate oxidase
PRO_0000184412

Regions

Nucleotide binding3 – 1715FAD Potential

Sites

Active site2121 By similarity
Active site2301 By similarity

Secondary structure

............................................................................... 472
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q972D2-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 9B31FAC6FE79801F

FASTA47252,582
        10         20         30         40         50         60 
MIYIIGSGIA GLSAGVALRR AGKKVTLISK RIDGGSTPIA KGGVAASVGS DDSPELHAQD 

        70         80         90        100        110        120 
TIRVGDGLCD VKTVNYVTSE AKNVIETFES WGFEFEEDLR LEGGHTKRRV LHRTDETGRE 

       130        140        150        160        170        180 
IFNFLLKLAR EEGIPIIEDR LVEIRVKDGK VTGFVTEKRG LVEDVDKLVL ATGGYSYLYE 

       190        200        210        220        230        240 
YSSTQSTNIG DGMAIAFKAG TILADMEFVQ FHPTVTSLDG EVFLLTETLR GEGAQIINEN 

       250        260        270        280        290        300 
GERFLFNYDK RGELAPRDIL SRAIYIEMLK GHKVFIDLSK IEDFERKFPV VAKYLARHGH 

       310        320        330        340        350        360 
NYKVKIPIFP AAHFVDGGIR VNIRGESNIV NLYAIGEVSD SGLHGANRLA SNSLLEGLVF 

       370        380        390        400        410        420 
GINLPRYVDS SWEGISTDDG IVHSVRISGN KTLSLKEIRR INWENVGIIR NEEKLVKAIN 

       430        440        450        460        470 
TYSSSTQNEA IISYLTALAA EIRKESRGNH FREDYPYKDP NWEKRIYFKL VV 

« Hide

Cross-references

Sequence databases

BA000023 Genomic DNA. Translation: BAB66237.1.
RefSeqNP_377128.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2E5VX-ray2.09A/B1-472[»]
ModBaseSearch...

Genome annotation databases

GeneID1459193.
GenomeReviewsGene locus ST1196 in contig BA000023_GR.
KEGGsto:ST1196.
NMPDRfig|273063.1.peg.1296.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ972D2.
OMAQ972D2. HYSPELY.

Enzyme and pathway databases

BRENDA1.4.3.16. 261167.

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_SULTO
AccessionPrimary (citable) accession number: Q972D2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: December 1, 2001
Last modified: June 16, 2009
This is version 48 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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