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Reviewed, UniProtKB/Swiss-Prot Q9HNZ0 (NADB_HALSA)

Last modified June 16, 2009. Version 48. 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: VNG_1883G
OrganismHalobacterium salinarium (Halobacterium halobium) [Complete proteome] [HAMAP]
Taxonomic identifier2242 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length509 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 – 509509L-aspartate oxidase
PRO_0000184407

Regions

Nucleotide binding10 – 2415FAD Potential

Sites

Active site2351 By similarity
Active site2521 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HNZ0-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 2932FA3AB128F10E

FASTA50953,226
        10         20         30         40         50         60 
MTDATTTDVL VLGSGIAGCG AALAAAREGA SVLVATKAQQ PADASTDWAQ GGIATTRDDP 

        70         80         90        100        110        120 
ESLKRDILAA GDGEADPEAV DALVGDAAAA VEDVLVDTLG VPFDGEEGFD YAREAAHSAA 

       130        140        150        160        170        180 
RILHVDAATG HHILGPFLRH LDAHENVDML EDAAALDLIT DEGAVTGALL DRNPRTGDRA 

       190        200        210        220        230        240 
ETGVPVFAGS TVLATGGIGD LYRRSTNPRG STGDGVAMAA LAGADVTDAE YVQFHPTAYD 

       250        260        270        280        290        300 
DADPFLVSEA VRGEGALLRN ADGERFMPDY HEDAELAPRD VVARAVAAER DATGEVRLDV 

       310        320        330        340        350        360 
SPLAFAEEFP GLAEACADRG VDWETGIPVA PCEHFLCGGV AVDTVGRTSL DRLFAVGECA 

       370        380        390        400        410        420 
RTGVHGANRL ASTSLLEGLV WGLRAGETAA GDDRAPAPSE PPELRDRDPD LPDGFAAEKF 

       430        440        450        460        470        480 
RRLRRVMDEH VGLRRTGADL QRAQGVLRRL KGEVDSYART RTSRDLYQLR NAAVVGLLIA 

       490        500 
RAAGENPESA GCHHRSDEAA AEEAPDAGH 

« Hide

Cross-references

Sequence databases

AE004437 Genomic DNA. Translation: AAG20080.1.
PIRD84339.
RefSeqNP_280600.1.

3D structure databases

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

Genome annotation databases

GeneID1448381.
GenomeReviewsGene locus VNG_1883G in contig AE004437_GR.
KEGGhal:VNG1883G.
NMPDRfig|64091.1.peg.1623.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9HNZ0.
OMAQ9HNZ0. GAYIWNR.

Enzyme and pathway databases

BioCycHSP64091:VNG1883G-MON.
BRENDA1.4.3.16. 141893.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProtoNetSearch...

Entry information

Entry nameNADB_HALSA
AccessionPrimary (citable) accession number: Q9HNZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: March 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

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