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Reviewed, UniProtKB/Swiss-Prot Q929Z2 (NADB_LISIN)

Last modified November 3, 2009. Version 45. 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: lin2131
OrganismListeria innocua [Complete proteome] [HAMAP]
Taxonomic identifier1642 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

Protein attributes

Sequence length484 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 – 484484L-aspartate oxidase
PRO_0000184386

Regions

Nucleotide binding7 – 2115FAD Potential

Sites

Active site2241 By similarity
Active site2431 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q929Z2-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 548B9BA10EBA4261

FASTA48453,411
        10         20         30         40         50         60 
MTKERVIIIG SGIAGCTAAL RLMQDYDVTI ITKGHKEQSN SMLAQGGVAA AISKSDTPKK 

        70         80         90        100        110        120 
HFSDTFQAGC FHNKVRAVNQ LVTCGPIVIQ KLINEGMTFD EKDGELSLGL EGAHQLPRIL 

       130        140        150        160        170        180 
HSGGDQTGKF LTTFLQEKLT KVNWQEQKMA IEIIKHDGRA IGVHCLDKEN QLHTYYGEHI 

       190        200        210        220        230        240 
ILASGGLGQL FPVTTNAATI SGDGLALAYR ADATLSDMEF IQFHPTLLFL NGRCHGLISE 

       250        260        270        280        290        300 
AVRGEGATLI RADGSAIMET VHPLADLAPR DVVAATLFEE IERGNQVFLD ITKVAHFEKR 

       310        320        330        340        350        360 
FPAITTSLDE HQVPFRETKR IPVHPGAHFL MGGVRTDLNG KTNIPHLYAI GEVANTGVHG 

       370        380        390        400        410        420 
ANRLASNSLL ETLVFGEKVA EYIHTQKNNR IIAPENPPTY QTTMPHLPEK HILQEKIWET 

       430        440        450        460        470        480 
LGITRKPEKI TEFLHWLETF DYANHTRETA EISHMIITSK LIAESALKRT ESLGAHRILK 


GVTK 

« Hide

Cross-references

Sequence databases

AL596171 Genomic DNA. Translation: CAC97361.1.
PIRAI1698.
RefSeqNP_471465.1.

3D structure databases

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

Genome annotation databases

GeneID1130858.
GenomeReviewsGene locus lin2131 in contig AL592022_GR.
KEGGlin:lin2131.
NMPDRfig|272626.1.peg.2118.

Organism-specific databases

ListiListLIN02131.
CMRSearch...

Phylogenomic databases

HOGENOMQ929Z2.
OMAGAYIWNR.

Enzyme and pathway databases

BioCycLINN272626:LIN2131-MON.
BRENDA1.4.3.16. 270396.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR005288. NadB.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00551. nadB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADB_LISIN
AccessionPrimary (citable) accession number: Q929Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: December 1, 2001
Last modified: November 3, 2009
This is version 45 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