Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q8XNE2 (NADB_CLOPE)

Last modified November 25, 2008. Version 37. 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: CPE0395
OrganismClostridium perfringens [Complete proteome] [HAMAP]
Taxonomic identifier1502 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length439 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 + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2).

Cofactor

FAD.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.

Subcellular location

CytoplasmBy 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-KW

   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 – 439439L-aspartate oxidase
PRO_0000184383

Regions

Nucleotide binding8 – 2215FAD Potential

Sites

Active site2251 By similarity
Active site2461 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XNE2-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: D89A50E494E5F5C7

FASTA43949,236
        10         20         30         40         50         60 
MKRVADVLIV GSGVAGLYAS LNLREDLEII MVSKKSVNLC NSSLAQGGIA VARGKEDFQS 

        70         80         90        100        110        120 
FIEDTLKAGK YENNIDSVRV LVEESMDNIN KLIDLGANFE KDENGVLFTK EGAHEINRIV 

       130        140        150        160        170        180 
YHKDITGKHV EDILLENVKR RKNIKIIEDC EMVDIYHRGN RCIGALFNKD GQDLSIYAKV 

       190        200        210        220        230        240 
VILATGGIGG LFKKSTNERI ITGDSIGVAI RNNIEIKDLS YIQIHPTAFF SKKSEEKRFL 

       250        260        270        280        290        300 
ISESVRGEGG KLLNCNGERF VDELLPRDIV SKKIYEEMKK TNSNNVFLDV SFMEKSFLQN 

       310        320        330        340        350        360 
RFPNIYNKCL EEGIDISKEP IPVAPAQHYF MGGIKVDLNG KTSMENLYAF GETSCTGVHG 

       370        380        390        400        410        420 
ANRLASNSLL EALVFSRRGA LEINSYIDNL ELIIEERECE DLDKYRLLNR KILIDEICRL 

       430 
RGDIKDELVT CGGECKKSS 

« Hide

References

[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed: 11792842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.

Cross-references

Sequence databases

BA000016 Genomic DNA. Translation: BAB80101.1.
RefSeqNP_561311.1.

3D structure databases

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

Genome annotation databases

GeneID988648.
GenomeReviewsGene locus CPE0395 in contig BA000016_GR.
KEGGcpe:CPE0395.
NMPDRfig|195102.1.peg.458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8XNE2.

Enzyme and pathway databases

BioCycCPER195102:CPE0395-MON.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNADB_CLOPE
AccessionPrimary (citable) accession number: Q8XNE2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: March 1, 2002
Last modified: November 25, 2008
This is version 37 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