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Reviewed, UniProtKB/Swiss-Prot Q9KDJ5 (NADB_BACHD)

Last modified June 16, 2009. Version 46. 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

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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: BH1218
OrganismBacillus halodurans [Complete proteome] [HAMAP]
Taxonomic identifier86665 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509L-aspartate oxidase
PRO_0000184379

Regions

Nucleotide binding8 – 2215FAD Potential

Sites

Active site2221 By similarity
Active site2421 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9KDJ5-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: FE8DA59633AA0421

FASTA50956,327
        10         20         30         40         50         60 
MRCDGEVIIV GSGIAAMMSA YLLRKSFHVI MITKSDVFAS NSFLAQGGIA APIAEGDDWQ 

        70         80         90        100        110        120 
AHTADTWKAG AAHGDETSIE MMTKHAVNMI ELLDDLGVSF DREESGGYSL GLEGAHGTRR 

       130        140        150        160        170        180 
IVHVNGAETG KAVMRALWKA IKNEITLLDR TCVYRFIKNK DEIIGVETDQ GSLFAPVTIV 

       190        200        210        220        230        240 
ATGGCGQMYS VTSNGKEATG DGIALAYRSG AAISDVEFIQ FHPTVYTGNE KEKGLLISEA 

       250        260        270        280        290        300 
VRGEGGQLIT SAGERLQSLK SRDVVSREIF RQEREGHTVH LDLTGISDFE RKFPALYKGF 

       310        320        330        340        350        360 
NKSDRRTLKP RVTPGAHFLN GGISVDAWGQ TSLSRLYAVG EVACTGVHGA NRLASNSLLE 

       370        380        390        400        410        420 
GLVFAHQAAT HIQQTFQPLT AGLFVERDKA EPRSFKLPTR EDLQKKMMRY VGIERHARSL 

       430        440        450        460        470        480 
WYMNNWFQPF LDTAHYNGPW PERDMFEQAN MTLLASLITR SAAIRTESRG GHFRADYPNG 

       490        500 
LDKFQQLIIE WQNGAHMKRQ RPTIKELSR

« Hide

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References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

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Cross-references

Sequence databases

BA000004 Genomic DNA. Translation: BAB04937.1.
PIRB83802.
RefSeqNP_242084.1.

3D structure databases

HSSPHSSP built from PDB template 1D4D based on UniProtKB P83223.
ModBaseSearch...

Genome annotation databases

GeneID894195.
GenomeReviewsGene locus BH1218 in contig BA000004_GR.
KEGGbha:BH1218.
NMPDRfig|272558.1.peg.1218.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9KDJ5.
OMAQ9KDJ5. GAYIWNR.

Enzyme and pathway databases

BioCycBHAL272558:BH1218-MON.
BRENDA1.4.3.16. 191865.

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...

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Entry information

Entry nameNADB_BACHD
AccessionPrimary (citable) accession number: Q9KDJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 46 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)

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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