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Reviewed, UniProtKB/Swiss-Prot Q97K95 (NADB_CLOAB)

Last modified November 3, 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

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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: CA_C1024
OrganismClostridium acetobutylicum [Complete proteome] [HAMAP]
Taxonomic identifier1488 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

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Protein attributes

Sequence length434 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 – 434434L-aspartate oxidase
PRO_0000184382

Regions

Nucleotide binding8 – 2215FAD Potential

Sites

Active site2261 By similarity
Active site2471 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q97K95-1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: EB63A654716ABE30

FASTA43448,355
        10         20         30         40         50         60 
MNIQTDVLII GTGVAGLYSA LSLKNDIKVT MLTKSKACEC NTYLAQGGIS TALNKKDEPL 

        70         80         90        100        110        120 
FVDDTLRAGQ YRNIKESVKI LAAESKQNID TLINFGMKFD KNEDGSLNYT REGAHSVNRI 

       130        140        150        160        170        180 
VHSTDETGKV VFETLYNEVK KRPNIEIIEN IQVFDLISED NICFGASALK NNTIYTFHSK 

       190        200        210        220        230        240 
ATILASGGIG GLFKNSTNQR TLTADGIAMA LRHNIDVRDL NYIQFHPTAL YDSNTQEKKF 

       250        260        270        280        290        300 
LISESVRGEG GKLLSIENER FVDELLPRDV VANAIYKEEE KDNSKYVYLD ITSMDADFIT 

       310        320        330        340        350        360 
KRFPGIYKEC LSRGLDITKN KIPVTPVQHY FMGGIKVDFN SLTSMKNLYA CGEVSSTGVH 

       370        380        390        400        410        420 
GANRLASNSL LEGLVFSKRA AENINHSISF IERNEKNENL TLSDALSIIK CNRNIVINKF 

       430 
ESILGEKKNE LVNI

« Hide

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References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

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Cross-references

Sequence databases

AE001437 Genomic DNA. Translation: AAK79000.1.
PIRE97026.
RefSeqNP_347660.1.

3D structure databases

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

Genome annotation databases

GeneID1117207.
GenomeReviewsGene locus CA_C1024 in contig AE001437_GR.
KEGGcac:CAC1024.
NMPDRfig|272562.1.peg.1189.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ97K95.
OMAGAYIWNR.

Enzyme and pathway databases

BioCycCACE272562:CAC1024-MON.
BRENDA1.4.3.16. 2866.

Family and domain databases

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

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Entry information

Entry nameNADB_CLOAB
AccessionPrimary (citable) accession number: Q97K95
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 1, 2001
Last modified: November 3, 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)

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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