Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9KPA4 (NADB_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-aspartate oxidase
Short name=LASPO
EC=1.4.3.16
Alternative name(s):
Quinolinate synthase B
Gene names
Name:nadB
Ordered Locus Names:VC_2469
OrganismVibrio cholerae
Taxonomic identifier666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
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.

Sequence caution

The sequence AAF95611.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-aspartate oxidase activity

Inferred from electronic annotation. Source: EC

L-aspartate:fumarate oxidoreductase 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 – 535535L-aspartate oxidase
PRO_0000184403

Regions

Nucleotide binding12 – 2615FAD Potential

Sites

Active site2441 By similarity
Active site2631 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KPA4 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 0CC31E7FEEF7A601

FASTA53559,873
        10         20         30         40         50         60 
MNADREHQCD VLVIGSGAAG LSLALQVAQY GKVIVLSKGP RSEGATFYAQ GGIAAVFDES 

        70         80         90        100        110        120 
DSIESHVQDT LIAGAGICDE QTVRFIAEHA KECVQWLIDG GVPFDKEEDS DNDHPRYHLT 

       130        140        150        160        170        180 
REGGHSHRRI LHAADATGMA MQTSLQDNAH NHPNITVLER HNALDLITED KIGGDANKVV 

       190        200        210        220        230        240 
GAYVWNRNAE HVETIRAKFV VLATGGASKV YQYTSNPDVS SGDGIAMAWR AGCRVANLEF 

       250        260        270        280        290        300 
NQFHPTCLYH PEARNFLLTE ALRGEGAYLR RPDGSRFMPD FDERAELAPR DIVARAIDFE 

       310        320        330        340        350        360 
MKRLGADCMY LDISHKPADF IEKHFPTIYS RLMDLGIDMT KEPIPIVPAA HYTCGGVMVN 

       370        380        390        400        410        420 
PQGQTDLKQL YAIGEVSYTG LHGANRMASN SLLECVVYAW SASQDIIAQL PNASMPESLP 

       430        440        450        460        470        480 
AWDESQVTCS DEEVVLQHNW HELRLFMWDY MGIVRTNKRL ERAMRRIQLL QQETHEYYSN 

       490        500        510        520        530 
FRVSNNLLEM RNLLQVAELM VRCAMQRKES RGLHYTLDYP DQLAESGPTI LVPEK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003852 Genomic DNA. Translation: AAF95611.1. Different initiation.
PIRB82074.
RefSeqNP_232098.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KPA4.
SMRQ9KPA4. Positions 6-533.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2613011.
GenomeReviewsGene locus VC_2469 in contig AE003852_GR.
KEGGvch:VC2469.
PATRIC20083957. VBIVibCho83274_2353.
TIGRVC_2469.

Phylogenomic databases

HOGENOMHBG293998.
OMAGAYIWNR.
PhylomeDBQ9KPA4.
ProtClustDBPRK09077.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
IPR005288. NadB.
[Graphical view]
Gene3DG3DSA:1.20.58.100. Fum_Rdtase/Succ_DH_flav-like_C. 1 hit.
KOK00278.
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF46977. Succ_DH_flav_C. 1 hit.
TIGRFAMsTIGR00551. NadB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADB_VIBCH
AccessionPrimary (citable) accession number: Q9KPA4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: August 30, 2002
Last modified: January 25, 2012
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents