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Reviewed, UniProtKB/Swiss-Prot Q92R32 (NADB_RHIME)

Last modified June 16, 2009. Version 51. 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: R01095
ORF Names: SMc02599
OrganismRhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier382 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length532 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 – 532532L-aspartate oxidase
PRO_0000184397

Regions

Nucleotide binding18 – 3215FAD Potential

Sites

Active site2421 By similarity
Active site2611 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92R32-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 7C3321F90921E8E9

FASTA53256,646
        10         20         30         40         50         60 
MLTDHFRPQS FNGIDDIVIV GGGLAGLFCA LKLAPRPVTI LAAAPIGYGA SSAWAQGGIA 

        70         80         90        100        110        120 
AAMSKGDTFE KHVADTVAAG AGIVDEKMTR MMVAEGPARI HDLLEFGVPF DRDLEGKLLL 

       130        140        150        160        170        180 
SREAAHSERR IVRVKGDMAG KSIMEALIAA VRNTPSIRVI EGYVVEELVR EGRFISGVIA 

       190        200        210        220        230        240 
RPDAGQSKSR VSFPARAVVL CSGGVGHLYA VTTNPWEACG QGVGMAARAG AIIADPEFVQ 

       250        260        270        280        290        300 
FHPTAIDIGK DPAPLATEAL RGDGATLINS EGRRFMLDIH PDGELAPRDI VSRGVFAEVQ 

       310        320        330        340        350        360 
AGRGAFLDCT KAVGRHFPEM FPTVYASCMA AGIDPVRQPI PVTPAVHYHM GGVLTDGEGR 

       370        380        390        400        410        420 
TSIDGLWAAG EVTSTGVHGA NRLASNSLLE AVVFAARIAE NIKGSLPAPK LTAWGDNAGE 

       430        440        450        460        470        480 
NDDPVTVEDS PPFKVLRQLM SDCVGVVRTR ESLTRAIRGI AELERTNKRL RFANIATTAK 

       490        500        510        520        530 
LIAIAALQRT ESRGGHFRAD CPDERPEWRR RTYLTLAQAE RLAAEVAESE PA 

« Hide

References

Cross-references

Sequence databases

AL591688 Genomic DNA. Translation: CAC45674.1.
RefSeqNP_385201.1.

3D structure databases

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

Genome annotation databases

GeneID1232739.
GenomeReviewsGene locus R01095 in contig AL591688_GR.
KEGGsme:SMc02599.
NMPDRfig|266834.1.peg.2389.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ92R32.
OMAQ92R32. AGCHYNN.

Enzyme and pathway databases

BioCycSMEL266834:SMC02599-MON.
BRENDA1.4.3.16. 142.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
IPR005288. NadB.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00551. nadB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADB_RHIME
AccessionPrimary (citable) accession number: Q92R32
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: December 1, 2001
Last modified: June 16, 2009
This is version 51 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