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Reviewed, UniProtKB/Swiss-Prot Q59767 (NADB_RHORU)

Last modified June 16, 2009. Version 42. 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
OrganismRhodospirillum rubrum
Taxonomic identifier1085 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length277 AA.
Sequence statusFragment.
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
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 277›277L-aspartate oxidase
PRO_0000184398

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q59767-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 253364CE414F5204

FASTA27728,540
        10         20         30         40         50         60 
ILVDAQGRRF MTALDPAAEL APRDVVTRGV AAAIKAGKGA FLDARTALGA AFPQAFPTVY 

        70         80         90        100        110        120 
AACRASGIDP VRQPIPIAPA AHYHMGGVLT DSFGRTSIDG LWAVGEVACT GAHGANRLAS 

       130        140        150        160        170        180 
NSLLEAVVFA ARVAGDVGAA PLRRGWPPPA PPDLSPRPPP AEDAAAITRL RATMSARVGV 

       190        200        210        220        230        240 
IRDGQGLESA LATIETIAAG ARSPRLRAMT TAARLITAAA LARRESRGAH FRADYPATDP 

       250        260        270 
AQSHRATAPF GPLRTVPPHP AQSLGEGLAA PPMETRS 

« Hide

References

[1]"Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators."
Shelver D., Kerby R.L., He Y., Roberts G.P.
J. Bacteriol. 177:2157-2163(1995) [PubMed: 7721706] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: UR1.

Cross-references

Sequence databases

U65510 Genomic DNA. Translation: AAC45129.1.
PIRT51327.

3D structure databases

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

Enzyme and pathway databases

BRENDA1.4.3.16. 1671.

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...

Entry information

Entry nameNADB_RHORU
AccessionPrimary (citable) accession number: Q59767
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 42 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