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Reviewed, UniProtKB/Swiss-Prot Q98AV8 (NADB_RHILO)

Last modified November 3, 2009. Version 41. 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: mll5834
OrganismRhizobium loti (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier381 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length513 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 – 513513L-aspartate oxidase
PRO_0000184396

Regions

Nucleotide binding13 – 2715FAD Potential

Sites

Active site2331 By similarity
Active site2521 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98AV8-1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 6DA2B4B63F4200BC

FASTA51353,469
        10         20         30         40         50         60 
MTADIHHIGG APVIIGAGIA GLMTALHLAP QPVVLLSRTS LGTEASSILA QGGLAASLGE 

        70         80         90        100        110        120 
DDSPDLHLAD TLAAGEGLCD EQMARRVVEA APQAVENLIR LGTPFDRSLD GRLQLGLEAA 

       130        140        150        160        170        180 
HSRRRIVHAA GDATGRELFR ALLGVARRTR SITIMEGMTA LRLVVAEGSI VGLLTVLHGA 

       190        200        210        220        230        240 
VFALPTRRVV LATGGIGGLF CDTTNPLSSF GHGLALAACA GAELADLEFV QFHPTALDIA 

       250        260        270        280        290        300 
RRPMPLVSEA VRGEGAVLID EHGHRLLADT PGAELASRDV VARAISDQLA AGHGVYLDAR 

       310        320        330        340        350        360 
HCLGQKFARR FPAIDAICKH AGIDPAVEPI PVRPAAHYHM GGVAVDAEGR TSVSGLWACG 

       370        380        390        400        410        420 
EVACTGLHGA NRLASNSLTE AVATAAWVAE SVAGTSAGWQ WPRLPATVPI RPDPSPIRTI 

       430        440        450        460        470        480 
VSNALGIVRN GKSLCDTVAT LLPISVCETA AADPALVALL MAIAALRREE SRGSHFRSDF 

       490        500        510 
PGRDAAALPS RLTLCTAFEN AVTLRWQASE RSR 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

BA000012 Genomic DNA. Translation: BAB52214.1.
RefSeqNP_106428.1.

3D structure databases

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

Genome annotation databases

GeneID1229087.
GenomeReviewsGene locus mll5834 in contig BA000012_GR.
KEGGmlo:mll5834.
NMPDRfig|266835.1.peg.4531.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ98AV8.
OMAVSRHLGV.

Enzyme and pathway databases

BRENDA1.4.3.16. 3315.

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_RHILO
AccessionPrimary (citable) accession number: Q98AV8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 1, 2001
Last modified: November 3, 2009
This is version 41 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