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Reviewed, UniProtKB/Swiss-Prot Q9K107 (NADB_NEIMB)

Last modified February 9, 2010. Version 52. 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: NMB0392
OrganismNeisseria meningitidis serogroup B [Complete proteome] [HAMAP]
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length502 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.

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 – 502502L-aspartate oxidase
PRO_0000184392

Regions

Nucleotide binding8 – 2215FAD Potential

Sites

Active site2281 By similarity
Active site2491 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K107-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 644152CC3753E294

FASTA50254,563
        10         20         30         40         50         60 
MQTDCDVLIA GNGLAALTLA LSLPESFRIV ILCKNRLDDT ASRHAQGGIA AAWSGEDDIE 

        70         80         90        100        110        120 
KHVADTLEAG AGLCDEAAVR AILSQGKPAI EWLLAQGVAF DRNHNGLHLT REGGHTCRRI 

       130        140        150        160        170        180 
AHVADYTGEA VMQSLIAQIR RRPNIRVCER QMALDIQTES GAACGLTVLD CRTQETYRIR 

       190        200        210        220        230        240 
ARHTVLAGGG LGQIYAATTT PPECTGDAIA MAIRAGCAVG NLEFIQFHPT GLARPSENGR 

       250        260        270        280        290        300 
TFLISEAVRG EGGILTNQAG ERFMPHYDRR AELAPRDIVA RAIAAEIAKQ TQDFVSLDIS 

       310        320        330        340        350        360 
HQPAAFVRRH FPSIHRHCLS QCGLDITRQA IPVRPVQHYT CGGIQTDPCG RTSLPQLYAL 

       370        380        390        400        410        420 
GETACTGLHG ANRLASNSLL ECVVTARLCA QAIADGQAFQ AEPFQRPSES LSAEAGIFSD 

       430        440        450        460        470        480 
DLQNTFSRPV LQTFNQRHLG ILRNDTGLRR AIAQLQLWKQ NQAEPHTASE YENRNLLECS 

       490        500 
LAVAQAAYRR RQNIGAHFNS DC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002098 Genomic DNA. Translation: AAF40832.1.
PIRH81203.
RefSeqNP_273441.1.

3D structure databases

SMRQ9K107. Positions 3-502.
ModBaseSearch...

Genome annotation databases

GeneID902507.
GenomeReviewsGene locus NMB0392 in contig AE002098_GR.
KEGGnme:NMB0392.
NMPDRfig|122586.1.peg.375.
TIGRNMB0392.

Phylogenomic databases

HOGENOMHBG293998.
OMAGAYIWNR.

Enzyme and pathway databases

BioCycNMEN122586:NMB_0392-MONOMER.
BRENDA1.4.3.16. 293828.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
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_NEIMB
AccessionPrimary (citable) accession number: Q9K107
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 52 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