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Reviewed, UniProtKB/Swiss-Prot Q87D19 (NADB_XYLFT)

Last modified November 25, 2008. Version 37. 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: PD_0868
OrganismXylella fastidiosa (strain Temecula1 / ATCC 700964) [Complete proteome] [HAMAP]
Taxonomic identifier183190 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length512 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 + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2).

Cofactor

FAD.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.

Subcellular location

CytoplasmBy 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: InterPro

   Molecular functionL-aspartate oxidase activity

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512L-aspartate oxidase
PRO_0000184405

Regions

Nucleotide binding13 – 2715FAD Potential

Sites

Active site2331 By similarity
Active site2521 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87D19-1 [UniParc].

Last modified June 16, 2003. Version 1.
Checksum: 581222938C6BA53C

FASTA51253,938
        10         20         30         40         50         60 
MAKIVDCFAD RPIIVGSGLA GLIAALTISP EPSVLVTRSA LGAETSSAWA QGGMSVSLSP 

        70         80         90        100        110        120 
DDNPSLHLAD TLAAGDGLCD AVAAESIILE ALDAFHVLQH FGIHFDQDSN GHLALGLEAA 

       130        140        150        160        170        180 
HSRRRIVHVG GDRSGTAIVQ ALTACVLNDP SITVLEGLEA RHILMADNVV CGLLLANPTS 

       190        200        210        220        230        240 
EIVLPSSRIL LATGGIGGLY DATTNPVNNF GQGIAMAARA GAVLADMEFV QFHPTALHCH 

       250        260        270        280        290        300 
NRPLALVSEA VRGEGAVLIN ERGERFMADI PGAELAARNI VAQAISAEIT RGGQVFLDAR 

       310        320        330        340        350        360 
QALGARFSTR FPTITALCHK VGIDPVHMPI PVCPAAHYHM GGIATDRQGR SSIPGLWVAG 

       370        380        390        400        410        420 
EAASTGLHGA NRLASNSLLE AVVMGTRAAR DITSHNTPHP LGTIPITPKK PDTTLIRPIV 

       430        440        450        460        470        480 
SQCLGVLRHA ADMHRAIAAL LPFVEGEEES SDPAIVALLI AIFAHLRTES RGAHARTDFP 

       490        500        510 
LKHDTTQRRN MTLEDVLEIA HSRIAQRKEK IS 

« Hide

Cross-references

Sequence databases

AE009442 Genomic DNA. Translation: AAO28735.1.
RefSeqNP_779086.1.

3D structure databases

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

Genome annotation databases

GeneID1143590.
GenomeReviewsGene locus PD_0868 in contig AE009442_GR.
KEGGxft:PD0868.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ87D19.

Enzyme and pathway databases

BioCycXFAS183190:PD_0868-MON.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR004112. Fum_Rdtase/Succ_DHase_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_XYLFT
AccessionPrimary (citable) accession number: Q87D19
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: November 25, 2008
This is version 37 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