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Q397Y5 (ASPD_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable L-aspartate dehydrogenase

EC=1.4.1.21
Gene names
Name:nadX
Ordered Locus Names:Bcep18194_B1112
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate By similarity. HAMAP MF_01265

Catalytic activity

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H. HAMAP MF_01265

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. HAMAP MF_01265

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity. HAMAP MF_01265

Sequence similarities

Belongs to the L-aspartate dehydrogenase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

NADP catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

aspartate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Probable L-aspartate dehydrogenase HAMAP MF_01265
PRO_1000067300

Sites

Active site2241 By similarity
Binding site1281NAD; via amide nitrogen By similarity
Binding site1941NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q397Y5 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 22CC0523B9FBADBF

FASTA27127,841
        10         20         30         40         50         60 
MRNAHAPVDV AMIGFGAIGA AVYHAVEHDA SLRIAHVIVP EHQCAAVQGV LGGAVEVVSS 

        70         80         90        100        110        120 
VDALARRPEF ALECAGHSAL VDHVVPLLKA GTDCAVASIG ALSDLALLDV LAQAADEGDA 

       130        140        150        160        170        180 
TVTLLSGAIG GIDALASAKQ GGLDEVLYVG RKPPLGWLGT PAEALCDLRA MTGEKVIFEG 

       190        200        210        220        230        240 
SARDAARLYP KNANVAATVA LAGLGLDATH VRLIADPSVE RNVHRITARG AFGEMSLEMS 

       250        260        270 
GKPLPDNPKT SALTAYSAIR ALRNRAARCV I 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000152 Genomic DNA. Translation: ABB11226.1.
RefSeqYP_371870.1. NC_007511.1.

3D structure databases

ProteinModelPortalQ397Y5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ397Y5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3752877.
GenomeReviewsGene locus Bcep18194_B1112 in contig CP000152_GR.
KEGGbur:Bcep18194_B1112.
NMPDRfig|269483.3.peg.1109.
PATRIC19292972. VBIBurSp120713_5849.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHBG649642.
OMAECAGHSA.
ProtClustDBPRK13303.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_B1112-MONOMER.

Family and domain databases

HAMAPMF_01265. NadX.
[Tree]
InterProIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. Asp_DH_NAD_syn.
IPR020626. Asp_DH_NAD_syn_prok.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK06989.
PfamPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASPD_BURS3
AccessionPrimary (citable) accession number: Q397Y5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families