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Q397Y5 (ASPD_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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 identifier482957 [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-Rule MF_01265

Catalytic activity

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

Pathway

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

Miscellaneous

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

Sequence similarities

Belongs to the L-aspartate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Probable L-aspartate dehydrogenase HAMAP-Rule 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...
MobiDBSearch...

Protein-protein interaction databases

STRING269483.Bcep18194_B1112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB11226; ABB11226; Bcep18194_B1112.
GeneID3752877.
KEGGbur:Bcep18194_B1112.
PATRIC19292972. VBIBurSp120713_5849.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHOG000206326.
KOK06989.
OMAECAGHSA.
OrthoDBEOG6ND0JC.

Enzyme and pathway databases

BioCycBSP269483:GHLS-4531-MONOMER.
UniPathwayUPA00253; UER00456.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01265. NadX.
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]
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: May 14, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways