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A3MD35 (ASPD_BURM7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:BMA10247_A0979
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

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_1000067294

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A3MD35 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 5703F6D14871D311

FASTA27127,747
        10         20         30         40         50         60 
MRNAHAPVDV AMIGFGAIGA AVYRAVEHDA ALRVAHVIVP EHQCDAVRGA LGERVDVVSS 

        70         80         90        100        110        120 
VDALACRPQF ALECAGHGAL VDHVVPLLKA GTDCAVASIG ALSDLALLDA LSNAADAGGA 

       130        140        150        160        170        180 
TLTLLSGAIG GIDALAAARQ GGLDEVRYIG RKPPLGWLGT PAEAICDLRA MAAEQTIFEG 

       190        200        210        220        230        240 
SARDAAQLYP RNANVAATVA LAGVGLDATR VCLIADPAVT RNVHRIVARG AFGEMSIEMS 

       250        260        270 
GKPLPDNPKT SALTAFSAIR ALRNRASHCV I 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10247.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000547 Genomic DNA. Translation: ABO03049.1.
RefSeqYP_001078171.1. NC_009079.1.

3D structure databases

ProteinModelPortalA3MD35.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING320389.BMA10247_A0979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO03049; ABO03049; BMA10247_A0979.
GeneID4890690.
KEGGbmn:BMA10247_A0979.
PATRIC19139687. VBIBurMal96640_0915.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHOG000206326.
KOK06989.
OMAECAGHSA.
OrthoDBEOG6ND0JC.

Enzyme and pathway databases

BioCycBMAL320389:GH97-4510-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_BURM7
AccessionPrimary (citable) accession number: A3MD35
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: May 14, 2014
This is version 51 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