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A3M394 (ASPD_ACIBT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:A1S_0956
OrganismAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]
Taxonomic identifier400667 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length263 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 – 263263Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265
PRO_1000140084

Sites

Active site2161 By similarity
Binding site1201NAD; via amide nitrogen By similarity
Binding site1861NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A3M394 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: A2F94A128F512144

FASTA26327,954
        10         20         30         40         50         60 
MKKLMMIGFG AMAAEVYAHL PQDLQLKWIV VPSRSIEKVQ SQVSSDIQVI SDIEQCDGTP 

        70         80         90        100        110        120 
DYVIEVAGQA AVKEHAQKVL AKGWTIGLIS VGTLADSEFL VQLKQTAEKN DAHLHLLAGA 

       130        140        150        160        170        180 
IAGIDGISAA KEGGLQKVTY KGCKSPKSWK GSYAEQLVDL DHVSEPTVFF TGTAREAAMK 

       190        200        210        220        230        240 
FPANANVAAT IALAGLGMDE TMVELTVDPT INKNKHTIVA EGGFGQMTIE LVGVPLPSNP 

       250        260 
KTSTLAALSV IRACRNSVEA IQI 

« Hide

References

[1]"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17978 / NCDC KC 755.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000521 Genomic DNA. Translation: ABO11388.2.
RefSeqYP_001083990.2. NC_009085.1.

3D structure databases

ProteinModelPortalA3M394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING400667.A1S_0956.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO11388; ABO11388; A1S_0956.
GeneID4917096.
KEGGacb:A1S_0956.
PATRIC20718112. VBIAciBau103176_0970.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHOG000206326.
KOK06989.
OrthoDBEOG6ND0JC.
ProtClustDBPRK13303.

Enzyme and pathway databases

BioCycABAU400667:GI0Q-944-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_ACIBT
AccessionPrimary (citable) accession number: A3M394
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: February 19, 2014
This is version 55 of the entry and version 2 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