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Q9HYA4 (ASPD_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. 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:PA3505
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length267 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 – 267267Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265
PRO_0000144890

Sites

Active site2201 By similarity
Binding site1241NAD; via amide nitrogen By similarity
Binding site1901NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HYA4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 208FBC975A872F86

FASTA26727,920
        10         20         30         40         50         60 
MLNIVMIGCG AIGAGVLELL ENDPQLRVDA VIVPRDSETQ VRHRLASLRR PPRVLSALPA 

        70         80         90        100        110        120 
GERPDLLVEC AGHRAIEQHV LPALAQGIPC LVVSVGALSE PGLVERLEAA AQAGGSRIEL 

       130        140        150        160        170        180 
LPGAIGAIDA LSAARVGGLE SVRYTGRKPA SAWLGTPGET VCDLQRLEKA RVIFDGSARE 

       190        200        210        220        230        240 
AARLYPKNAN VAATLSLAGL GLDRTQVRLI ADPESCENVH QVEASGAFGG FELTLRGKPL 

       250        260 
AANPKTSALT VYSVVRALGN HAHAISI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG06893.1.
PIRG83206.
RefSeqNP_252195.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9HYA4.
SMRQ9HYA4. Positions 6-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA3505.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG06893; AAG06893; PA3505.
GeneID879175.
KEGGpae:PA3505.
PATRIC19841623. VBIPseAer58763_3669.

Organism-specific databases

PseudoCAPPA3505.

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHOG000206326.
KOK06989.
OMAECAGHSA.
OrthoDBEOG6ND0JC.

Enzyme and pathway databases

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_PSEAE
AccessionPrimary (citable) accession number: Q9HYA4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 78 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