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Q8XRV9 (ASPD_RALSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable L-aspartate dehydrogenase

EC=1.4.1.21
Gene names
Name:nadX
Ordered Locus Names:RSp0722
ORF Names:RS01727
Encoded onPlasmid megaplasmid Rsp
OrganismRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum) [Complete proteome] [HAMAP]
Taxonomic identifier267608 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length268 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 – 268268Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265
PRO_0000144891

Sites

Active site2211 By similarity
Binding site1251NAD; via amide nitrogen By similarity
Binding site1911NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XRV9 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 9195BAB7EAA9AAE9

FASTA26828,259
        10         20         30         40         50         60 
MLHVSMVGCG AIGQGVLELL KSDPDLCFDT VIVPEHGMDR ARAAIAPFAP RTRVMTRLPA 

        70         80         90        100        110        120 
QADRPDLLVE CAGHDALREH VVPALEQGID CLVVSVGALS EPGLAERLEA AARRGHAQMQ 

       130        140        150        160        170        180 
LLSGAIGAID ALAAARVGGL DAVVYTGRKP PRAWKGTPAE RQFDLDALDR TTVIFEGKAS 

       190        200        210        220        230        240 
DAALLFPKNA NVAATLALAG LGMERTHVRL LADPTIDENI HHVEARGAFG GFELIMRGKP 

       250        260 
LAANPKTSAL TVFSVVRALG NRAHAVSI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL646053 Genomic DNA. Translation: CAD17873.1.
RefSeqNP_522283.1. NC_003296.1.

3D structure databases

ProteinModelPortalQ8XRV9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267608.RS01727.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD17873; CAD17873; RSp0722.
GeneID1223029.
KEGGrso:RS01727.
PATRIC20267051. VBIRalSol70888_4197.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHOG000206326.
KOK06989.
OMAECAGHSA.
OrthoDBEOG6ND0JC.

Enzyme and pathway databases

BioCycRSOL267608:GCVU-4226-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_RALSO
AccessionPrimary (citable) accession number: Q8XRV9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2002
Last modified: May 14, 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