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Q0K391 (ASPD_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 42. 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:H16_B0736
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length266 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 MF_01265

Catalytic activity

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

Pathway

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

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity. HAMAP MF_01265

Sequence similarities

Belongs to the L-aspartate dehydrogenase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

NADP catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

aspartate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 266266Probable L-aspartate dehydrogenase HAMAP MF_01265
PRO_1000067312

Sites

Active site2191 By similarity
Binding site1231NAD; via amide nitrogen By similarity
Binding site1891NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0K391 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 81190186F4F9E17B

FASTA26627,776
        10         20         30         40         50         60 
MLHVSMVGCG AIGRGVMELL KSDPEVVFDV VIVPEHTMDE ARDAVTALAP GARVATHLDD 

        70         80         90        100        110        120 
QRPDLLVECA GHHALEEHIV PALERGIPCM VVSVGALSEP GMAERLEAAA RRGGTQVQLL 

       130        140        150        160        170        180 
SGAIGAIDAL AAARVGGLDE VIYTGRKPAR AWAGTPAEQL FDLDALTEAT VIFEGTARDA 

       190        200        210        220        230        240 
ARLYPKNANV AATVSLAGLG LDRTSVKLLA DPHAVENVHH VEARGAFGGF ELTMRGKPLA 

       250        260 
ANPKTSALTV FSVVRALGNR AHAVSI 

« Hide

References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260480 Genomic DNA. Translation: CAJ95533.1.
RefSeqYP_728898.1. NC_008314.1.

3D structure databases

ProteinModelPortalQ0K391.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0K391.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4454967.
GenomeReviewsGene locus H16_B0736 in contig AM260480_GR.
KEGGreh:H16_B0736.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHBG649642.
OMAECAGHSA.
ProtClustDBPRK13303.

Enzyme and pathway databases

BioCycREUT381666:H16_B0736-MONOMER.

Family and domain databases

HAMAPMF_01265. NadX.
[Tree]
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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK06989.
PfamPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASPD_CUPNH
AccessionPrimary (citable) accession number: Q0K391
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 3, 2006
Last modified: November 16, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families