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UniProtKB/Swiss-Prot entry Q0K391

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ASPD_RALEH
Primary accession number Q0K391
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on October 3, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 19)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: H16_B0736
From
Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [TaxID: 381666] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Cupriavidus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1244; PubMed=16964242 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16.";
Nat. Biotechnol. 24:1257-1262(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AM260480; CAJ95533.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_728898.1; -.
3D structure databases
ModBase Q0K391.
Ontologies
GO
GO:0033735; Molecular function: aspartate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from HAMAP).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from HAMAP).
GO:0016639; Molecular function: oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor (inferred from electronic annotation from HAMAP).
GO:0009435; Biological process: NAD biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01265; -; 1.
PBIL [Tree]
InterPro IPR005106; Asp/hSer_DHase_NAD-bd.
IPR002811; Asp_DHase.
IPR011182; Asp_DHase_NAD_syn.
Graphical view of domain structure.
Pfam PF01958; DUF108; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005227; Asp_dh_NAD_syn; 1.
ProDom PD017325; Asp_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q0K391.
Genome annotation databases
GeneID 4454967; -.
GenomeReviews AM260480_GR; H16_B0736.
KEGG reh:H16_B0736; -.
Phylogenomic databases
HOGENOM Q0K391; -.
Genome annotation databases
CMR Q0K391; H16_B0736.
Other
ProtoNet Q0K391.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   266  266     Probable L-aspartate dehydrogenase. PRO_1000067312
ACT_SITE   219   219        By similarity. 
BINDING   123   123        NAD; via amide nitrogen (By similarity). 
BINDING   189   189        NAD (By similarity). 
Sequence information
Length: 266 AA [This is the length of the unprocessed precursor] Molecular weight: 27776 Da [This is the MW of the unprocessed precursor] CRC64: 81190186F4F9E17B [This is a checksum on the sequence] 
        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
Q0K391 in FASTA format

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