B3R8S4 (ASPD_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable L-aspartate dehydrogenase
EC=1.4.1.21

Gene names

Name:	nadX
Ordered Locus Names:	RALTA_B0572

Organism

Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]

Taxonomic identifier

164546 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Protein existence	Inferred 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. HAMAP-Rule MF_01265
Sequence similarities	Belongs to the L-aspartate dehydrogenase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: HAMAP NADP catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Inferred from electronic annotation. Source: HAMAP NADP binding Inferred from electronic annotation. Source: HAMAP aspartate dehydrogenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 266	266	Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265		PRO_1000140086
Sites
	Active site	219	1	By similarity
	Binding site	123	1	NAD; via amide nitrogen By similarity
	Binding site	189	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	B3R8S4 [UniParc]. Last modified September 2, 2008. Version 1. Checksum: ACE91AE7E3C72B96	FASTA	266	27,799
	10 20 30 40 50 60 MLHVSMVGCG AIGRGVLELL KSDPDVVFDV VIVPEHTMDE ARGAVSALAP RARVATHLDD 70 80 90 100 110 120 QRPDLLVECA GHHALEEHIV PALERGIPCM VVSVGALSEP GMAERLEAAA RRGGTQVQLL 130 140 150 160 170 180 SGAIGAIDAL AAARVGGLDE VIYTGRKPAR AWTGTPAEQL FDLEALTEAT VIFEGTARDA 190 200 210 220 230 240 ARLYPKNANV AATVSLAGLG LDRTAVKLLA DPHAVENVHH VEARGAFGGF ELTMRGKPLA 250 260 ANPKTSALTV FSVVRALGNR AHAVSI

References

[1]

"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia." Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C. Genome Res. 18:1472-1483(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: R1 / LMG 19424.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU633750 Genomic DNA. Translation: CAQ71192.1.
RefSeq	YP_002007253.1. NC_010530.1.
3D structure databases
ProteinModelPortal	B3R8S4.
ModBase	Search...
Protein-protein interaction databases
STRING	164546.RALTA_B0572.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAQ71192; CAQ71192; RALTA_B0572.
GeneID	6455299.
KEGG	cti:RALTA_B0572.
PATRIC	21534923. VBICupTai42494_4076.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1712.
HOGENOM	HOG000206326.
KO	K06989.
OMA	PKTSYLA.
ProtClustDB	PRK13303.
Enzyme and pathway databases
BioCyc	CTAI164546:GJNE-3784-MONOMER.
UniPathway	UPA00253; UER00456.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_01265. NadX.
InterPro	IPR005106. 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]
Pfam	PF01958. DUF108. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
PIRSF	PIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ASPD_CUPTR

Accession

Primary (citable) accession number: B3R8S4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	September 2, 2008
Last modified:	May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program