Reviewed, UniProtKB/Swiss-Prot A3NIZ0 (ASPD_BURP6)

Names and origin

Protein names

Recommended name:
    Probable L-aspartate dehydrogenase
    EC=1.4.1.21

Gene names

Name:	nadX
Ordered Locus Names:	BURPS668_A1314

Organism

Burkholderia pseudomallei (strain 668) [Complete proteome] [HAMAP]

Taxonomic identifier

320373 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate By similarity.
Catalytic activity	L-aspartate + H(2)O + NAD(P)(+) = oxaloacetate + NH(3) + NAD(P)H.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.
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.

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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro 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 – 271	271	Probable L-aspartate dehydrogenase		PRO_1000067299
Sites
	Active site	224	1	By similarity
	Binding site	128	1	NAD; via amide nitrogen By similarity
	Binding site	194	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3NIZ0-1 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 5703F6D14871D311	FASTA	271	27,747
	10 20 30 40 50 60 MRNAHAPVDV AMIGFGAIGA AVYRAVEHDA ALRVAHVIVP EHQCDAVRGA LGERVDVVSS 70 80 90 100 110 120 VDALACRPQF ALECAGHGAL VDHVVPLLKA GTDCAVASIG ALSDLALLDA LSNAADAGGA 130 140 150 160 170 180 TLTLLSGAIG GIDALAAARQ GGLDEVRYIG RKPPLGWLGT PAEAICDLRA MAAEQTIFEG 190 200 210 220 230 240 SARDAAQLYP RNANVAATVA LAGVGLDATR VCLIADPAVT RNVHRIVARG AFGEMSIEMS 250 260 270 GKPLPDNPKT SALTAFSAIR ALRNRASHCV I

References

[1]	DeShazer D., Woods D.E., Nierman W.C. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000571 Genomic DNA. Translation: ABN88349.1.
RefSeq	YP_001062311.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4888894.
GenomeReviews	Gene locus BURPS668_A1314 in contig CP000571_GR.
KEGG	bpd:BURPS668_A1314.
TIGR	BURPS668_A1314.
Family and domain databases
HAMAP	MF_01265. [Tree]
InterPro	IPR005106. Asp/hSer_DHase_NAD-bd. IPR002811. Asp_DHase. IPR011182. Asp_DHase_NAD_syn. [Graphical view]
Pfam	PF01958. DUF108. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
PIRSF	PIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProDom	PD017325. Asp_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

ASPD_BURP6

Accession

Primary (citable) accession number: A3NIZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	April 3, 2007
Last modified:	November 25, 2008
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)