Reviewed, UniProtKB/Swiss-Prot Q7WE57 (ASPD3_BORBR)

Names and origin

Protein names

Recommended name:
    Probable L-aspartate dehydrogenase 3
    EC=1.4.1.21

Gene names

Name:	nadX3
Ordered Locus Names:	BB4781

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	272 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 – 272	272	Probable L-aspartate dehydrogenase 3		PRO_0000144882
Sites
	Active site	224	1	By similarity
	Binding site	126	1	NAD; via amide nitrogen By similarity
	Binding site	194	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WE57-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 886F834DB20755BD	FASTA	272	28,270
	10 20 30 40 50 60 MSSREELGVA VAGLGAIGKA LANRLARNEV AGCRLSAVSG RDPGRTADFI ASLPRPVPAV 70 80 90 100 110 120 PLHELPRHAD IVVECAPAAV LPQIVEPVLD AGKKVIVLSV GALLEFPELF RKAGSSDGQI 130 140 150 160 170 180 LVPTGALLGL DAVTAAAEGR IESVKMVSRK PPIGFKGAPI LAERNLDIDG LTEPLLLYSG 190 200 210 220 230 240 SARAAARGFP ANLNVAVALS LAGIGPDETQ LEVWADPGVV RNTHTIEVVS DAALLRMTIE 250 260 270 NIPSENPKTG RITAQSVMAM LRKMSAPVRV GT

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640451 Genomic DNA. Translation: CAE35144.1.
RefSeq	NP_891314.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2659376.
GenomeReviews	Gene locus BB4781 in contig BX470250_GR.
KEGG	bbr:BB4781.
NMPDR	fig|257310.1.peg.4761.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WE57.
Enzyme and pathway databases
BioCyc	BBRO257310:BB4781-MON.
Family and domain databases
HAMAP	MF_01265. [Tree]
InterPro	IPR005106. Asp/hSer_DHase_NAD-bd. IPR002811. Asp_DHase. IPR011182. Asp_DHase_NAD_syn. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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

ASPD3_BORBR

Accession

Primary (citable) accession number: Q7WE57

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	October 1, 2003
Last modified:	November 25, 2008
This is version 34 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)