Reviewed, UniProtKB/Swiss-Prot Q7W850 (ASPD2_BORPA)

Names and origin

Protein names

Recommended name:
    Probable L-aspartate dehydrogenase 2
    EC=1.4.1.21

Gene names

Name:	nadX2
Ordered Locus Names:	BPP2295

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	267 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 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 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 or NADH binding Inferred from electronic annotation. Source: HAMAP NADP or NADPH 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 – 267	267	Probable L-aspartate dehydrogenase 2 HAMAP MF_01265		PRO_0000144884
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)
	Q7W850-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: F893BCE262E4F60E	FASTA	267	27,782
	10 20 30 40 50 60 MTHRIAFIGL GAIASDVAAG LLADAAQPCQ LAALTRNAAD LPPALAGRVA LLDGLPGLLA 70 80 90 100 110 120 WRPDLVVEAA GQQAIAEHAE GCLKAGLDMI ICSAGALADD ALRARLIAAA EAGGARIRVP 130 140 150 160 170 180 AGAIAGLDYL QAVAGRDDAE VVYESRKPVA AWRAELPGMG IDPDTLAESR TLFSGPAREA 190 200 210 220 230 240 ALRFPKNLNV AATLALAGIG MTRTRVEVVV DPRARGNQHR IQVRSPLGEM QIELVNAPSP 250 260 ANPKTSWLVA QSVLATIRRH LARFTIG

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: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640430 Genomic DNA. Translation: CAE37593.1.
RefSeq	NP_884541.1.
3D structure databases
SMR	Q7W850. Positions 4-265.
ModBase	Search...
Genome annotation databases
GeneID	1664742.
KEGG	bpa:BPP2295.
NMPDR	fig|257311.1.peg.2175.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG649642.
OMA	LATIRRH.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP2295-MONOMER.
BRENDA	1.4.1.21. 263123.
Family and domain databases
HAMAP	MF_01265. NadX. [Tree]
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

ASPD2_BORPA

Accession

Primary (citable) accession number: Q7W850

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 46 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)