Reviewed, UniProtKB/Swiss-Prot Q5LPG8 (ASPD_SILPO)

Names and origin

Protein names

Recommended name:
    Probable L-aspartate dehydrogenase
    EC=1.4.1.21

Gene names

Name:	nadX
Ordered Locus Names:	SPO2880

Organism

Silicibacter pomeroyi [Complete proteome] [HAMAP]

Taxonomic identifier

89184 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Silicibacter

Protein attributes

Sequence length	275 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 – 275	275	Probable L-aspartate dehydrogenase		PRO_0000144892
Sites
	Active site	226	1	By similarity
	Binding site	130	1	NAD; via amide nitrogen By similarity
	Binding site	196	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5LPG8-1 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: D98084319F319CD8	FASTA	275	27,808
	10 20 30 40 50 60 MWKLWGSWPE GDRVRIALIG HGPIAAHVAA HLPVGVQLTG ALCRPGRDDA ARAALGVSVA 70 80 90 100 110 120 QALEGLPQRP DLLVDCAGHS GLRAHGLTAL GAGVEVLTVS VGALADAVFC AELEDAARAG 130 140 150 160 170 180 GTRLCLASGA IGALDALAAA AMGTGLQVTY TGRKPPQGWR GSRAEKVLDL KALTGPVTHF 190 200 210 220 230 240 TGTARAAAQA YPKNANVAAA VALAGAGLDA TRAELIADPG AAANIHEIAA EGAFGRFRFQ 250 260 270 IEGLPLPGNP RSSALTALSL LAALRQRGAA IRPSF

References

[1]

"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment." Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M. , Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N. Nature 432:910-913(2004) [PubMed: 15602564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700808 / DSM 15171 / DSS-3.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000031 Genomic DNA. Translation: AAV96121.1.
RefSeq	YP_168088.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3195767.
GenomeReviews	Gene locus SPO2880 in contig CP000031_GR.
KEGG	sil:SPO2880.
NMPDR	fig|246200.3.peg.3822.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5LPG8.
Enzyme and pathway databases
BioCyc	SPOM246200:SPO_2880-MON.
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_SILPO

Accession

Primary (citable) accession number: Q5LPG8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	February 1, 2005
Last modified:	November 25, 2008
This is version 32 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)