Reviewed, UniProtKB/Swiss-Prot Q58325 (ASPD_METJA)

Names and origin

Protein names

Recommended name:
    Probable L-aspartate dehydrogenase
    EC=1.4.1.21

Gene names

Name:	nadX
Ordered Locus Names:	MJ0915

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	267 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 – 267	267	Probable L-aspartate dehydrogenase		PRO_0000144896
Sites
	Active site	218	1	By similarity
	Binding site	124	1	NAD; via amide nitrogen By similarity
	Binding site	190	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q58325-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B2C427DFD3AE1A4F	FASTA	267	28,755
	10 20 30 40 50 60 MLKIGIVGCG AIGNFITKKV LDGTIKNAKI SAVYDRNFDK AKTLSERTGA KICSSIDDLV 70 80 90 100 110 120 KEDLDLVVEA ASIKAVEEIA EKSLINNKDV LIMSVGALAD KKLFLKLRDL AKTVGRKIYL 130 140 150 160 170 180 PSGAIGGLDA IKALRLGEIE EVVLKTTKPV AALEDALKNL GYKPEDIKNP VIVFEGDVFK 190 200 210 220 230 240 AIKEFPANIN VSVTLSIAAE FPAKVVIVAD PNAKLNKHEL FVKSSIGTLR VCIENVPFEE 250 260 NPRTSALAAY SAVRLIRDLA EPVKVGT

References

[1]

"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L77117 Genomic DNA. Translation: AAB98920.1.
PIR	C64414.
RefSeq	NP_247910.1.
3D structure databases
HSSP	HSSP built from PDB template 1H2H based on UniProtKB Q9X1X6.
ModBase	Search...
Genome annotation databases
GeneID	1451804.
GenomeReviews	Gene locus MJ0915 in contig L77117_GR.
KEGG	mja:MJ0915.
NMPDR	fig|243232.1.peg.947.
TIGR	MJ0915.
Phylogenomic databases
HOGENOM	Q58325.
Enzyme and pathway databases
BioCyc	MJAN243232:MJ_0915-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

ASPD_METJA

Accession

Primary (citable) accession number: Q58325

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 54 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)