[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1126/science.1127062; PubMed=16857943 [NCBI, ExPASy, EBI, Israel, Japan] Erkel C., Kube M., Reinhardt R., Liesack W.; "Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere."; Science 313:370-372(2006).

Comments

FUNCTION: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate (By similarity).
CATALYTIC ACTIVITY: L-aspartate + H₂O + NAD(P)⁺ = oxaloacetate + NH₃ + 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).
SIMILARITY: Belongs to the L-aspartate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AM114193; CAJ35703.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_685029.1; -.

3D structure databases

ModBase

Q0W7E0.

Ontologies

GO:0033735;	Molecular function: aspartate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from HAMAP).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from HAMAP).
GO:0016639;	Molecular function: oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor (inferred from electronic annotation from HAMAP).
GO:0009435;	Biological process: NAD biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01265; -; 1.
PBIL [Tree]

InterPro

IPR005106; Asp/hSer_DHase_NAD-bd.
IPR002811; Asp_DHase.
IPR011182; Asp_DHase_NAD_syn.
Graphical view of domain structure.

Pfam

PF01958; DUF108; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005227; Asp_dh_NAD_syn; 1.

ProDom

PD017325; Asp_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]

BLOCKS

Q0W7E0.

Genome annotation databases

GeneID

5143303; -.

GenomeReviews

AM114193_GR; UNCMA_24780.

CMR

Q0W7E0; UNCMA_24780.

Other

ProtoNet

Q0W7E0.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 270`	`270`	`Probable L-aspartate dehydrogenase.`	`PRO_1000067314`
`ACT_SITE`	`221 221`		`By similarity.`
`BINDING`	`123 123`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`191 191`		`NAD (By similarity).`

Sequence information

Length: 270 AA [This is the length of the unprocessed precursor]

Molecular weight: 28621 Da [This is the MW of the unprocessed precursor]

CRC64: 62A6113535FAE704 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFRIGIVGAG AIGKEIARAI DNGTVPAKLE AIYDRDTAEA TSFAASLKSK PRVLPLEELV 

        70         80         90        100        110        120 
EASNFVVEAA AQSAVREVAI AALSRSRSVM IMSVGALADK ELLETIRTMA KEHCCSIYLP 

       130        140        150        160        170        180 
SGAIGGLDAV KAASICKIDS VTITTRKPRD GLRGAPFIVR NNIDVDSMDE PTEIFSGPAA 

       190        200        210        220        230        240 
VAIKEFPANV NVAASLSLVG IGFERTLVRV VVDPTIKRNI HEISVRGEFG ELHTVVENVP 

       250        260        270 
ARSNPKTSFL AALSAIATLR QVCEPLKIGT

Q0W7E0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools