[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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

BC088252; AAH88252.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001009643.2; -.

UniGene

Rn.54118

3D structure databases

ModBase

Q5I0J9.

Organism-specific databases

RGD

1310111; RGD1310111.

Gene expression databases

ArrayExpress

Q5I0J9; -.

GermOnline

ENSRNOG00000019424; Rattus norvegicus.

Family and domain databases

InterPro

IPR005106; Asp/hSer_DHase_NAD-bd.
IPR002811; Asp_DHase.
IPR011182; Asp_DHase_NAD_syn.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

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

Q5I0J9.

Genome annotation databases

Ensembl

ENSRNOG00000019424; Rattus norvegicus. [Contig view]

GeneID

292875; -.

KEGG

rno:292875; -.

Phylogenomic databases

HOVERGEN

Q5I0J9; -.

Other

ProtoNet

Q5I0J9.

UniRef

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

Keywords

NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 297`	`297`	`Putative L-aspartate dehydrogenase.`	`PRO_0000144902`
`BINDING`	`131 131`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`196 196`		`NAD (By similarity).`

Sequence information

Length: 297 AA [This is the length of the unprocessed precursor]

Molecular weight: 31260 Da [This is the MW of the unprocessed precursor]

CRC64: 572A02B436161734 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDASMVPRVP HKVGVVGYGR LGQSLVSRLL AQGSELGLEL VFVWNRDPGR MAGSVPPALQ 

        70         80         90        100        110        120 
LEDLTTLEER HPDLVVEVAH PKIIHESGVQ ILRHANLLVG SPSALADQTT ERQLLEASNH 

       130        140        150        160        170        180 
WGHTVFVARG ALWGCEDISR LDAAGGLQSL RVTMATHPDG FRLEGPLAAA HSSGPRTVLY 

       190        200        210        220        230        240 
EGPVRGLCPL APRNSNTMAA AALAAPSLGF DRVIGVLVAD LSLTDMHVVD VELTGPQGPQ 

       250        260        270        280        290 
AAALPCTPTE RTQPSLALSL APLLLQPSGT AYWAAVSFPP DLGSASAEFP PLPLLSP

Q5I0J9 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