Q9DCQ2 (ASPD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative L-aspartate dehydrogenase
EC=1.4.1.21

Alternative name(s):
Aspartate dehydrogenase domain-containing protein

Gene names

Name:

Aspdh

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	287 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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.
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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway NADP catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro aspartate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 287	287	Putative L-aspartate dehydrogenase		PRO_0000144901
Sites
	Binding site	131	1	NAD; via amide nitrogen By similarity
	Binding site	196	1	NAD By similarity
Experimental info
	Sequence conflict	117	1	A → V in AAH19451. Ref.2
	Sequence conflict	245	1	A → S in AAH19451. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9DCQ2 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 889D164D943B88DD	FASTA	287	30,270
	10 20 30 40 50 60 MATSTLPQVP YKVGVVGYGR LGQSLVSRLL AQGSELGLEL VFVWNRDPGR MAGSVPPALQ 70 80 90 100 110 120 LQDLTALEER HPDLVVEVAH PKIIHESGAQ ILRHANLLVG SPSALADQTT EQQLLEASKR 130 140 150 160 170 180 WGHTVFVARG ALWGSEDISR LDAAGGLQSL RVTMATHPDG FRLEGPLAAA HSSGPRTVLY 190 200 210 220 230 240 EGPVRGLCPL APRNSNTMAA AALAAPSLGF DRVIGVLVAD LSLTDMHVVD VELLGPPGPS 250 260 270 280 GRSFAVHTHR ENPAQPGAVT GSATVTAFWH SLLGCCQLTS RPGIHLC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver.
[3]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 13-20, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK002587 mRNA. Translation: BAB22209.1. BC019451 mRNA. Translation: AAH19451.1.
IPI	IPI00471091.
RefSeq	NP_080966.1. NM_026690.1.
UniGene	Mm.88478.
3D structure databases
ProteinModelPortal	Q9DCQ2.
SMR	Q9DCQ2. Positions 13-231.
ModBase	Search...
PTM databases
PhosphoSite	Q9DCQ2.
Proteomic databases
PaxDb	Q9DCQ2.
PRIDE	Q9DCQ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035929; ENSMUSP00000039202; ENSMUSG00000038704.
GeneID	68352.
KEGG	mmu:68352.
UCSC	uc009gpk.1. mouse.
Organism-specific databases
CTD	554235.
MGI	MGI:1915602. Aspdh.
Phylogenomic databases
eggNOG	COG1712.
GeneTree	ENSGT00390000004452.
HOGENOM	HOG000007399.
HOVERGEN	HBG062283.
InParanoid	Q9DCQ2.
OMA	LAFVWNR.
OrthoDB	EOG44QT21.
Enzyme and pathway databases
UniPathway	UPA00253; UER00456.
Gene expression databases
ArrayExpress	Q9DCQ2.
Bgee	Q9DCQ2.
CleanEx	MM_0610012D14RIK.
Genevestigator	Q9DCQ2.
GermOnline	ENSMUSG00000038704. Mus musculus.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR005106. Asp/hSer_DH_NAD-bd. IPR002811. Asp_DH. IPR011182. Asp_DH_NAD_syn. 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...
Other
NextBio	327053.
SOURCE	Search...

Entry information

Entry name

ASPD_MOUSE

Accession

Primary (citable) accession number: Q9DCQ2
Secondary accession number(s): Q8VCQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program