[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; DOI=10.1038/20601; PubMed=10360571 [NCBI, ExPASy, EBI, Israel, Japan] Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; "Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."; Nature 399:323-329(1999).
[2]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH NAD. Joint center for structural genomics (JCSG); "Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution."; Submitted (JUL-2002) to the PDB data bank.
[3]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-241 IN COMPLEX WITH NAD, FUNCTION, CHARACTERIZATION, AND KINETIC PARAMETERS. DOI=10.1074/jbc.M211892200; PubMed=12496312 [NCBI, ExPASy, EBI, Israel, Japan] Yang Z., Savchenko A., Yakunin A.F., Zhang R., Edwards A.M., Arrowsmith C.H., Tong L.; "Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643."; J. Biol. Chem. 278:8804-8808(2003).

Comments

FUNCTION: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. Does not show aspartate oxidase activity. Is also able to catalyze the reverse reaction, i.e. the reductive amination of oxaloacetate.
CATALYTIC ACTIVITY: L-aspartate + H₂O + NAD(P)⁺ = oxaloacetate + NH₃ + NAD(P)H.
ENZYME REGULATION: Competitively inhibited by L-malate and NH(4)(+).
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=0.067 mM for L-aspartate (in the presence of NAD);
K_M=1.20 mM for L-aspartate (in the presence of NADP);
K_M=0.25 mM for NAD;
K_M=0.72 mM for NADP;
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1 .
SUBUNIT: Homodimer (Probable).
MISCELLANEOUS: The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.
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

AE000512; AAD36710.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H72226; H72226.

RefSeq

NP_229443.1; -.

3D structure databases

PDB

1H2H; X-ray; 2.60 A; A=1-241.	[ExPASy / RCSB / EBI]
1J5P; X-ray; 1.90 A; A=1-241.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1H2H; -.
1J5P; -.

ModBase

Q9X1X6.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1643-MON; -.

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.
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

Q9X1X6.

Genome annotation databases

GeneID

897714; -.

GenomeReviews

AE000512_GR; TM_1643.

KEGG

tma:TM1643; -.

NMPDR

fig|243274.1.peg.1627; -.

TIGR

TM_1643; -.

Phylogenomic databases

HOGENOM

Q9X1X6; -.

Other

Q9X1X6; -.

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

Keywords

3D-structure; Complete proteome; NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 241`	`241`	`L-aspartate dehydrogenase.`	`PRO_0000144893`
`ACT_SITE`	`193 193`		`Probable.`
`BINDING`	`11 11`		`NAD; via amide nitrogen.`
`BINDING`	`28 28`		`NAD.`
`BINDING`	`57 57`		`NAD.`
`BINDING`	`63 63`		`NAD.`
`BINDING`	`64 64`		`NAD.`
`BINDING`	`78 78`		`NAD; via carbonyl oxygen.`
`BINDING`	`79 79`		`NAD.`
`BINDING`	`109 109`		`NAD; via amide nitrogen.`
`BINDING`	`164 164`		`NAD.`
`STRAND`	`2 6`	`5`
`HELIX`	`10 18`	`9`
`STRAND`	`22 27`	`6`
`STRAND`	`35 39`	`5`
`STRAND`	`51 54`	`4`
`HELIX`	`58 68`	`11`
`STRAND`	`71 77`	`7`
`HELIX`	`80 84`	`5`
`HELIX`	`86 97`	`12`
`STRAND`	`102 105`	`4`
`HELIX`	`113 119`	`7`
`HELIX`	`120 122`	`3`
`STRAND`	`123 132`	`10`
`HELIX`	`134 137`	`4`
`STRAND`	`145 150`	`6`
`HELIX`	`152 158`	`7`
`STRAND`	`160 162`	`3`
`HELIX`	`164 173`	`10`
`HELIX`	`175 177`	`3`
`STRAND`	`178 184`	`7`
`STRAND`	`192 210`	`19`
`HELIX`	`221 235`	`15`
`STRAND`	`237 240`	`4`

Sequence information

Length: 241 AA [This is the length of the unprocessed precursor]

Molecular weight: 26640 Da [This is the MW of the unprocessed precursor]

CRC64: AF52221512C3DE2E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTVLIIGMGN IGKKLVELGN FEKIYAYDRI SKDIPGVVRL DEFQVPSDVS TVVECASPEA 

        70         80         90        100        110        120 
VKEYSLQILK NPVNYIIIST SAFADEVFRE RFFSELKNSP ARVFFPSGAI GGLDVLSSIK 

       130        140        150        160        170        180 
DFVKNVRIET IKPPKSLGLD LKGKTVVFEG SVEEASKLFP RNINVASTIG LIVGFEKVKV 

       190        200        210        220        230        240 
TIVADPAMDH NIHIVRISSA IGNYEFKIEN IPSPENPKTS MLTVYSILRT LRNLESKIIF 


G

Q9X1X6 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