L-aspartate dehydrogenase - Thermotoga maritima

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Reviewed, UniProtKB/Swiss-Prot Q9X1X6 (ASPD_THEMA)

Last modified June 16, 2009. Version 56. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
L-aspartate dehydrogenase
EC=1.4.1.21

Gene names

Name:	nadX
Ordered Locus Names:	TM_1643

Organism

Thermotoga maritima [Complete proteome] [HAMAP]

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

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Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (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. Ref.3
Catalytic activity	L-aspartate + H₂O + NAD(P)⁺ = oxaloacetate + NH₃ + NAD(P)H. HAMAP MF_01265
Enzyme regulation	Competitively inhibited by L-malate and NH₄⁺. HAMAP MF_01265
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. HAMAP MF_01265
Subunit structure	Homodimer Probable.
Miscellaneous	The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia. HAMAP MF_01265
Sequence similarities	Belongs to the L-aspartate dehydrogenase family.
biophysicochemical properties	Kinetic parameters: K_M=0.067 mM for L-aspartate (in the presence of NAD) Ref.3 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

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Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure 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 or NADH binding Inferred from electronic annotation. Source: HAMAP NADP or NADPH binding Inferred from electronic annotation. Source: HAMAP aspartate dehydrogenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 241

241

L-aspartate dehydrogenase HAMAP MF_01265

PRO_0000144893

Sites

Active site

193

Probable

Binding site

NAD; via amide nitrogen HAMAP MF_01265

Binding site

NAD HAMAP MF_01265

Binding site

NAD HAMAP MF_01265

Binding site

NAD HAMAP MF_01265

Binding site

NAD HAMAP MF_01265

Binding site

NAD; via carbonyl oxygen HAMAP MF_01265

Binding site

NAD HAMAP MF_01265

Binding site

109

NAD; via amide nitrogen HAMAP MF_01265

Binding site

164

NAD HAMAP MF_01265

Secondary structure

241

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9X1X6-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: AF52221512C3DE2E
Show »

FASTA

241

26,640

        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

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." 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. Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution." Joint center for structural genomics (JCSG) Submitted (JUL-2002) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH NAD.
[3]	"Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643." Yang Z., Savchenko A., Yakunin A.F., Zhang R., Edwards A.M., Arrowsmith C.H., Tong L. J. Biol. Chem. 278:8804-8808(2003) [PubMed: 12496312] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-241 IN COMPLEX WITH NAD, FUNCTION, CHARACTERIZATION, KINETIC PARAMETERS.

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Cross-references

Sequence databases

AE000512 Genomic DNA. Translation: AAD36710.1.

PIR

H72226.

RefSeq

NP_229443.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H2H	X-ray	2.60	A	1-241	[»]
1J5P	X-ray	1.90	A	1-241	[»]

ModBase

Search...

Genome annotation databases

GeneID

897714.

GenomeReviews

Gene locus TM_1643 in contig AE000512_GR.

KEGG

tma:TM1643.

NMPDR

fig|243274.1.peg.1627.

TIGR

TM_1643.

Phylogenomic databases

HOGENOM

Q9X1X6.

OMA

Q9X1X6. ECAGHSA.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1643-MON.

BRENDA

1.4.1.21. 16699.

Family and domain databases

HAMAP

MF_01265.
[Tree]

InterPro

IPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. Asp_DH_NAD_syn.
IPR016040. NAD(P)-bd_dom.
[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...

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Entry information

Entry name

ASPD_THEMA

Accession

Primary (citable) accession number: Q9X1X6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 56 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)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families