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Q9X1X6 (ASPD_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-aspartate dehydrogenase

EC=1.4.1.21
Gene names
Name:nadX
Ordered Locus Names:TM_1643
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-Rule MF_01265

Enzyme regulation

Competitively inhibited by L-malate and NH4+. HAMAP-Rule MF_01265

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. HAMAP-Rule MF_01265

Subunit structure

Homodimer Probable.

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.

Sequence similarities

Belongs to the L-aspartate dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.067 mM for L-aspartate (in the presence of NAD) Ref.3

KM=1.20 mM for L-aspartate (in the presence of NADP)

KM=0.25 mM for NAD

KM=0.72 mM for NADP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 241241L-aspartate dehydrogenase HAMAP-Rule MF_01265
PRO_0000144893

Sites

Active site1931 Probable
Binding site111NAD; via amide nitrogen
Binding site281NAD
Binding site571NAD
Binding site631NAD
Binding site641NAD
Binding site781NAD; via carbonyl oxygen
Binding site791NAD
Binding site1091NAD; via amide nitrogen
Binding site1641NAD

Secondary structure

............................................ 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X1X6 [UniParc].

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

FASTA24126,640
        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

References

« Hide '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. expand/collapse author list , 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.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-241 IN COMPLEX WITH NAD, FUNCTION, CHARACTERIZATION, KINETIC PARAMETERS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36710.1.
PIRH72226.
RefSeqNP_229443.1. NC_000853.1.
YP_007978001.1. NC_021214.1.
YP_008991263.1. NC_023151.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2HX-ray2.60A1-241[»]
1J5PX-ray1.90A1-241[»]
ProteinModelPortalQ9X1X6.
SMRQ9X1X6. Positions 1-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1643.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36710; AAD36710; TM_1643.
GeneID15495254.
18093056.
897714.
KEGGtma:TM1643.
tmm:Tmari_1652.
PATRIC23938260. VBITheMar51294_1662.

Phylogenomic databases

eggNOGCOG1712.
KOK06989.
OMAPKTSYLA.
OrthoDBEOG6ND0JC.
ProtClustDBPRK13303.

Enzyme and pathway databases

BRENDA1.4.1.21. 6331.
SABIO-RKQ9X1X6.
UniPathwayUPA00253; UER00456.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01265. NadX.
InterProIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. Asp_DH_NAD_syn.
IPR020626. Asp_DH_NAD_syn_prok.
IPR022487. Asp_DH_NAD_synth_arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF005227. Asp_dh_NAD_syn. 1 hit.
TIGRFAMsTIGR03855. NAD_NadX. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9X1X6.

Entry information

Entry nameASPD_THEMA
AccessionPrimary (citable) accession number: Q9X1X6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 1, 1999
Last modified: March 19, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways