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Q9X1X6

- ASPD_THEMA

UniProt

Q9X1X6 - ASPD_THEMA

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Protein

L-aspartate dehydrogenase

Gene
nadX, TM_1643
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H.UniRule annotation

Enzyme regulationi

Competitively inhibited by L-malate and NH4+.UniRule annotation

Kineticsi

  1. KM=0.067 mM for L-aspartate (in the presence of NAD)1 Publication
  2. KM=1.20 mM for L-aspartate (in the presence of NADP)
  3. KM=0.25 mM for NAD
  4. KM=0.72 mM for NADP

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111NAD; via amide nitrogen
Binding sitei28 – 281NAD
Binding sitei57 – 571NAD
Binding sitei63 – 631NAD
Binding sitei64 – 641NAD
Binding sitei78 – 781NAD; via carbonyl oxygen
Binding sitei79 – 791NAD
Binding sitei109 – 1091NAD; via amide nitrogen
Binding sitei164 – 1641NAD
Active sitei193 – 1931 Inferred

GO - Molecular functioni

  1. aspartate dehydrogenase activity Source: UniProtKB-EC
  2. NAD binding Source: UniProtKB-HAMAP
  3. NADP binding Source: UniProtKB-HAMAP
  4. oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Source: UniProtKB-HAMAP

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-HAMAP
  2. NADP catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BRENDAi1.4.1.21. 6331.
SABIO-RKQ9X1X6.
UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
L-aspartate dehydrogenase (EC:1.4.1.21)
Gene namesi
Name:nadX
Ordered Locus Names:TM_1643
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241L-aspartate dehydrogenaseUniRule annotationPRO_0000144893Add
BLAST

Interactioni

Subunit structurei

Homodimer Inferred.

Protein-protein interaction databases

STRINGi243274.TM1643.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi10 – 189
Beta strandi22 – 276
Beta strandi35 – 395
Beta strandi51 – 544
Helixi58 – 6811
Beta strandi71 – 777
Helixi80 – 845
Helixi86 – 9712
Beta strandi102 – 1043
Helixi113 – 1197
Helixi120 – 1223
Beta strandi123 – 13210
Helixi134 – 1374
Beta strandi145 – 1506
Helixi152 – 1587
Beta strandi160 – 1623
Helixi164 – 17310
Helixi175 – 1773
Beta strandi178 – 1847
Beta strandi192 – 20110
Beta strandi203 – 2086
Helixi221 – 23515

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2HX-ray2.60A1-241[»]
1J5PX-ray1.90A1-241[»]
ProteinModelPortaliQ9X1X6.
SMRiQ9X1X6. Positions 1-241.

Miscellaneous databases

EvolutionaryTraceiQ9X1X6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1712.
KOiK06989.
OMAiECAGHSA.
OrthoDBiEOG6ND0JC.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01265. NadX.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR022487. Asp_DH_arc.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF005227. Asp_dh_NAD_syn. 1 hit.
TIGRFAMsiTIGR03855. NAD_NadX. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X1X6-1 [UniParc]FASTAAdd to Basket

« Hide

MTVLIIGMGN IGKKLVELGN FEKIYAYDRI SKDIPGVVRL DEFQVPSDVS    50
TVVECASPEA VKEYSLQILK NPVNYIIIST SAFADEVFRE RFFSELKNSP 100
ARVFFPSGAI GGLDVLSSIK DFVKNVRIET IKPPKSLGLD LKGKTVVFEG 150
SVEEASKLFP RNINVASTIG LIVGFEKVKV TIVADPAMDH NIHIVRISSA 200
IGNYEFKIEN IPSPENPKTS MLTVYSILRT LRNLESKIIF G 241
Length:241
Mass (Da):26,640
Last modified:November 1, 1999 - v1
Checksum:iAF52221512C3DE2E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD36710.1.
PIRiH72226.
RefSeqiNP_229443.1. NC_000853.1.
YP_007978001.1. NC_021214.1.
YP_008991263.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36710; AAD36710; TM_1643.
GeneIDi897714.
KEGGitma:TM1643.
tmi:THEMA_06030.
tmm:Tmari_1652.
PATRICi23938260. VBITheMar51294_1662.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD36710.1 .
PIRi H72226.
RefSeqi NP_229443.1. NC_000853.1.
YP_007978001.1. NC_021214.1.
YP_008991263.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H2H X-ray 2.60 A 1-241 [» ]
1J5P X-ray 1.90 A 1-241 [» ]
ProteinModelPortali Q9X1X6.
SMRi Q9X1X6. Positions 1-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM1643.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD36710 ; AAD36710 ; TM_1643 .
GeneIDi 897714.
KEGGi tma:TM1643.
tmi:THEMA_06030.
tmm:Tmari_1652.
PATRICi 23938260. VBITheMar51294_1662.

Phylogenomic databases

eggNOGi COG1712.
KOi K06989.
OMAi ECAGHSA.
OrthoDBi EOG6ND0JC.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BRENDAi 1.4.1.21. 6331.
SABIO-RK Q9X1X6.

Miscellaneous databases

EvolutionaryTracei Q9X1X6.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_01265. NadX.
InterProi IPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR022487. Asp_DH_arc.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF005227. Asp_dh_NAD_syn. 1 hit.
TIGRFAMsi TIGR03855. NAD_NadX. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiASPD_THEMA
AccessioniPrimary (citable) accession number: Q9X1X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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