Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9X1X6

- ASPD_THEMA

UniProt

Q9X1X6 - ASPD_THEMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

L-aspartate dehydrogenase

Gene

nadX

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 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.

Enzyme regulationi

Competitively inhibited by L-malate and NH4+.

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)1 Publication
  3. KM=0.25 mM for NAD1 Publication
  4. KM=0.72 mM for NADP1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111NAD; via amide nitrogen1 Publication
Binding sitei28 – 281NAD1 Publication
Binding sitei57 – 571NAD1 Publication
Binding sitei63 – 631NAD1 Publication
Binding sitei64 – 641NAD1 Publication
Binding sitei78 – 781NAD; via carbonyl oxygen1 Publication
Binding sitei79 – 791NAD1 Publication
Binding sitei109 – 1091NAD; via amide nitrogen1 Publication
Binding sitei164 – 1641NAD1 Publication
Active sitei193 – 1931Curated

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 dehydrogenasePRO_0000144893Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

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 – 65Combined sources
Helixi10 – 189Combined sources
Beta strandi22 – 276Combined sources
Beta strandi35 – 395Combined sources
Beta strandi51 – 544Combined sources
Helixi58 – 6811Combined sources
Beta strandi71 – 777Combined sources
Helixi80 – 845Combined sources
Helixi86 – 9712Combined sources
Beta strandi102 – 1043Combined sources
Helixi113 – 1197Combined sources
Helixi120 – 1223Combined sources
Beta strandi123 – 13210Combined sources
Helixi134 – 1374Combined sources
Beta strandi145 – 1506Combined sources
Helixi152 – 1587Combined sources
Beta strandi160 – 1623Combined sources
Helixi164 – 17310Combined sources
Helixi175 – 1773Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi192 – 20110Combined sources
Beta strandi203 – 2086Combined sources
Helixi221 – 23515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2HX-ray2.60A1-241[»]
1J5PX-ray1.90A1-241[»]
ProteinModelPortaliQ9X1X6.
SMRiQ9X1X6. Positions 1-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X1X6.

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1712.
InParanoidiQ9X1X6.
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

        10         20         30         40         50
MTVLIIGMGN IGKKLVELGN FEKIYAYDRI SKDIPGVVRL DEFQVPSDVS
60 70 80 90 100
TVVECASPEA VKEYSLQILK NPVNYIIIST SAFADEVFRE RFFSELKNSP
110 120 130 140 150
ARVFFPSGAI GGLDVLSSIK DFVKNVRIET IKPPKSLGLD LKGKTVVFEG
160 170 180 190 200
SVEEASKLFP RNINVASTIG LIVGFEKVKV TIVADPAMDH NIHIVRISSA
210 220 230 240
IGNYEFKIEN IPSPENPKTS MLTVYSILRT LRNLESKIIF G
Length:241
Mass (Da):26,640
Last modified:November 1, 1999 - v1
Checksum:iAF52221512C3DE2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
GeneIDi18093056.
897714.
KEGGitma:TM1643.
PATRICi23938260. VBITheMar51294_1662.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 18093056.
897714.
KEGGi tma:TM1643.
PATRICi 23938260. VBITheMar51294_1662.

Phylogenomic databases

eggNOGi COG1712.
InParanoidi Q9X1X6.
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: November 26, 2014
This is version 96 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