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Protein

L-aspartate dehydrogenase

Gene

nadX

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

    Pathway: NAD(+) biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes iminoaspartate from L-aspartate (dehydrogenase route).
    Proteins known to be involved in this subpathway in this organism are:
    1. L-aspartate dehydrogenase (nadX)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes iminoaspartate from L-aspartate (dehydrogenase route), the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    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

    GO - Biological processi

    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 Componenti: 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.
    OMAiPKTSYLA.
    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.
    WP_004082138.1. NC_023151.1.
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36710.1.
    PIRiH72226.
    RefSeqiNP_229443.1. NC_000853.1.
    WP_004082138.1. NC_023151.1.
    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H2HX-ray2.60A1-241[»]
    1J5PX-ray1.90A1-241[»]
    ProteinModelPortaliQ9X1X6.
    SMRiQ9X1X6. Positions 1-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243274.TM1643.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    eggNOGiCOG1712.
    InParanoidiQ9X1X6.
    KOiK06989.
    OMAiPKTSYLA.
    OrthoDBiEOG6ND0JC.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9X1X6.

    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.
    ProtoNetiSearch...

    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: May 27, 2015
    This is version 101 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.