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Q9X1X6

- ASPD_THEMA

UniProt

Q9X1X6 - ASPD_THEMA

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
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X1X6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L-aspartate dehydrogenase family.Curated

    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

    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: October 1, 2014
    This is version 94 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