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B1LB32

- ASPD_THESQ

UniProt

B1LB32 - ASPD_THESQ

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Thermotoga sp. (strain RQ2)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      Previous versions | rss
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    • Comment

    Functioni

    Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.UniRule annotation

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091NAD; via amide nitrogenUniRule annotation
    Binding sitei164 – 1641NADUniRule annotation
    Active sitei193 – 1931UniRule annotation

    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

    BioCyciTSP126740:GH49-1222-MONOMER.
    UniPathwayiUPA00253; UER00456.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable L-aspartate dehydrogenaseUniRule annotation (EC:1.4.1.21UniRule annotation)
    Gene namesi
    Name:nadXUniRule annotation
    Ordered Locus Names:TRQ2_1186
    OrganismiThermotoga sp. (strain RQ2)
    Taxonomic identifieri126740 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000001687: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 241241Probable L-aspartate dehydrogenasePRO_1000140090Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi126740.TRQ2_1186.

    Structurei

    3D structure databases

    ProteinModelPortaliB1LB32.
    SMRiB1LB32. Positions 1-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L-aspartate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1712.
    HOGENOMiHOG000206326.
    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.

    B1LB32-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVLIIGMGN IGKKLVELGN FEKIYAYDRI SKDIPGVVRL GEFQVPSDVS    50
    TVVECASPEA VKEYSLQILK SPVNYIIIST SAFADEVFRE RFFSELKNSP 100
    ARVFFPSGAI GGLDVLSSIK DFVETVRIET IKPPKSLGLD LKGKTVVFEG 150
    SVEEASKLFP RNINVASTIG LIVGFEKVKV TIVADPAMDH NIHIVRISSA 200
    IGNYEFKIEN IPSPENPKTS MLTVYSILRA LRNLESKIVF G 241
    Length:241
    Mass (Da):26,499
    Last modified:April 29, 2008 - v1
    Checksum:iA7E5A04E3C7B3E82
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000969 Genomic DNA. Translation: ACB09530.1.
    RefSeqiYP_001739213.1. NC_010483.1.

    Genome annotation databases

    EnsemblBacteriaiACB09530; ACB09530; TRQ2_1186.
    GeneIDi6092621.
    KEGGitrq:TRQ2_1186.
    PATRICi23948974. VBITheSp108950_1207.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000969 Genomic DNA. Translation: ACB09530.1 .
    RefSeqi YP_001739213.1. NC_010483.1.

    3D structure databases

    ProteinModelPortali B1LB32.
    SMRi B1LB32. Positions 1-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 126740.TRQ2_1186.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB09530 ; ACB09530 ; TRQ2_1186 .
    GeneIDi 6092621.
    KEGGi trq:TRQ2_1186.
    PATRICi 23948974. VBITheSp108950_1207.

    Phylogenomic databases

    eggNOGi COG1712.
    HOGENOMi HOG000206326.
    KOi K06989.
    OMAi ECAGHSA.
    OrthoDBi EOG6ND0JC.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci TSP126740:GH49-1222-MONOMER.

    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: RQ2.

    Entry informationi

    Entry nameiASPD_THESQ
    AccessioniPrimary (citable) accession number: B1LB32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 45 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.UniRule annotation

    Keywords - Technical termi

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3