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Q126F5

- ASPD_POLSJ

UniProt

Q126F5 - ASPD_POLSJ

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      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 sitei124 – 1241NAD; via amide nitrogenUniRule annotation
    Binding sitei190 – 1901NADUniRule annotation
    Active sitei220 – 2201UniRule 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

    BioCyciPSP296591:GHI4-4405-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:Bpro_3686
    OrganismiPolaromonas sp. (strain JS666 / ATCC BAA-500)
    Taxonomic identifieri296591 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas
    ProteomesiUP000001983: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 267267Probable L-aspartate dehydrogenasePRO_1000067310Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi296591.Bpro_3686.

    Structurei

    3D structure databases

    ProteinModelPortaliQ126F5.
    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q126F5-1 [UniParc]FASTAAdd to Basket

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    MLKIAMIGCG AIGASVLELL HGDSDVVVDR VITVPEARDR TEIAVARWAP    50
    RARVLEVLAA DDAPDLVVEC AGHGAIAAHV VPALERGIPC VVTSVGALSA 100
    PGMAQLLEQA ARRGKTQVQL LSGAIGGIDA LAAARVGGLD SVVYTGRKPP 150
    MAWKGTPAEA VCDLDSLTVA HCIFDGSAEQ AAQLYPKNAN VAATLSLAGL 200
    GLKRTQVQLF ADPGVSENVH HVAAHGAFGS FELTMRGRPL AANPKTSALT 250
    VYSVVRALLN RGRALVI 267
    Length:267
    Mass (Da):27,568
    Last modified:August 22, 2006 - v1
    Checksum:iF1000ACBA87EB262
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000316 Genomic DNA. Translation: ABE45587.1.
    RefSeqiWP_011484578.1. NC_007948.1.
    YP_550485.1. NC_007948.1.

    Genome annotation databases

    EnsemblBacteriaiABE45587; ABE45587; Bpro_3686.
    GeneIDi4013636.
    KEGGipol:Bpro_3686.
    PATRICi22960604. VBIPolSp102244_3756.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000316 Genomic DNA. Translation: ABE45587.1 .
    RefSeqi WP_011484578.1. NC_007948.1.
    YP_550485.1. NC_007948.1.

    3D structure databases

    ProteinModelPortali Q126F5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 296591.Bpro_3686.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE45587 ; ABE45587 ; Bpro_3686 .
    GeneIDi 4013636.
    KEGGi pol:Bpro_3686.
    PATRICi 22960604. VBIPolSp102244_3756.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci PSP296591:GHI4-4405-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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JS666 / ATCC BAA-500.

    Entry informationi

    Entry nameiASPD_POLSJ
    AccessioniPrimary (citable) accession number: Q126F5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 60 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, Reference proteome

    Documents

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

    External Data

    Dasty 3