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B2UJ42

- ASPD_RALPJ

UniProt

B2UJ42 - ASPD_RALPJ

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Ralstonia pickettii (strain 12J)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (01 Jul 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 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

    BioCyciRPIC402626:GH94-4565-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:Rpic_4503
    OrganismiRalstonia pickettii (strain 12J)
    Taxonomic identifieri402626 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia
    ProteomesiUP000002566: Chromosome 2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 267267Probable L-aspartate dehydrogenasePRO_1000140089Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi402626.Rpic_4503.

    Structurei

    3D structure databases

    ProteinModelPortaliB2UJ42.
    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.

    B2UJ42-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLHVSMVGCG AIGQGVLELL KSDPDVCFDA VIVPEHAMDK AREAIAPFAP    50
    NARVTTHLSA DAHTDLLVEC AGHDALEEHV LPALEQGIDC LVVSVGALSQ 100
    PGVAERLEAA ARRGNAQVQL LSGAIGAIDA LAAARVGGLD AVIYTGRKPP 150
    RAWKDTPAEQ QFDLDALREP TVIFEGNARE AARLFPKNAN VAATLSLAGL 200
    GLEHTHVKLL ADPTVDENIH HVEARGAFGG FELTMRGKPL AANPKTSALT 250
    VFSVVRALGN RAHAVSI 267
    Length:267
    Mass (Da):27,992
    Last modified:July 1, 2008 - v1
    Checksum:i0505734D6239093A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001069 Genomic DNA. Translation: ACD29593.1.
    RefSeqiYP_001893020.1. NC_010678.1.

    Genome annotation databases

    EnsemblBacteriaiACD29593; ACD29593; Rpic_4503.
    GeneIDi6285681.
    KEGGirpi:Rpic_4503.
    PATRICi20249971. VBIRalPic63053_0756.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001069 Genomic DNA. Translation: ACD29593.1 .
    RefSeqi YP_001893020.1. NC_010678.1.

    3D structure databases

    ProteinModelPortali B2UJ42.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 402626.Rpic_4503.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACD29593 ; ACD29593 ; Rpic_4503 .
    GeneIDi 6285681.
    KEGGi rpi:Rpic_4503.
    PATRICi 20249971. VBIRalPic63053_0756.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci RPIC402626:GH94-4565-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. "Complete sequence of chromosome 2 of Ralstonia pickettii 12J."
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
      , Kyrpides N., Mikhailova N., Marsh T., Richardson P.
      Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 12J.

    Entry informationi

    Entry nameiASPD_RALPJ
    AccessioniPrimary (citable) accession number: B2UJ42
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 42 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