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A3M394

- ASPD_ACIBT

UniProt

A3M394 - ASPD_ACIBT

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 2 (02 Sep 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 sitei120 – 1201NAD; via amide nitrogenUniRule annotation
    Binding sitei186 – 1861NADUniRule annotation
    Active sitei216 – 2161UniRule 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

    BioCyciABAU400667:GI0Q-944-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:A1S_0956
    OrganismiAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
    Taxonomic identifieri400667 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex
    ProteomesiUP000006737: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 263263Probable L-aspartate dehydrogenasePRO_1000140084Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi400667.A1S_0956.

    Structurei

    3D structure databases

    ProteinModelPortaliA3M394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L-aspartate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1712.
    HOGENOMiHOG000206326.
    KOiK06989.
    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.

    A3M394-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKLMMIGFG AMAAEVYAHL PQDLQLKWIV VPSRSIEKVQ SQVSSDIQVI    50
    SDIEQCDGTP DYVIEVAGQA AVKEHAQKVL AKGWTIGLIS VGTLADSEFL 100
    VQLKQTAEKN DAHLHLLAGA IAGIDGISAA KEGGLQKVTY KGCKSPKSWK 150
    GSYAEQLVDL DHVSEPTVFF TGTAREAAMK FPANANVAAT IALAGLGMDE 200
    TMVELTVDPT INKNKHTIVA EGGFGQMTIE LVGVPLPSNP KTSTLAALSV 250
    IRACRNSVEA IQI 263
    Length:263
    Mass (Da):27,954
    Last modified:September 2, 2008 - v2
    Checksum:iA2F94A128F512144
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000521 Genomic DNA. Translation: ABO11388.2.
    RefSeqiYP_001083990.2. NC_009085.1.

    Genome annotation databases

    EnsemblBacteriaiABO11388; ABO11388; A1S_0956.
    GeneIDi4917096.
    KEGGiacb:A1S_0956.
    PATRICi20718112. VBIAciBau103176_0970.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000521 Genomic DNA. Translation: ABO11388.2 .
    RefSeqi YP_001083990.2. NC_009085.1.

    3D structure databases

    ProteinModelPortali A3M394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 400667.A1S_0956.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO11388 ; ABO11388 ; A1S_0956 .
    GeneIDi 4917096.
    KEGGi acb:A1S_0956.
    PATRICi 20718112. VBIAciBau103176_0970.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci ABAU400667:GI0Q-944-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. "New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
      Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
      Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17978 / NCDC KC 755.

    Entry informationi

    Entry nameiASPD_ACIBT
    AccessioniPrimary (citable) accession number: A3M394
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 58 of the entry and version 2 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