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Q6FDH0

- ASPD_ACIAD

UniProt

Q6FDH0 - ASPD_ACIAD

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    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

    BioCyciASP62977:GJVV-940-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:ACIAD0997
    OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
    Taxonomic identifieri62977 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
    ProteomesiUP000000430: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 263263Probable L-aspartate dehydrogenasePRO_0000144879Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi62977.ACIAD0997.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6FDH0.
    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.

    Q6FDH0-1 [UniParc]FASTAAdd to Basket

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    MKQLMMIGFG AMASEVYAHL PQDLELKWIV VPERSVESVK QKVDRHIQVI    50
    SDINQCDGAP DYVIEVAGQA AVKEHAKNVL AHGWNIGLIS VGTLADSEFF 100
    TELQQTAEQN GAHLHLLAGA IAGIDGIAAA KEGGLEKVTY KGCKSPNSWR 150
    GSYAEQLIDL DQVHTVTMFY RGTAREAAQK FPANANVAAT IALAGVGMDN 200
    TIVELTVDPD TTQNKHTIVA EGRFGQMTIE MVGVPLASNP KTSTLAALSV 250
    IRACRNSVEA IQI 263
    Length:263
    Mass (Da):28,221
    Last modified:July 19, 2004 - v1
    Checksum:i9AB52FEC3BA88672
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR543861 Genomic DNA. Translation: CAG67888.1.
    RefSeqiYP_045710.1. NC_005966.1.

    Genome annotation databases

    EnsemblBacteriaiCAG67888; CAG67888; ACIAD0997.
    GeneIDi2880590.
    KEGGiaci:ACIAD0997.
    PATRICi20739852. VBIAciSp98416_0890.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR543861 Genomic DNA. Translation: CAG67888.1 .
    RefSeqi YP_045710.1. NC_005966.1.

    3D structure databases

    ProteinModelPortali Q6FDH0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 62977.ACIAD0997.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG67888 ; CAG67888 ; ACIAD0997 .
    GeneIDi 2880590.
    KEGGi aci:ACIAD0997.
    PATRICi 20739852. VBIAciSp98416_0890.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci ASP62977:GJVV-940-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. "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
      Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
      Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33305 / BD413 / ADP1.

    Entry informationi

    Entry nameiASPD_ACIAD
    AccessioniPrimary (citable) accession number: Q6FDH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 72 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