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Q7WE57

- ASPD3_BORBR

UniProt

Q7WE57 - ASPD3_BORBR

Protein

Probable L-aspartate dehydrogenase 3

Gene

nadX3

Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      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 sitei126 – 1261NAD; via amide nitrogenUniRule annotation
    Binding sitei194 – 1941NADUniRule annotation
    Active sitei224 – 2241UniRule 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

    BioCyciBBRO257310:BB4781-MONOMER.
    UniPathwayiUPA00253; UER00456.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable L-aspartate dehydrogenase 3UniRule annotation (EC:1.4.1.21UniRule annotation)
    Gene namesi
    Name:nadX3UniRule annotation
    Ordered Locus Names:BB4781
    OrganismiBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
    Taxonomic identifieri257310 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
    ProteomesiUP000001027: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 272272Probable L-aspartate dehydrogenase 3PRO_0000144882Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi257310.BB4781.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7WE57.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L-aspartate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1712.
    HOGENOMiHOG000206326.
    KOiK06989.
    OMAiFHAKIEN.
    OrthoDBiEOG6VTK2D.

    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.

    Q7WE57-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSREELGVA VAGLGAIGKA LANRLARNEV AGCRLSAVSG RDPGRTADFI    50
    ASLPRPVPAV PLHELPRHAD IVVECAPAAV LPQIVEPVLD AGKKVIVLSV 100
    GALLEFPELF RKAGSSDGQI LVPTGALLGL DAVTAAAEGR IESVKMVSRK 150
    PPIGFKGAPI LAERNLDIDG LTEPLLLYSG SARAAARGFP ANLNVAVALS 200
    LAGIGPDETQ LEVWADPGVV RNTHTIEVVS DAALLRMTIE NIPSENPKTG 250
    RITAQSVMAM LRKMSAPVRV GT 272
    Length:272
    Mass (Da):28,270
    Last modified:October 1, 2003 - v1
    Checksum:i886F834DB20755BD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX640451 Genomic DNA. Translation: CAE35144.1.
    RefSeqiNP_891314.1. NC_002927.3.

    Genome annotation databases

    EnsemblBacteriaiCAE35144; CAE35144; BB4781.
    GeneIDi2659376.
    KEGGibbr:BB4781.
    PATRICi21143052. VBIBorBro124907_4869.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX640451 Genomic DNA. Translation: CAE35144.1 .
    RefSeqi NP_891314.1. NC_002927.3.

    3D structure databases

    ProteinModelPortali Q7WE57.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 257310.BB4781.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE35144 ; CAE35144 ; BB4781 .
    GeneIDi 2659376.
    KEGGi bbr:BB4781.
    PATRICi 21143052. VBIBorBro124907_4869.

    Phylogenomic databases

    eggNOGi COG1712.
    HOGENOMi HOG000206326.
    KOi K06989.
    OMAi FHAKIEN.
    OrthoDBi EOG6VTK2D.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci BBRO257310:BB4781-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. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
      Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
      , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
      Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-588 / NCTC 13252 / RB50.

    Entry informationi

    Entry nameiASPD3_BORBR
    AccessioniPrimary (citable) accession number: Q7WE57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 71 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