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A3MD35

- ASPD_BURM7

UniProt

A3MD35 - ASPD_BURM7

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Burkholderia mallei (strain NCTC 10247)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (03 Apr 2007)
      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 sitei128 – 1281NAD; 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

    BioCyciBMAL320389:GH97-4510-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:BMA10247_A0979
    OrganismiBurkholderia mallei (strain NCTC 10247)
    Taxonomic identifieri320389 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000002284: Chromosome II

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 271271Probable L-aspartate dehydrogenasePRO_1000067294Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi320389.BMA10247_A0979.

    Structurei

    3D structure databases

    ProteinModelPortaliA3MD35.
    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.

    A3MD35-1 [UniParc]FASTAAdd to Basket

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    MRNAHAPVDV AMIGFGAIGA AVYRAVEHDA ALRVAHVIVP EHQCDAVRGA    50
    LGERVDVVSS VDALACRPQF ALECAGHGAL VDHVVPLLKA GTDCAVASIG 100
    ALSDLALLDA LSNAADAGGA TLTLLSGAIG GIDALAAARQ GGLDEVRYIG 150
    RKPPLGWLGT PAEAICDLRA MAAEQTIFEG SARDAAQLYP RNANVAATVA 200
    LAGVGLDATR VCLIADPAVT RNVHRIVARG AFGEMSIEMS GKPLPDNPKT 250
    SALTAFSAIR ALRNRASHCV I 271
    Length:271
    Mass (Da):27,747
    Last modified:April 3, 2007 - v1
    Checksum:i5703F6D14871D311
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000547 Genomic DNA. Translation: ABO03049.1.
    RefSeqiYP_001078171.1. NC_009079.1.

    Genome annotation databases

    EnsemblBacteriaiABO03049; ABO03049; BMA10247_A0979.
    GeneIDi4890690.
    KEGGibmn:BMA10247_A0979.
    PATRICi19139687. VBIBurMal96640_0915.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000547 Genomic DNA. Translation: ABO03049.1 .
    RefSeqi YP_001078171.1. NC_009079.1.

    3D structure databases

    ProteinModelPortali A3MD35.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 320389.BMA10247_A0979.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO03049 ; ABO03049 ; BMA10247_A0979 .
    GeneIDi 4890690.
    KEGGi bmn:BMA10247_A0979.
    PATRICi 19139687. VBIBurMal96640_0915.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci BMAL320389:GH97-4510-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. DeShazer D., Woods D.E., Nierman W.C.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCTC 10247.

    Entry informationi

    Entry nameiASPD_BURM7
    AccessioniPrimary (citable) accession number: A3MD35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 53 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