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A8GIW3

- ASPD_SERP5

UniProt

A8GIW3 - ASPD_SERP5

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Serratia proteamaculans (strain 568)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (13 Nov 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 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

    BioCyciSPRO399741:GI55-4042-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:Spro_3958
    OrganismiSerratia proteamaculans (strain 568)
    Taxonomic identifieri399741 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia
    ProteomesiUP000007074: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 264264Probable L-aspartate dehydrogenasePRO_1000067313Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi399741.Spro_3958.

    Structurei

    3D structure databases

    ProteinModelPortaliA8GIW3.
    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.

    A8GIW3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKIMMIGYG AMAREVLSRL PDGVSVGWIL ARAAHHAAID SAFGGQVQAL    50
    THPDQCTEQP DLVLECASQQ AVAEFGEAVV TRGWPLAVIS TGALADAALQ 100
    QRLQQACRQH QGQLIVLSGA VAGMDGLASA REGGLDSVTY QACKSPASWR 150
    GSMAEQLIDL DAVSEAQVFF EGSAREAARL FPANANVAAT IALNGLGMDA 200
    TRVRLLVDPA TRRNTHRLQV CGNFGEFQIE LSGNPLASNP KTSTLAALSA 250
    VQACRRLVDG GFIA 264
    Length:264
    Mass (Da):27,768
    Last modified:November 13, 2007 - v1
    Checksum:i2F4AEBCAAA6FB520
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000826 Genomic DNA. Translation: ABV43053.1.
    RefSeqiWP_012146660.1. NC_009832.1.
    YP_001480181.1. NC_009832.1.

    Genome annotation databases

    EnsemblBacteriaiABV43053; ABV43053; Spro_3958.
    GeneIDi5603713.
    KEGGispe:Spro_3958.
    PATRICi32420737. VBISerPro44537_4016.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000826 Genomic DNA. Translation: ABV43053.1 .
    RefSeqi WP_012146660.1. NC_009832.1.
    YP_001480181.1. NC_009832.1.

    3D structure databases

    ProteinModelPortali A8GIW3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 399741.Spro_3958.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV43053 ; ABV43053 ; Spro_3958 .
    GeneIDi 5603713.
    KEGGi spe:Spro_3958.
    PATRICi 32420737. VBISerPro44537_4016.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci SPRO399741:GI55-4042-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 568.

    Entry informationi

    Entry nameiASPD_SERP5
    AccessioniPrimary (citable) accession number: A8GIW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 50 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