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Protein

D-amino acid dehydrogenase

Gene

dadA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D-serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine.2 Publications

Catalytic activityi

A D-amino acid + H2O + acceptor = a 2-oxo acid + NH3 + reduced acceptor.2 Publications

Cofactori

FADBy similarity

Enzyme regulationi

Is activated by the HinT protein. Is inhibited by D-cycloserine.2 Publications

Kineticsi

  1. KM=30 mM for D-alanine2 Publications
  2. KM=6.4 mM for 3,4-dehydro-D-proline2 Publications

    pH dependencei

    Optimum pH is about 8.9 with D-alanine as substrate and about 9 with 3,4-dehydro-D-proline as substrate.2 Publications

    Pathwayi: D-alanine degradation

    This protein is involved in step 1 of the subpathway that synthesizes NH(3) and pyruvate from D-alanine.
    Proteins known to be involved in this subpathway in this organism are:
    1. D-amino acid dehydrogenase (dadA)
    This subpathway is part of the pathway D-alanine degradation, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes NH(3) and pyruvate from D-alanine, the pathway D-alanine degradation and in Amino-acid degradation.

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi3 – 17FADSequence analysisAdd BLAST15

    GO - Molecular functioni

    • D-amino-acid dehydrogenase activity Source: EcoCyc

    GO - Biological processi

    • D-alanine catabolic process Source: EcoCyc
    • D-amino acid catabolic process Source: UniProtKB-HAMAP
    • L-alanine oxidation to pyruvate via D-alanine Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciEcoCyc:DALADEHYDROGA-MONOMER.
    ECOL316407:JW1178-MONOMER.
    MetaCyc:DALADEHYDROGA-MONOMER.
    UniPathwayiUPA00043; UER00498.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-amino acid dehydrogenase (EC:1.4.99.-2 Publications)
    Alternative name(s):
    D-alanine dehydrogenase
    Gene namesi
    Name:dadA
    Synonyms:dadR
    Ordered Locus Names:b1189, JW1178
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11407. dadA.

    Subcellular locationi

    • Cell inner membrane 2 Publications; Peripheral membrane protein 2 Publications

    GO - Cellular componenti

    • plasma membrane Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Loss of the ability to utilize both D- and L-stereoisomers of alanine as sole sources of carbon, nitrogen and energy for growth.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001661311 – 432D-amino acid dehydrogenaseAdd BLAST432

    Proteomic databases

    EPDiP0A6J5.
    PaxDbiP0A6J5.
    PRIDEiP0A6J5.

    Expressioni

    Inductioni

    By D-alanine. Is regulated by catabolite repression.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi4260104. 11 interactors.
    DIPiDIP-6852N.
    IntActiP0A6J5. 21 interactors.
    STRINGi511145.b1189.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A6J5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DadA oxidoreductase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105MWK. Bacteria.
    COG0665. LUCA.
    HOGENOMiHOG000217450.
    InParanoidiP0A6J5.
    KOiK00285.
    OMAiCDNSGAY.
    PhylomeDBiP0A6J5.

    Family and domain databases

    Gene3Di3.40.50.720. 3 hits.
    HAMAPiMF_01202. DadA. 1 hit.
    InterProiIPR023080. DadA.
    IPR006076. FAD-dep_OxRdtase.
    IPR023753. FAD/NAD-binding_dom.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01266. DAO. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 3 hits.

    Sequencei

    Sequence statusi: Complete.

    P0A6J5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRVVILGSGV VGVASAWYLN QAGHEVTVID REPGAALETS AANAGQISPG
    60 70 80 90 100
    YAAPWAAPGV PLKAIKWMFQ RHAPLAVRLD GTQFQLKWMW QMLRNCDTSH
    110 120 130 140 150
    YMENKGRMVR LAEYSRDCLK ALRAETNIQY EGRQGGTLQL FRTEQQYENA
    160 170 180 190 200
    TRDIAVLEDA GVPYQLLESS RLAEVEPALA EVAHKLTGGL QLPNDETGDC
    210 220 230 240 250
    QLFTQNLARM AEQAGVKFRF NTPVDQLLCD GEQIYGVKCG DEVIKADAYV
    260 270 280 290 300
    MAFGSYSTAM LKGIVDIPVY PLKGYSLTIP IAQEDGAPVS TILDETYKIA
    310 320 330 340 350
    ITRFDNRIRV GGMAEIVGFN TELLQPRRET LEMVVRDLYP RGGHVEQATF
    360 370 380 390 400
    WTGLRPMTPD GTPVVGRTRF KNLWLNTGHG TLGWTMACGS GQLLSDLLSG
    410 420 430
    RTPAIPYEDL SVARYSRGFT PSRPGHLHGA HS
    Length:432
    Mass (Da):47,607
    Last modified:March 29, 2005 - v1
    Checksum:iEE747358845B6280
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L02948 Unassigned DNA. Translation: AAC36880.1.
    U00096 Genomic DNA. Translation: AAC74273.1.
    AP009048 Genomic DNA. Translation: BAA36044.1.
    PIRiB53383.
    RefSeqiNP_415707.1. NC_000913.3.
    WP_001266908.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74273; AAC74273; b1189.
    BAA36044; BAA36044; BAA36044.
    GeneIDi945752.
    KEGGiecj:JW1178.
    eco:b1189.
    PATRICi32117624. VBIEscCol129921_1234.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L02948 Unassigned DNA. Translation: AAC36880.1.
    U00096 Genomic DNA. Translation: AAC74273.1.
    AP009048 Genomic DNA. Translation: BAA36044.1.
    PIRiB53383.
    RefSeqiNP_415707.1. NC_000913.3.
    WP_001266908.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP0A6J5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260104. 11 interactors.
    DIPiDIP-6852N.
    IntActiP0A6J5. 21 interactors.
    STRINGi511145.b1189.

    Proteomic databases

    EPDiP0A6J5.
    PaxDbiP0A6J5.
    PRIDEiP0A6J5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74273; AAC74273; b1189.
    BAA36044; BAA36044; BAA36044.
    GeneIDi945752.
    KEGGiecj:JW1178.
    eco:b1189.
    PATRICi32117624. VBIEscCol129921_1234.

    Organism-specific databases

    EchoBASEiEB1379.
    EcoGeneiEG11407. dadA.

    Phylogenomic databases

    eggNOGiENOG4105MWK. Bacteria.
    COG0665. LUCA.
    HOGENOMiHOG000217450.
    InParanoidiP0A6J5.
    KOiK00285.
    OMAiCDNSGAY.
    PhylomeDBiP0A6J5.

    Enzyme and pathway databases

    UniPathwayiUPA00043; UER00498.
    BioCyciEcoCyc:DALADEHYDROGA-MONOMER.
    ECOL316407:JW1178-MONOMER.
    MetaCyc:DALADEHYDROGA-MONOMER.

    Miscellaneous databases

    PROiP0A6J5.

    Family and domain databases

    Gene3Di3.40.50.720. 3 hits.
    HAMAPiMF_01202. DadA. 1 hit.
    InterProiIPR023080. DadA.
    IPR006076. FAD-dep_OxRdtase.
    IPR023753. FAD/NAD-binding_dom.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01266. DAO. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 3 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDADA_ECOLI
    AccessioniPrimary (citable) accession number: P0A6J5
    Secondary accession number(s): P29011
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: November 2, 2016
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to be a heterodimer based on the purification of the enzyme first reported from E.coli B, but results of enzyme assays in PubMed:21378189 have indicated that DadA is solely responsible for the observed dehydrogenase activity.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.