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Protein

Quinone-dependent D-lactate dehydrogenase

Gene

dld

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

Functioni

Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane.5 Publications

Catalytic activityi

(R)-lactate + a quinone = pyruvate + a quinol.UniRule annotation2 Publications

Cofactori

FADUniRule annotation4 Publications

Enzyme regulationi

Inhibited by 2-hydroxy-3-butynoic acid, but not by p-chloromercuribenzoate, n-ethylmaleimide, or 5,5'-dithiobis(2-nitrobenzoic acid).1 Publication

Kineticsi

  1. KM=0.16 mM for D-lactate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei143FAD; via amide nitrogenUniRule annotationCombined sources1 Publication1
    Binding sitei150FADUniRule annotationCombined sources1 Publication1
    Binding sitei160FAD; via amide nitrogenUniRule annotationCombined sources1 Publication1
    Binding sitei262FAD; via amide nitrogen and carbonyl oxygenUniRule annotationCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi76 – 80FADUniRule annotationCombined sources1 Publication5
    Nucleotide bindingi84 – 85FADUniRule annotationCombined sources1 Publication2

    GO - Molecular functioni

    GO - Biological processi

    • aerobic respiration Source: EcoCyc
    • anaerobic respiration Source: EcoCyc
    • lactate oxidation Source: EcoCyc
    • respiratory electron transport chain Source: EcoCyc
    • transmembrane transport Source: InterPro

    Keywordsi

    Molecular functionOxidoreductase
    LigandFAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciEcoCyc:DLACTDEHYDROGFAD-MONOMER.
    MetaCyc:DLACTDEHYDROGFAD-MONOMER.
    BRENDAi1.1.1.28. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Quinone-dependent D-lactate dehydrogenaseUniRule annotationCurated (EC:1.1.5.12UniRule annotation2 Publications)
    Alternative name(s):
    (R)-lactate:quinone 2-oxidoreductaseCurated
    D-lactate dehydrogenase2 PublicationsUniRule annotation
    Short name:
    D-LDH1 PublicationUniRule annotation
    Respiratory D-lactate dehydrogenaseCurated
    Gene namesi
    Name:dld1 PublicationUniRule annotation
    Ordered Locus Names:b2133, JW2121
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10231. dld.

    Subcellular locationi

    • Cell inner membrane UniRule annotation3 Publications; Peripheral membrane protein UniRule annotation1 Publication; Cytoplasmic side UniRule annotation1 Publication
    • Note: May bind the membrane through electrostatic rather than hydrophobic forces.1 Publication

    GO - Cellular componenti

    • extrinsic component of cytoplasmic side of plasma membrane Source: EcoCyc
    • integral component of plasma membrane Source: InterPro
    • plasma membrane Source: EcoCyc

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Chemistry databases

    DrugBankiDB03147. Flavin adenine dinucleotide.
    DB00756. Hexachlorophene.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000799282 – 571Quinone-dependent D-lactate dehydrogenaseAdd BLAST570

    Keywords - PTMi

    Quinone

    Proteomic databases

    PaxDbiP06149.
    PRIDEiP06149.

    Interactioni

    Protein-protein interaction databases

    BioGridi4260452. 15 interactors.
    IntActiP06149. 17 interactors.
    STRINGi316385.ECDH10B_2289.

    Chemistry databases

    BindingDBiP06149.

    Structurei

    Secondary structure

    1571
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi10 – 20Combined sources11
    Helixi22 – 24Combined sources3
    Helixi29 – 36Combined sources8
    Beta strandi39 – 41Combined sources3
    Beta strandi47 – 50Combined sources4
    Helixi55 – 67Combined sources13
    Beta strandi71 – 77Combined sources7
    Beta strandi81 – 83Combined sources3
    Beta strandi96 – 100Combined sources5
    Beta strandi107 – 110Combined sources4
    Turni111 – 114Combined sources4
    Beta strandi115 – 118Combined sources4
    Helixi124 – 131Combined sources8
    Helixi132 – 134Combined sources3
    Helixi143 – 147Combined sources5
    Helixi151 – 156Combined sources6
    Beta strandi174 – 179Combined sources6
    Beta strandi185 – 189Combined sources5
    Beta strandi191 – 193Combined sources3
    Helixi199 – 207Combined sources9
    Helixi213 – 215Combined sources3
    Helixi228 – 233Combined sources6
    Helixi247 – 249Combined sources3
    Beta strandi259 – 268Combined sources10
    Beta strandi277 – 284Combined sources8
    Helixi286 – 299Combined sources14
    Beta strandi305 – 311Combined sources7
    Helixi312 – 318Combined sources7
    Helixi379 – 387Combined sources9
    Beta strandi389 – 396Combined sources8
    Helixi400 – 414Combined sources15
    Beta strandi418 – 421Combined sources4
    Helixi424 – 434Combined sources11
    Helixi437 – 447Combined sources11
    Helixi449 – 451Combined sources3
    Beta strandi452 – 461Combined sources10
    Helixi475 – 478Combined sources4
    Beta strandi481 – 489Combined sources9
    Turni490 – 493Combined sources4
    Beta strandi494 – 502Combined sources9
    Helixi507 – 520Combined sources14
    Beta strandi527 – 529Combined sources3
    Turni532 – 534Combined sources3
    Helixi539 – 548Combined sources10
    Turni556 – 560Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1F0XX-ray1.90A/B1-571[»]
    ProteinModelPortaliP06149.
    SMRiP06149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06149.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini42 – 213FAD-binding PCMH-typeUniRule annotationAdd BLAST172

    Domaini

    Contains 3 domains: the flavin adenine dinucleotide (FAD)-binding domain, the cap domain and the membrane-binding domain.1 Publication

    Sequence similaritiesi

    Belongs to the quinone-dependent D-lactate dehydrogenase family.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4105CXG. Bacteria.
    COG0277. LUCA.
    HOGENOMiHOG000122232.
    InParanoidiP06149.
    KOiK03777.

    Family and domain databases

    Gene3Di3.30.1370.20. 1 hit.
    3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    3.30.70.610. 2 hits.
    HAMAPiMF_02092. DLDH_Dld. 1 hit.
    InterProiView protein in InterPro
    IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016172. D-lactate_DH_C-sub1.
    IPR016173. D-lactate_DH_C-sub2.
    IPR012256. D_lactate_DH.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR016164. FAD-linked_Oxase-like_C.
    IPR015409. Lactate_DH_C.
    IPR006094. Oxid_FAD_bind_N.
    PfamiView protein in Pfam
    PF01565. FAD_binding_4. 1 hit.
    PF09330. Lact-deh-memb. 1 hit.
    PIRSFiPIRSF000101. D-lactate_dh. 1 hit.
    SUPFAMiSSF55103. SSF55103. 1 hit.
    SSF56176. SSF56176. 1 hit.
    PROSITEiView protein in PROSITE
    PS51387. FAD_PCMH. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06149-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSMTTTDNK AFLNELARLV GSSHLLTDPA KTARYRKGFR SGQGDALAVV
    60 70 80 90 100
    FPGSLLELWR VLKACVTADK IILMQAANTG LTEGSTPNGN DYDRDVVIIS
    110 120 130 140 150
    TLRLDKLHVL GKGEQVLAYP GTTLYSLEKA LKPLGREPHS VIGSSCIGAS
    160 170 180 190 200
    VIGGICNNSG GSLVQRGPAY TEMSLFARIN EDGKLTLVNH LGIDLGETPE
    210 220 230 240 250
    QILSKLDDDR IKDDDVRHDG RHAHDYDYVH RVRDIEADTP ARYNADPDRL
    260 270 280 290 300
    FESSGCAGKL AVFAVRLDTF EAEKNQQVFY IGTNQPEVLT EIRRHILANF
    310 320 330 340 350
    ENLPVAGEYM HRDIYDIAEK YGKDTFLMID KLGTDKMPFF FNLKGRTDAM
    360 370 380 390 400
    LEKVKFFRPH FTDRAMQKFG HLFPSHLPPR MKNWRDKYEH HLLLKMAGDG
    410 420 430 440 450
    VGEAKSWLVD YFKQAEGDFF VCTPEEGSKA FLHRFAAAGA AIRYQAVHSD
    460 470 480 490 500
    EVEDILALDI ALRRNDTEWY EHLPPEIDSQ LVHKLYYGHF MCYVFHQDYI
    510 520 530 540 550
    VKKGVDVHAL KEQMLELLQQ RGAQYPAEHN VGHLYKAPET LQKFYRENDP
    560 570
    TNSMNPGIGK TSKRKNWQEV E
    Length:571
    Mass (Da):64,612
    Last modified:January 23, 2007 - v3
    Checksum:i77FB2C467CB4389F
    GO

    Sequence cautioni

    The sequence AAA60530 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M10038 Genomic DNA. Translation: AAA23688.1.
    X01067 Genomic DNA. Translation: CAA25531.1.
    U00007 Genomic DNA. Translation: AAA60530.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC75194.1.
    AP009048 Genomic DNA. Translation: BAE76610.1.
    PIRiA21893. DEECDL.
    RefSeqiNP_416637.1. NC_000913.3.
    WP_000097403.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75194; AAC75194; b2133.
    BAE76610; BAE76610; BAE76610.
    GeneIDi946653.
    KEGGiecj:JW2121.
    eco:b2133.
    PATRICifig|1411691.4.peg.110.

    Similar proteinsi

    Entry informationi

    Entry nameiDLD_ECOLI
    AccessioniPrimary (citable) accession number: P06149
    Secondary accession number(s): Q2MAU6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: September 27, 2017
    This is version 154 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families