Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-lactate dehydrogenase

Gene

lldD

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

Functioni

Catalyzes the conversion of L-lactate to pyruvate. Seems to be a primary dehydrogenase in the respiratory chain. To a lesser extent, can also oxidize DL-alpha-hydroxybutyrate, but not D-lactate.2 Publications

Catalytic activityi

(S)-lactate + an oxidized electron acceptor = pyruvate + a reduced electron acceptor.UniRule annotation1 Publication

Cofactori

FMNUniRule annotation1 Publication

Enzyme regulationi

Is activated by 2-fold in the presence of high concentrations of sodium and potassium ions. Is almost completely inhibited by a high concentration of pyruvate (10 mM).

Kineticsi

  1. KM=120 µM for L-lactate1 Publication
  2. KM=770 µM for DL-alpha-hydroxybutyrate1 Publication

    pH dependencei

    Optimum pH is 8-9.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei24 – 241SubstrateUniRule annotation
    Binding sitei106 – 1061FMNUniRule annotation
    Binding sitei127 – 1271FMNUniRule annotation
    Binding sitei129 – 1291SubstrateUniRule annotation
    Binding sitei155 – 1551FMNUniRule annotation
    Binding sitei164 – 1641SubstrateUniRule annotation
    Binding sitei251 – 2511FMNUniRule annotation
    Active sitei275 – 2751Proton acceptorUniRule annotation
    Binding sitei278 – 2781SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi306 – 33025FMNUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    • FMN binding Source: EcoCyc
    • L-lactate dehydrogenase activity Source: EcoCyc

    GO - Biological processi

    • aerobic respiration Source: EcoCyc
    • lactate oxidation Source: EcoCyc
    • L-fucose catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    BioCyciEcoCyc:L-LACTDEHYDROGFMN-MONOMER.
    ECOL316407:JW3580-MONOMER.
    MetaCyc:L-LACTDEHYDROGFMN-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-lactate dehydrogenaseUniRule annotation (EC:1.1.-.-UniRule annotation)
    Gene namesi
    Name:lldDUniRule annotation
    Synonyms:lctD
    Ordered Locus Names:b3605, JW3580
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11963. lldD.

    Subcellular locationi

    • Cell inner membrane UniRule annotation1 Publication; Peripheral membrane protein UniRule annotation1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene lose the ability to grow on L-lactate as the sole source of carbon and energy, but can still utilize D-lactate.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 396396L-lactate dehydrogenasePRO_0000206335Add
    BLAST

    Proteomic databases

    PaxDbiP33232.
    PRIDEiP33232.

    Expressioni

    Inductioni

    Is induced by aerobic growth on L-lactate, but not by aerobic growth on D-lactate or glycerol or by anaerobic growth on glucose.2 Publications

    Interactioni

    Subunit structurei

    Forms homooligomers.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    yfgLP777741EBI-553210,EBI-907297

    Protein-protein interaction databases

    DIPiDIP-10108N.
    IntActiP33232. 15 interactions.
    MINTiMINT-6478320.
    STRINGi511145.b3605.

    Structurei

    3D structure databases

    ProteinModelPortaliP33232.
    SMRiP33232. Positions 8-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 380380FMN hydroxy acid dehydrogenaseUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.UniRule annotation
    Contains 1 FMN hydroxy acid dehydrogenase domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1304.
    HOGENOMiHOG000217464.
    InParanoidiP33232.
    KOiK00101.
    OMAiAWIKEQW.
    OrthoDBiEOG6HMXBG.
    PhylomeDBiP33232.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01559. L_lact_dehydr.
    InterProiIPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    IPR020920. LldD.
    [Graphical view]
    PfamiPF01070. FMN_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P33232-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR
    60 70 80 90 100
    ILKNMSDLSL ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAKAADAHG
    110 120 130 140 150
    IPFTLSTVSV CPIEEVAPAI KRPMWFQLYV LRDRGFMRNA LERAKAAGCS
    160 170 180 190 200
    TLVFTVDMPT PGARYRDAHS GMSGPNAAMR RYLQAVTHPQ WAWDVGLNGR
    210 220 230 240 250
    PHDLGNISAY LGKPTGLEDY IGWLGNNFDP SISWKDLEWI RDFWDGPMVI
    260 270 280 290 300
    KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD
    310 320 330 340 350
    IAILADSGIR NGLDVVRMIA LGADTVLLGR AFLYALATAG QAGVANLLNL
    360 370 380 390
    IEKEMKVAMT LTGAKSISEI TQDSLVQGLG KELPAALAPM AKGNAA
    Length:396
    Mass (Da):42,728
    Last modified:February 1, 1994 - v1
    Checksum:iCA0D8E308713BF83
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L13970 Unassigned DNA. Translation: AAA03585.1.
    U00039 Genomic DNA. Translation: AAB18582.1.
    U00096 Genomic DNA. Translation: AAC76629.1.
    AP009048 Genomic DNA. Translation: BAE77687.1.
    PIRiC49904.
    RefSeqiNP_418062.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC76629; AAC76629; b3605.
    BAE77687; BAE77687; BAE77687.
    GeneIDi948121.
    KEGGiecj:Y75_p3569.
    eco:b3605.
    PATRICi32122695. VBIEscCol129921_3724.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L13970 Unassigned DNA. Translation: AAA03585.1.
    U00039 Genomic DNA. Translation: AAB18582.1.
    U00096 Genomic DNA. Translation: AAC76629.1.
    AP009048 Genomic DNA. Translation: BAE77687.1.
    PIRiC49904.
    RefSeqiNP_418062.1. NC_000913.3.

    3D structure databases

    ProteinModelPortaliP33232.
    SMRiP33232. Positions 8-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10108N.
    IntActiP33232. 15 interactions.
    MINTiMINT-6478320.
    STRINGi511145.b3605.

    Proteomic databases

    PaxDbiP33232.
    PRIDEiP33232.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76629; AAC76629; b3605.
    BAE77687; BAE77687; BAE77687.
    GeneIDi948121.
    KEGGiecj:Y75_p3569.
    eco:b3605.
    PATRICi32122695. VBIEscCol129921_3724.

    Organism-specific databases

    EchoBASEiEB1906.
    EcoGeneiEG11963. lldD.

    Phylogenomic databases

    eggNOGiCOG1304.
    HOGENOMiHOG000217464.
    InParanoidiP33232.
    KOiK00101.
    OMAiAWIKEQW.
    OrthoDBiEOG6HMXBG.
    PhylomeDBiP33232.

    Enzyme and pathway databases

    BioCyciEcoCyc:L-LACTDEHYDROGFMN-MONOMER.
    ECOL316407:JW3580-MONOMER.
    MetaCyc:L-LACTDEHYDROGFMN-MONOMER.

    Miscellaneous databases

    PROiP33232.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01559. L_lact_dehydr.
    InterProiIPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    IPR020920. LldD.
    [Graphical view]
    PfamiPF01070. FMN_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Three overlapping lct genes involved in L-lactate utilization by Escherichia coli."
      Dong J.M., Taylor J.S., Latour D.J., Iuchi S., Lin E.C.C.
      J. Bacteriol. 175:6671-6678(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
      Strain: K12.
    2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
      Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
      Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Inducible membrane-bound L-lactate dehydrogenase from Escherichia coli. Purification and properties."
      Futai M., Kimura H.
      J. Biol. Chem. 252:5820-5827(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiLLDD_ECOLI
    AccessioniPrimary (citable) accession number: P33232
    Secondary accession number(s): Q2M7R9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: June 24, 2015
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3

    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 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.