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P33232

- LLDD_ECOLI

UniProt

P33232 - LLDD_ECOLI

Protein

L-lactate dehydrogenase

Gene

lldD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    Cofactori

    FMN.1 PublicationUniRule annotation

    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

    1. FMN binding Source: EcoCyc
    2. L-lactate dehydrogenase (cytochrome) activity Source: InterPro
    3. L-lactate dehydrogenase activity Source: EcoCyc

    GO - Biological processi

    1. aerobic respiration Source: EcoCyc
    2. lactate oxidation Source: EcoCyc
    3. L-fucose catabolic process Source: EcoCyc

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11963. lldD.

    Subcellular locationi

    Cell inner membrane 1 PublicationUniRule annotation; Peripheral membrane protein 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. plasma membrane Source: EcoCyc

    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

    Gene expression databases

    GenevestigatoriP33232.

    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.
    KOiK00101.
    OMAiDCTLLGR.
    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. L-lactate_DHase_bac.
    [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

    MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR    50
    ILKNMSDLSL ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAKAADAHG 100
    IPFTLSTVSV CPIEEVAPAI KRPMWFQLYV LRDRGFMRNA LERAKAAGCS 150
    TLVFTVDMPT PGARYRDAHS GMSGPNAAMR RYLQAVTHPQ WAWDVGLNGR 200
    PHDLGNISAY LGKPTGLEDY IGWLGNNFDP SISWKDLEWI RDFWDGPMVI 250
    KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD 300
    IAILADSGIR NGLDVVRMIA LGADTVLLGR AFLYALATAG QAGVANLLNL 350
    IEKEMKVAMT LTGAKSISEI TQDSLVQGLG KELPAALAPM AKGNAA 396
    Length:396
    Mass (Da):42,728
    Last modified:February 1, 1994 - v1
    Checksum:iCA0D8E308713BF83
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491828.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76629; AAC76629; b3605.
    BAE77687; BAE77687; BAE77687.
    GeneIDi12933567.
    948121.
    KEGGiecj:Y75_p3569.
    eco:b3605.
    PATRICi32122695. VBIEscCol129921_3724.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi C49904.
    RefSeqi NP_418062.1. NC_000913.3.
    YP_491828.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P33232.
    SMRi P33232. Positions 8-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10108N.
    IntActi P33232. 15 interactions.
    MINTi MINT-6478320.
    STRINGi 511145.b3605.

    Proteomic databases

    PaxDbi P33232.
    PRIDEi P33232.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76629 ; AAC76629 ; b3605 .
    BAE77687 ; BAE77687 ; BAE77687 .
    GeneIDi 12933567.
    948121.
    KEGGi ecj:Y75_p3569.
    eco:b3605.
    PATRICi 32122695. VBIEscCol129921_3724.

    Organism-specific databases

    EchoBASEi EB1906.
    EcoGenei EG11963. lldD.

    Phylogenomic databases

    eggNOGi COG1304.
    HOGENOMi HOG000217464.
    KOi K00101.
    OMAi DCTLLGR.
    OrthoDBi EOG6HMXBG.
    PhylomeDBi P33232.

    Enzyme and pathway databases

    BioCyci EcoCyc:L-LACTDEHYDROGFMN-MONOMER.
    ECOL316407:JW3580-MONOMER.
    MetaCyc:L-LACTDEHYDROGFMN-MONOMER.

    Miscellaneous databases

    PROi P33232.

    Gene expression databases

    Genevestigatori P33232.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01559. L_lact_dehydr.
    InterProi IPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    IPR020920. L-lactate_DHase_bac.
    [Graphical view ]
    Pfami PF01070. FMN_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 120 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