LLDD_ECOLI
ID LLDD_ECOLI Reviewed; 396 AA.
AC P33232; Q2M7R9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01559};
DE EC=1.1.-.- {ECO:0000255|HAMAP-Rule:MF_01559};
GN Name=lldD {ECO:0000255|HAMAP-Rule:MF_01559}; Synonyms=lctD;
GN OrderedLocusNames=b3605, JW3580;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=8407843; DOI=10.1128/jb.175.20.6671-6678.1993;
RA Dong J.M., Taylor J.S., Latour D.J., Iuchi S., Lin E.C.C.;
RT "Three overlapping lct genes involved in L-lactate utilization by
RT Escherichia coli.";
RL J. Bacteriol. 175:6671-6678(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18473; DOI=10.1016/s0021-9258(17)40096-2;
RA Futai M., Kimura H.;
RT "Inducible membrane-bound L-lactate dehydrogenase from Escherichia coli.
RT Purification and properties.";
RL J. Biol. Chem. 252:5820-5827(1977).
CC -!- FUNCTION: Catalyzes the conversion of L-lactate to pyruvate. Seems to
CC be a primary dehydrogenase in the respiratory chain. To a lesser
CC extent, can also oxidize DL-alpha-hydroxybutyrate, but not D-lactate.
CC {ECO:0000269|PubMed:18473, ECO:0000269|PubMed:8407843}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + A = AH2 + pyruvate; Xref=Rhea:RHEA:45816,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16651,
CC ChEBI:CHEBI:17499; Evidence={ECO:0000255|HAMAP-Rule:MF_01559,
CC ECO:0000269|PubMed:18473};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01559, ECO:0000269|PubMed:18473};
CC -!- ACTIVITY REGULATION: Is activated by 2-fold in the presence of high
CC concentrations of sodium and potassium ions. Is almost completely
CC inhibited by a high concentration of pyruvate (10 mM).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for L-lactate {ECO:0000269|PubMed:18473};
CC KM=770 uM for DL-alpha-hydroxybutyrate {ECO:0000269|PubMed:18473};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:18473};
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000269|PubMed:18473}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01559, ECO:0000269|PubMed:18473}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01559, ECO:0000269|PubMed:18473}.
CC -!- INDUCTION: Is induced by aerobic growth on L-lactate, but not by
CC aerobic growth on D-lactate or glycerol or by anaerobic growth on
CC glucose. {ECO:0000269|PubMed:18473, ECO:0000269|PubMed:8407843}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC on L-lactate as the sole source of carbon and energy, but can still
CC utilize D-lactate. {ECO:0000269|PubMed:8407843}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01559}.
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DR EMBL; L13970; AAA03585.1; -; Unassigned_DNA.
DR EMBL; U00039; AAB18582.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76629.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77687.1; -; Genomic_DNA.
DR PIR; C49904; C49904.
DR RefSeq; NP_418062.1; NC_000913.3.
DR RefSeq; WP_000586962.1; NZ_SSZK01000022.1.
DR AlphaFoldDB; P33232; -.
DR SMR; P33232; -.
DR BioGRID; 4262561; 51.
DR DIP; DIP-10108N; -.
DR IntAct; P33232; 16.
DR MINT; P33232; -.
DR STRING; 511145.b3605; -.
DR jPOST; P33232; -.
DR PaxDb; P33232; -.
DR PRIDE; P33232; -.
DR EnsemblBacteria; AAC76629; AAC76629; b3605.
DR EnsemblBacteria; BAE77687; BAE77687; BAE77687.
DR GeneID; 67417608; -.
DR GeneID; 948121; -.
DR KEGG; ecj:JW3580; -.
DR KEGG; eco:b3605; -.
DR PATRIC; fig|1411691.4.peg.3101; -.
DR EchoBASE; EB1906; -.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_020639_0_0_6; -.
DR InParanoid; P33232; -.
DR OMA; FTRLMQT; -.
DR PhylomeDB; P33232; -.
DR BioCyc; EcoCyc:L-LACTDEHYDROGFMN-MON; -.
DR BioCyc; MetaCyc:L-LACTDEHYDROGFMN-MON; -.
DR SABIO-RK; P33232; -.
DR PRO; PR:P33232; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0009060; P:aerobic respiration; IEP:EcoCyc.
DR GO; GO:0042355; P:L-fucose catabolic process; IEP:EcoCyc.
DR GO; GO:0019516; P:lactate oxidation; IMP:EcoCyc.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01559; L_lact_dehydr; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR InterPro; IPR020920; LldD.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Flavoprotein; FMN; Membrane;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..396
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000206335"
FT DOMAIN 1..380
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT BINDING 127
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT BINDING 155
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT BINDING 251
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
FT BINDING 306..330
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559"
SQ SEQUENCE 396 AA; 42728 MW; CA0D8E308713BF83 CRC64;
MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR ILKNMSDLSL
ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAKAADAHG IPFTLSTVSV CPIEEVAPAI
KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR
RYLQAVTHPQ WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLGNNFDP SISWKDLEWI
RDFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD
IAILADSGIR NGLDVVRMIA LGADTVLLGR AFLYALATAG QAGVANLLNL IEKEMKVAMT
LTGAKSISEI TQDSLVQGLG KELPAALAPM AKGNAA
