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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

  1. FMN binding Source: EcoCyc
  2. 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
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11963. lldD.

Subcellular locationi

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

GO - Cellular componenti

  1. 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

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.
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. 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

        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.
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:
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.
YP_491828.1. NC_007779.1.

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.
GeneIDi12933567.
948121.
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.

Gene expression databases

GenevestigatoriP33232.

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]
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: January 7, 2015
This is version 123 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.