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Protein

L-lactate dehydrogenase

Gene

ldh

Organism
Lactobacillus casei
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of lactate to pyruvate.1 Publication3 Publications

Catalytic activityi

(S)-lactate + NAD+ = pyruvate + NADH.1 Publication2 Publications

Enzyme regulationi

Allosterically activated by fructose 1,6-bisphosphate (FBP) alone under acidic conditions, while it requires additional activation factors such as divalent cations (Mn2+) under neutral conditions (PubMed:14601, PubMed:7766183). Under acidic conditions, Mn2+ is an inhibitor in the absence of fructose 1,6-bisphosphate (FBP) (PubMed:14601, PubMed:7766183). In case of L.casei, L-LDH binds four fructose 1,6-bisphosphate (FBP) molecules per tetramer, while usual allosteric L-LDH binds only two fructose 1,6-bisphosphate (FBP) molecules per tetramer (PubMed:14601, PubMed:7766183).1 Publication2 Publications

Kineticsi

  1. KM=0.45 mM for pyruvate (at pH 4.8)1 Publication
  2. KM=0.71 mM for pyruvate (at pH 5.5)1 Publication
  3. KM=3 mM for pyruvate (at pH 6.2)1 Publication
  4. KM=12 mM for pyruvate (at pH 7)1 Publication
  1. Vmax=2500 µmol/min/mg enzyme with pyruvate as substrate (at pH 6.2)1 Publication
  2. Vmax=2400 µmol/min/mg enzyme with pyruvate as substrate (at pH 7)1 Publication
  3. Vmax=2000 µmol/min/mg enzyme with pyruvate as substrate (at pH 5.5)1 Publication
  4. Vmax=1900 µmol/min/mg enzyme with pyruvate as substrate (at pH 4.8)1 Publication

Temperature dependencei

Thermostable up to 50 degrees Celsius. Thermostabilized in the presence of both fructose 1,6-bisphosphate (FBP) and Mn2+ ions.2 Publications

Pathwayi: pyruvate fermentation to lactate

This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh)
This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei41NADUniRule annotation1
Binding sitei46NADUniRule annotation1
Binding sitei71NADUniRule annotation1
Binding sitei88SubstrateUniRule annotation1
Binding sitei94SubstrateCombined sources1 Publication1
Binding sitei107NADUniRule annotation1
Binding sitei149NADUniRule annotation1
Binding sitei159Allosteric activatorCombined sources1 Publication1
Active sitei181Proton acceptorCombined sources2 Publications1
Binding sitei235SubstrateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 20NADUniRule annotation2
Nucleotide bindingi85 – 86NADUniRule annotation2
Nucleotide bindingi124 – 126NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAllosteric enzyme, Oxidoreductase
LigandNAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8681
SABIO-RKiP00343
UniPathwayiUPA00554; UER00611

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase1 Publication (EC:1.1.1.271 Publication2 Publications)
Short name:
L-LDH1 Publication
Gene namesi
Name:ldh1 Publication
OrganismiLactobacillus casei
Taxonomic identifieri1582 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi171R → Q: Exhibits no significant catalytic activity toward pyruvate up to 50 mM at pH 5.0 in the absence of fructose 1,6-bisphosphate (FBP). In the presence of 5 mM fructose 1,6-bisphosphate (FBP), it exhibits marked catalytic activity. 1 Publication1
Mutagenesisi174H → D: Shows a lower thermoresistance than the wild-type, even in the absence of fructose 1,6-bisphosphate (FBP). Not thermostabilized in the presence of fructose 1,6-bisphosphate (FBP), Mn(2+) or both. Under acidic conditions, the mutant does not show a positive allosteric regulation by fructose 1,6-bisphosphate (FBP), which even inhibits the stimulative effects of the alternative activation factors. In addition, Mn(2+) ions also show greatly reduced inhibitory effects on the mutant enzyme. Under neutral conditions, the reaction of the mutant is slightly enhanced by fructose 1,6-bisphosphate (FBP), but not further stimulates by additional Mn(2+) ions, unlike the case of the wild-type. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001683472 – 326L-lactate dehydrogenaseAdd BLAST325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei226PhosphotyrosineUniRule annotation1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP00343

Interactioni

Subunit structurei

Homotetramer.1 Publication1 Publication

Structurei

Secondary structure

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi11 – 15Combined sources5
Helixi19 – 31Combined sources13
Beta strandi35 – 40Combined sources6
Helixi44 – 55Combined sources12
Helixi56 – 60Combined sources5
Beta strandi65 – 68Combined sources4
Helixi71 – 74Combined sources4
Beta strandi78 – 82Combined sources5
Beta strandi91 – 93Combined sources3
Helixi94 – 103Combined sources10
Helixi105 – 113Combined sources9
Turni114 – 116Combined sources3
Beta strandi119 – 123Combined sources5
Beta strandi125 – 127Combined sources3
Helixi128 – 139Combined sources12
Helixi143 – 145Combined sources3
Beta strandi146 – 148Combined sources3
Helixi152 – 166Combined sources15
Helixi170 – 172Combined sources3
Beta strandi177 – 182Combined sources6
Helixi189 – 191Combined sources3
Helixi199 – 205Combined sources7
Helixi211 – 232Combined sources22
Helixi237 – 251Combined sources15
Beta strandi256 – 266Combined sources11
Helixi267 – 269Combined sources3
Beta strandi270 – 282Combined sources13
Beta strandi285 – 289Combined sources5
Helixi296 – 310Combined sources15
Helixi313 – 316Combined sources4
Helixi318 – 323Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LLCX-ray3.00A2-326[»]
2ZQYX-ray2.60A/B/C/D1-326[»]
2ZQZX-ray2.50A/B/C/D/E/F1-326[»]
3VKUX-ray1.96A/B/C/D/E/F1-326[»]
3VKVX-ray2.70A/B/C/D/E/F1-326[»]
3VPFX-ray2.79A/B/C/D/E/F1-326[»]
ProteinModelPortaliP00343
SMRiP00343
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00343

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 129Substrate bindingCombined sources1 Publication4
Regioni154 – 157Substrate bindingCombined sources1 Publication4
Regioni171 – 174Allosteric activator bindingCombined sources1 Publication4

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. LDH family.Curated

Phylogenomic databases

eggNOGiENOG4105C80 Bacteria
COG0039 LUCA

Family and domain databases

Gene3Di3.90.110.10, 1 hit
HAMAPiMF_00488 Lactate_dehydrog, 1 hit
InterProiView protein in InterPro
IPR001557 L-lactate/malate_DH
IPR011304 L-lactate_DH
IPR018177 L-lactate_DH_AS
IPR022383 Lactate/malate_DH_C
IPR001236 Lactate/malate_DH_N
IPR015955 Lactate_DH/Glyco_Ohase_4_C
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF02866 Ldh_1_C, 1 hit
PF00056 Ldh_1_N, 1 hit
PIRSFiPIRSF000102 Lac_mal_DH, 1 hit
PRINTSiPR00086 LLDHDRGNASE
SUPFAMiSSF51735 SSF51735, 1 hit
SSF56327 SSF56327, 1 hit
TIGRFAMsiTIGR01771 L-LDH-NAD, 1 hit
PROSITEiView protein in PROSITE
PS00064 L_LDH, 1 hit

Sequencei

Sequence statusi: Complete.

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

P00343-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASITDKDHQ KVILVGDGAV GSSYAYAMVL QGIAQEIGIV DIFKDKTKGD
60 70 80 90 100
AIDLSNALPF TSPKKIYSAE YSDAKDADLV VITAGAPQKP GETRLDLVNK
110 120 130 140 150
NLKILKSIVD PIVDSGFNGI FLVAANPVDI LTYATWKLSG FPKNRVVGSG
160 170 180 190 200
TSLDTARFRQ SIAEMVNVDA RSVHAYIMGE HGDTEFPVWS HANIGGVTIA
210 220 230 240 250
EWVKAHPEIK EDKLVKMFED VRDAAYEIIK LKGATFYGIA TALARISKAI
260 270 280 290 300
LNDENAVLPL SVYMDGQYGL NDIYIGTPAV INRNGIQNIL EIPLTDHEEE
310 320
SMQKSASQLK KVLTDAFAKN DIETRQ
Length:326
Mass (Da):35,531
Last modified:January 23, 2007 - v3
Checksum:i934905641592AF8A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26Y → F AA sequence (PubMed:6411465).Curated1
Sequence conflicti52I → T AA sequence (PubMed:6411465).Curated1
Sequence conflicti88 – 89QK → KQ AA sequence (PubMed:6411465).Curated2
Sequence conflicti119G → L AA sequence (PubMed:6411465).Curated1
Sequence conflicti270L → I AA sequence (PubMed:6411465).Curated1
Sequence conflicti273I → L AA sequence (PubMed:6411465).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12591 Genomic DNA Translation: BAA02133.1
M76708 Genomic DNA Translation: AAA25245.2
PIRiA43944 DELBLA
RefSeqiWP_003567646.1, NZ_MWVD01000024.1

Genome annotation databases

GeneIDi31583240

Similar proteinsi

Entry informationi

Entry nameiLDH_LACCA
AccessioniPrimary (citable) accession number: P00343
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 138 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, Direct protein sequencing
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Main funding by: National Institutes of Health