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Protein

L-lactate dehydrogenase

Gene

ldh

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of lactate to pyruvate.2 Publications

Catalytic activityi

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

Enzyme regulationi

Allosterically activated by fructose 1,6-bisphosphate (FBP). The improvement in affinity for substrate occurs in two steps; the binding of fructose 1,6-bisphosphate (FBP) to the dimer, and the dimer to tetramer conversion.1 Publication2 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_1), 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 sitei38NADCombined sources2 Publications1
Binding sitei43NADUniRule annotation1
Binding sitei69NADUniRule annotation1
Binding sitei86SubstrateUniRule annotation1
Binding sitei92SubstrateCombined sources1 Publication1
Binding sitei105NADUniRule annotation1
Binding sitei147NADCombined sources2 Publications1
Binding sitei157Allosteric activatorCombined sources1 Publication1
Active sitei179Proton acceptorCombined sources1 Publication1
Binding sitei233SubstrateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi16 – 17NADCombined sources2 Publications2
Nucleotide bindingi83 – 84NADUniRule annotation2
Nucleotide bindingi122 – 124NADCombined sources2 Publications3

GO - Molecular functioni

  • L-lactate dehydrogenase activity Source: UniProtKB
  • NAD binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionAllosteric enzyme, Oxidoreductase
LigandNAD

Enzyme and pathway databases

BRENDAi1.1.1.27 623
SABIO-RKiP00344
UniPathwayiUPA00554; UER00611

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase1 Publication (EC:1.1.1.271 Publication)
Short name:
L-LDH1 Publication
Gene namesi
Name:ldh1 Publication
Synonyms:lct
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi157R → Q: This mutant undergoes a reversible subunit assembly from dimer to tetramer. However, the tetramer mutant is much more stable than the wild type, and is destabilized rather than stabilized by binding the allosteric regulator, fructose 1,6-bisphosphate (FBP). The mutation weakens the binding of fructose 1,6-bisphosphate (FBP) to both the dimeric and tetrameric forms, and almost abolishes any stimulatory effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001683281 – 317L-lactate dehydrogenaseAdd BLAST317

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei224PhosphotyrosineUniRule annotation1

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Exists as a dimer and a tetramer (dimer of dimers). The conversion occurs via the binding of fructose 1,6-bisphosphate (FBP) to the dimer.1 Publication3 Publications

Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2 – 5Combined sources4
Beta strandi8 – 12Combined sources5
Helixi16 – 28Combined sources13
Beta strandi32 – 37Combined sources6
Helixi41 – 54Combined sources14
Beta strandi57 – 60Combined sources4
Beta strandi63 – 66Combined sources4
Helixi69 – 71Combined sources3
Turni72 – 74Combined sources3
Beta strandi76 – 80Combined sources5
Turni88 – 90Combined sources3
Helixi93 – 95Combined sources3
Helixi96 – 113Combined sources18
Beta strandi117 – 121Combined sources5
Beta strandi123 – 125Combined sources3
Helixi126 – 137Combined sources12
Helixi141 – 143Combined sources3
Beta strandi144 – 146Combined sources3
Helixi150 – 164Combined sources15
Helixi168 – 170Combined sources3
Beta strandi171 – 177Combined sources7
Turni179 – 182Combined sources4
Beta strandi184 – 192Combined sources9
Beta strandi195 – 197Combined sources3
Helixi202 – 204Combined sources3
Turni205 – 207Combined sources3
Helixi208 – 230Combined sources23
Helixi235 – 249Combined sources15
Beta strandi254 – 264Combined sources11
Helixi265 – 267Combined sources3
Beta strandi269 – 280Combined sources12
Beta strandi283 – 287Combined sources5
Helixi294 – 313Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LDBX-ray2.80A/B/C/D1-317[»]
1LDNX-ray2.50A/B/C/D/E/F/G/H1-316[»]
2LDBX-ray3.00A/B/C/D1-317[»]
ProteinModelPortaliP00344
SMRiP00344
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00344

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni124 – 127Substrate bindingUniRule annotation4
Regioni152 – 155Substrate bindingCombined sources1 Publication4
Regioni169 – 172Allosteric activator bindingCombined sources2 Publications4

Sequence similaritiesi

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

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.

P00344-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNNGGARVV VIGAGFVGAS YVFALMNQGI ADEIVLIDAN ESKAIGDAMD
60 70 80 90 100
FNHGKVFAPK PVDIWHGDYD DCRDADLVVI CAGANQKPGE TRLDLVDKNI
110 120 130 140 150
AIFRSIVESV MASGFQGLFL VATNPVDILT YATWKFSGLP HERVIGSGTI
160 170 180 190 200
LDTARFRFLL GEYFSVAPQN VHAYIIGEHG DTELPVWSQA YIGVMPIRKL
210 220 230 240 250
VESKGEEAQK DLERIFVNVR DAAYQIIEKK GATYYGIAMG LARVTRAILH
260 270 280 290 300
NENAILTVSA YLDGLYGERD VYIGVPAVIN RNGIREVIEI ELNDDEKNRF
310
HHSAATLKSV LARAFTR
Length:317
Mass (Da):34,863
Last modified:January 1, 1988 - v1
Checksum:i4B146CF681C91046
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti113S → H in AAA22567 (PubMed:3675869).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14788 Genomic DNA Translation: AAA22568.1
M19396 Genomic DNA Translation: AAA22567.1
PIRiA26053 DEBSLF
RefSeqiWP_033016716.1, NZ_LUCR01000141.1

Similar proteinsi

Entry informationi

Entry nameiLDH_GEOSE
AccessioniPrimary (citable) accession number: P00344
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: April 25, 2018
This is version 138 of the entry and version 1 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health