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Protein

L-lactate dehydrogenase

Gene

ldh

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: pyruvate fermentation to lactate

This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.
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)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921Substrate
Binding sitei124 – 1241NAD or substrate1 Publication
Binding sitei155 – 1551Substrate
Active sitei179 – 1791Proton acceptor
Binding sitei233 – 2331Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 4329NADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.1.1.27. 623.
SABIO-RKP00344.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase (EC:1.1.1.27)
Short name:
L-LDH
Gene namesi
Name:ldh
Synonyms:lct
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317L-lactate dehydrogenasePRO_0000168328Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei224 – 2241PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 54Combined sources
Beta strandi8 – 125Combined sources
Helixi16 – 2813Combined sources
Beta strandi32 – 376Combined sources
Helixi41 – 5414Combined sources
Beta strandi57 – 604Combined sources
Beta strandi63 – 664Combined sources
Helixi69 – 713Combined sources
Turni72 – 743Combined sources
Beta strandi76 – 805Combined sources
Turni88 – 903Combined sources
Helixi93 – 953Combined sources
Helixi96 – 11318Combined sources
Beta strandi117 – 1215Combined sources
Beta strandi123 – 1253Combined sources
Helixi126 – 13712Combined sources
Helixi141 – 1433Combined sources
Beta strandi144 – 1463Combined sources
Helixi150 – 16415Combined sources
Helixi168 – 1703Combined sources
Beta strandi171 – 1777Combined sources
Turni179 – 1824Combined sources
Beta strandi184 – 1929Combined sources
Beta strandi195 – 1973Combined sources
Helixi202 – 2043Combined sources
Turni205 – 2073Combined sources
Helixi208 – 23023Combined sources
Helixi235 – 24915Combined sources
Beta strandi254 – 26411Combined sources
Helixi265 – 2673Combined sources
Beta strandi269 – 28012Combined sources
Beta strandi283 – 2875Combined sources
Helixi294 – 31320Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00344.

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. 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.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131S → H (PubMed:3675869).Curated

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_LDNU01000115.1.

Cross-referencesi

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_LDNU01000115.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-316.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
BRENDAi1.1.1.27. 623.
SABIO-RKP00344.

Miscellaneous databases

EvolutionaryTraceiP00344.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. 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.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. III) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Hydroxylamine-, o-iodosobenzoic acid- and tryptic-fragments. The complete amino-acid sequence."
    Wirz B., Suter F., Zuber H.
    Hoppe-Seyler's Z. Physiol. Chem. 364:893-909(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
  2. "Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene."
    Barstow D.A., Clarke A.R., Chia W.N., Wigley D., Sharman A.F., Holbrook J.J., Atkinson T., Minton N.P.
    Gene 46:47-55(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, VI. Nucleotide sequences of lactate dehydrogenase genes from the thermophilic bacteria Bacillus stearothermophilus, B. caldolyticus and B. caldotenax."
    Zuelli F., Weber H., Zuber H.
    Biol. Chem. Hoppe-Seyler 368:1167-1177(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. II) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Cyanogen bromide fragments and partial sequence."
    Tratschin J.D., Wirz B., Frank G., Zuber H.
    Hoppe-Seyler's Z. Physiol. Chem. 364:879-892(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
  5. "Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5-A resolution."
    Wigley D.B., Gamblin S.J., Turkenburg J.P., Dodson E.J., Piontek K., Muirhead H., Holbrook J.J.
    J. Mol. Biol. 223:317-335(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG.

Entry informationi

Entry nameiLDH_GEOSE
AccessioniPrimary (citable) accession number: P00344
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: December 9, 2015
This is version 131 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

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.