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Protein

L-lactate dehydrogenase

Gene
N/A
Organism
Plasmodium falciparum (isolate CDC / Honduras)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathway:ipyruvate 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
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 sitei14 – 141NAD; via amide nitrogen
Binding sitei15 – 151NAD; via amide nitrogen
Binding sitei35 – 351NAD
Binding sitei67 – 671NAD
Binding sitei81 – 811NAD; via amide nitrogen
Binding sitei82 – 821NAD; via carbonyl oxygen
Binding sitei95 – 951Substrate
Binding sitei125 – 1251NAD; via carbonyl oxygen
Binding sitei127 – 1271NAD
Binding sitei150 – 1501NAD; via carbonyl oxygen
Binding sitei158 – 1581Substrate
Active sitei182 – 1821Proton acceptor
Binding sitei182 – 1821Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 150137NADAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, Pyruvate

Enzyme and pathway databases

BRENDAi1.1.1.27. 4889.
SABIO-RKQ27743.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase (EC:1.1.1.27)
Alternative name(s):
LDH-P
OrganismiPlasmodium falciparum (isolate CDC / Honduras)
Taxonomic identifieri5836 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316L-lactate dehydrogenasePRO_0000168495Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi14 – 2512Combined sources
Beta strandi30 – 345Combined sources
Beta strandi36 – 394Combined sources
Helixi40 – 4910Combined sources
Helixi51 – 555Combined sources
Beta strandi61 – 644Combined sources
Helixi67 – 704Combined sources
Beta strandi74 – 785Combined sources
Helixi90 – 923Combined sources
Helixi95 – 973Combined sources
Helixi98 – 11619Combined sources
Beta strandi120 – 1245Combined sources
Beta strandi126 – 1283Combined sources
Helixi129 – 14012Combined sources
Helixi144 – 1463Combined sources
Beta strandi147 – 1504Combined sources
Helixi152 – 16716Combined sources
Helixi171 – 1733Combined sources
Beta strandi178 – 1803Combined sources
Helixi190 – 1923Combined sources
Helixi200 – 2056Combined sources
Helixi211 – 22212Combined sources
Helixi224 – 2307Combined sources
Beta strandi232 – 2343Combined sources
Helixi237 – 25115Combined sources
Beta strandi256 – 26611Combined sources
Helixi267 – 2693Combined sources
Beta strandi271 – 28212Combined sources
Beta strandi285 – 2895Combined sources
Helixi296 – 31621Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CEQX-ray2.00A1-316[»]
1CETX-ray2.05A1-316[»]
1LDGX-ray1.74A1-316[»]
1T24X-ray1.70A1-316[»]
1T25X-ray1.90A1-316[»]
1T26X-ray1.80A1-316[»]
1T2CX-ray2.01A1-316[»]
1T2DX-ray1.10A1-316[»]
1T2EX-ray1.85A1-316[»]
1U4OX-ray1.70A2-316[»]
1U4SX-ray2.00A2-316[»]
1U5AX-ray1.80A2-316[»]
1U5CX-ray2.65A2-316[»]
1XIVX-ray1.70A2-316[»]
2A94X-ray1.50A2-316[»]
4PLZX-ray1.05A1-316[»]
ProteinModelPortaliQ27743.
SMRiQ27743. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ27743.

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.
InterProiIPR001557. L-lactate/malate_DH.
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.
SUPFAMiSSF56327. SSF56327. 1 hit.

Sequencei

Sequence statusi: Complete.

Q27743-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPKAKIVLV GSGMIGGVMA TLIVQKNLGD VVLFDIVKNM PHGKALDTSH
60 70 80 90 100
TNVMAYSNCK VSGSNTYDDL AGADVVIVTA GFTKAPGKSD KEWNRDDLLP
110 120 130 140 150
LNNKIMIEIG GHIKKNCPNA FIIVVTNPVD VMVQLLHQHS GVPKNKIIGL
160 170 180 190 200
GGVLDTSRLK YYISQKLNVC PRDVNAHIVG AHGNKMVLLK RYITVGGIPL
210 220 230 240 250
QEFINNKLIS DAELEAIFDR TVNTALEIVN LHASPYVAPA AAIIEMAESY
260 270 280 290 300
LKDLKKVLIC STLLEGQYGH SDIFGGTPVV LGANGVEQVI ELQLNSEEKA
310
KFDEAIAETK RMKALA
Length:316
Mass (Da):34,108
Last modified:November 1, 1996 - v1
Checksum:iD25EB863954B8FC1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731A → S.2 Publications
Natural varianti96 – 961D → L.2 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93720 mRNA. Translation: AAA29633.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93720 mRNA. Translation: AAA29633.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CEQX-ray2.00A1-316[»]
1CETX-ray2.05A1-316[»]
1LDGX-ray1.74A1-316[»]
1T24X-ray1.70A1-316[»]
1T25X-ray1.90A1-316[»]
1T26X-ray1.80A1-316[»]
1T2CX-ray2.01A1-316[»]
1T2DX-ray1.10A1-316[»]
1T2EX-ray1.85A1-316[»]
1U4OX-ray1.70A2-316[»]
1U4SX-ray2.00A2-316[»]
1U5AX-ray1.80A2-316[»]
1U5CX-ray2.65A2-316[»]
1XIVX-ray1.70A2-316[»]
2A94X-ray1.50A2-316[»]
4PLZX-ray1.05A1-316[»]
ProteinModelPortaliQ27743.
SMRiQ27743. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ27743.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
BRENDAi1.1.1.27. 4889.
SABIO-RKQ27743.

Miscellaneous databases

EvolutionaryTraceiQ27743.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
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.
SUPFAMiSSF56327. SSF56327. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Expression of Plasmodium falciparum lactate dehydrogenase in Escherichia coli."
    Bzik D.J., Fox B.A., Gonyer K.
    Mol. Biochem. Parasitol. 59:155-166(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design."
    Dunn C., Banfield M., Barker J., Higham C., Moreton K., Turgut-Balik D., Brady L., Holbrook J.J.
    Nat. Struct. Biol. 3:912-915(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS), VARIANTS SER-73 AND LEU-96.
  3. "Chloroquine binds in the cofactor binding site of Plasmodium falciparum lactate dehydrogenase."
    Read J.A., Wilkinson K.W., Tranter R., Sessions R.B., Brady R.L.
    J. Biol. Chem. 274:10213-10218(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), VARIANTS SER-73 AND LEU-96.

Entry informationi

Entry nameiLDH_PLAFD
AccessioniPrimary (citable) accession number: Q27743
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

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

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.