Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q27743 (LDH_PLAFD) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase

EC=1.1.1.27
Alternative name(s):
LDH-P
OrganismPlasmodium falciparum (isolate CDC / Honduras)
Taxonomic identifier5836 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandNAD
Pyruvate
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionL-lactate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316L-lactate dehydrogenase
PRO_0000168495

Regions

Nucleotide binding14 – 150137NAD

Sites

Active site1821Proton acceptor
Binding site141NAD; via amide nitrogen
Binding site151NAD; via amide nitrogen
Binding site351NAD
Binding site671NAD
Binding site811NAD; via amide nitrogen
Binding site821NAD; via carbonyl oxygen
Binding site951Substrate
Binding site1251NAD; via carbonyl oxygen
Binding site1271NAD
Binding site1501NAD; via carbonyl oxygen
Binding site1581Substrate
Binding site1821Substrate

Natural variations

Natural variant731A → S. Ref.2 Ref.3
Natural variant961D → L. Ref.2 Ref.3

Secondary structure

......................................................... 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q27743 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D25EB863954B8FC1

FASTA31634,108
        10         20         30         40         50         60 
MAPKAKIVLV GSGMIGGVMA TLIVQKNLGD VVLFDIVKNM PHGKALDTSH TNVMAYSNCK 

        70         80         90        100        110        120 
VSGSNTYDDL AGADVVIVTA GFTKAPGKSD KEWNRDDLLP LNNKIMIEIG GHIKKNCPNA 

       130        140        150        160        170        180 
FIIVVTNPVD VMVQLLHQHS GVPKNKIIGL GGVLDTSRLK YYISQKLNVC PRDVNAHIVG 

       190        200        210        220        230        240 
AHGNKMVLLK RYITVGGIPL QEFINNKLIS DAELEAIFDR TVNTALEIVN LHASPYVAPA 

       250        260        270        280        290        300 
AAIIEMAESY LKDLKKVLIC STLLEGQYGH SDIFGGTPVV LGANGVEQVI ELQLNSEEKA 

       310 
KFDEAIAETK RMKALA 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93720 mRNA. Translation: AAA29633.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ27743.
SMRQ27743. Positions 2-316.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ27743.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ27743.
UniPathwayUPA00554; UER00611.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR001557. 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]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ27743.

Entry information

Entry nameLDH_PLAFD
AccessionPrimary (citable) accession number: Q27743
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways