Q27743 (LDH_PLAFD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: L-lactate dehydrogenase EC=1.1.1.27 Alternative name(s): LDH-P
Organism	Plasmodium falciparum (isolate CDC / Honduras)
Taxonomic identifier	5836 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania) › Plasmodium falciparum

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Glycolysis
Ligand	NAD Pyruvate
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	L-lactate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 316

316

L-lactate dehydrogenase

PRO_0000168495

Regions

Nucleotide binding

14 – 150

137

NAD

Sites

Active site

182

1

Proton acceptor

Binding site

14

1

NAD; via amide nitrogen

Binding site

15

1

NAD; via amide nitrogen

Binding site

35

1

NAD

Binding site

67

1

NAD

Binding site

81

1

NAD; via amide nitrogen

Binding site

82

1

NAD; via carbonyl oxygen

Binding site

95

1

Substrate

Binding site

125

1

NAD; via carbonyl oxygen

Binding site

127

1

NAD

Binding site

150

1

NAD; via carbonyl oxygen

Binding site

158

1

Substrate

Binding site

182

1

Substrate

Natural variations

Natural variant

73

1

A → S. Ref.2 Ref.3

Natural variant

96

1

D → L. Ref.2 Ref.3

Secondary structure

1

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316

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Helix

14 – 25

12

Beta strand

30 – 34

5

Beta strand

36 – 39

4

Helix

40 – 49

10

Helix

51 – 55

5

Beta strand

61 – 64

4

Helix

67 – 70

4

Beta strand

74 – 78

5

Helix

90 – 92

3

Helix

95 – 98

4

Helix

99 – 116

18

Beta strand

120 – 124

5

Beta strand

126 – 128

3

Helix

129 – 140

12

Helix

144 – 146

3

Beta strand

147 – 149

3

Helix

152 – 167

16

Helix

171 – 173

3

Beta strand

178 – 180

3

Helix

190 – 192

3

Helix

200 – 205

6

Helix

211 – 222

12

Helix

224 – 231

8

Beta strand

232 – 234

3

Helix

237 – 251

15

Beta strand

256 – 266

11

Helix

267 – 269

3

Beta strand

271 – 282

12

Beta strand

285 – 289

5

Helix

296 – 315

20

Sequences

	Sequence		Length	Mass (Da)
	Q27743 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D25EB863954B8FC1	FASTA	316	34,108
	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

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CEQ	X-ray	2.00	A	1-316	[»]
1CET	X-ray	2.05	A	1-316	[»]
1LDG	X-ray	1.74	A	1-316	[»]
1T24	X-ray	1.70	A	1-316	[»]
1T25	X-ray	1.90	A	1-316	[»]
1T26	X-ray	1.80	A	1-316	[»]
1T2C	X-ray	2.01	A	1-316	[»]
1T2D	X-ray	1.10	A	1-316	[»]
1T2E	X-ray	1.85	A	1-316	[»]
1U4O	X-ray	1.70	A	2-316	[»]
1U4S	X-ray	2.00	A	2-316	[»]
1U5A	X-ray	1.80	A	2-316	[»]
1U5C	X-ray	2.65	A	2-316	[»]
1XIV	X-ray	1.70	A	2-316	[»]
2A94	X-ray	1.50	A	2-316	[»]

ProteinModelPortal

Q27743.

SMR

Q27743. Positions 2-316.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

Q27743.

UniPathway

UPA00554; UER00611.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.
3.90.110.10. 1 hit.

InterPro

IPR001557. 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]

PANTHER

PTHR11540. PTHR11540. 1 hit.

Pfam

PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000102. Lac_mal_DH. 1 hit.

PRINTS

PR00086. LLDHDRGNASE.

SUPFAM

SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.

PROSITE

PS00064. L_LDH. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q27743.

EvolutionaryTrace

Q27743.

Entry information

Entry name

LDH_PLAFD

Accession

Primary (citable) accession number: Q27743

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)