ID LDH_PLAFD Reviewed; 316 AA. AC Q27743; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 120. DE RecName: Full=L-lactate dehydrogenase; DE EC=1.1.1.27; DE AltName: Full=LDH-P; OS Plasmodium falciparum (isolate CDC / Honduras). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=5836; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8515777; DOI=10.1016/0166-6851(93)90016-q; RA Bzik D.J., Fox B.A., Gonyer K.; RT "Expression of Plasmodium falciparum lactate dehydrogenase in Escherichia RT coli."; RL Mol. Biochem. Parasitol. 59:155-166(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS), AND VARIANTS SER-73 AND LEU-96. RX PubMed=8901865; DOI=10.1038/nsb1196-912; RA Dunn C., Banfield M., Barker J., Higham C., Moreton K., Turgut-Balik D., RA Brady L., Holbrook J.J.; RT "The structure of lactate dehydrogenase from Plasmodium falciparum reveals RT a new target for anti-malarial design."; RL Nat. Struct. Biol. 3:912-915(1996). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND VARIANTS SER-73 AND LEU-96. RX PubMed=10187806; DOI=10.1074/jbc.274.15.10213; RA Read J.A., Wilkinson K.W., Tranter R., Sessions R.B., Brady R.L.; RT "Chloroquine binds in the cofactor binding site of Plasmodium falciparum RT lactate dehydrogenase."; RL J. Biol. Chem. 274:10213-10218(1999). CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate CC from pyruvate: step 1/1. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M93720; AAA29633.1; -; mRNA. DR PDB; 1CEQ; X-ray; 2.00 A; A=1-316. DR PDB; 1CET; X-ray; 2.05 A; A=1-316. DR PDB; 1LDG; X-ray; 1.74 A; A=1-316. DR PDB; 1T24; X-ray; 1.70 A; A=1-316. DR PDB; 1T25; X-ray; 1.90 A; A=1-316. DR PDB; 1T26; X-ray; 1.80 A; A=1-316. DR PDB; 1T2C; X-ray; 2.01 A; A=1-316. DR PDB; 1T2D; X-ray; 1.10 A; A=1-316. DR PDB; 1T2E; X-ray; 1.85 A; A=1-316. DR PDB; 1U4O; X-ray; 1.70 A; A=2-316. DR PDB; 1U4S; X-ray; 2.00 A; A=2-316. DR PDB; 1U5A; X-ray; 1.80 A; A=2-316. DR PDB; 1U5C; X-ray; 2.65 A; A=2-316. DR PDB; 1XIV; X-ray; 1.70 A; A=2-316. DR PDB; 2A94; X-ray; 1.50 A; A=2-316. DR PDB; 4PLZ; X-ray; 1.05 A; A=1-316. DR PDBsum; 1CEQ; -. DR PDBsum; 1CET; -. DR PDBsum; 1LDG; -. DR PDBsum; 1T24; -. DR PDBsum; 1T25; -. DR PDBsum; 1T26; -. DR PDBsum; 1T2C; -. DR PDBsum; 1T2D; -. DR PDBsum; 1T2E; -. DR PDBsum; 1U4O; -. DR PDBsum; 1U4S; -. DR PDBsum; 1U5A; -. DR PDBsum; 1U5C; -. DR PDBsum; 1XIV; -. DR PDBsum; 2A94; -. DR PDBsum; 4PLZ; -. DR AlphaFoldDB; Q27743; -. DR SMR; Q27743; -. DR BindingDB; Q27743; -. DR DrugBank; DB04641; 3,7-DIHYDROXYNAPHTHALENE-2-CARBOXYLIC ACID. DR DrugBank; DB02111; 3-hydroxyisoxazole-4-carboxylic acid. DR DrugBank; DB02401; 4-Hydroxy-1,2,5-oxadiazole-3-carboxylic acid. DR DrugBank; DB03162; 4-oxo-4,5-dihydro-1,2,5-thiadiazole-3-carboxylic acid. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB04640; Naphthalene-2,6-disulfonic acid. DR DrugBank; DB03940; Oxamic Acid. DR ABCD; Q27743; 2 sequenced antibodies. DR BRENDA; 1.1.1.27; 4889. DR SABIO-RK; Q27743; -. DR UniPathway; UPA00554; UER00611. DR EvolutionaryTrace; Q27743; -. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro. DR CDD; cd01339; LDH-like_MDH; 1. DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR011275; Malate_DH_type3. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1. DR PANTHER; PTHR43128:SF34; L-LACTATE DEHYDROGENASE; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW 3D-structure; NAD; Oxidoreductase; Pyruvate. FT CHAIN 1..316 FT /note="L-lactate dehydrogenase" FT /id="PRO_0000168495" FT ACT_SITE 182 FT /note="Proton acceptor" FT BINDING 14..150 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 35 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 67 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 81 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 82 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 95 FT /ligand="substrate" FT BINDING 125 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 127 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 150 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 158 FT /ligand="substrate" FT BINDING 182 FT /ligand="substrate" FT VARIANT 73 FT /note="A -> S" FT /evidence="ECO:0000269|PubMed:10187806, FT ECO:0000269|PubMed:8901865" FT VARIANT 96 FT /note="D -> L" FT /evidence="ECO:0000269|PubMed:10187806, FT ECO:0000269|PubMed:8901865" FT STRAND 6..10 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 14..25 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 40..49 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 51..55 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:1T24" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:1CEQ" FT HELIX 98..116 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 129..140 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 147..150 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 152..167 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 200..205 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 211..222 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 224..230 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:1T26" FT HELIX 237..251 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 256..266 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 271..282 FT /evidence="ECO:0007829|PDB:4PLZ" FT STRAND 285..289 FT /evidence="ECO:0007829|PDB:4PLZ" FT HELIX 296..316 FT /evidence="ECO:0007829|PDB:4PLZ" SQ SEQUENCE 316 AA; 34108 MW; D25EB863954B8FC1 CRC64; MAPKAKIVLV GSGMIGGVMA TLIVQKNLGD VVLFDIVKNM PHGKALDTSH TNVMAYSNCK VSGSNTYDDL AGADVVIVTA GFTKAPGKSD KEWNRDDLLP LNNKIMIEIG GHIKKNCPNA FIIVVTNPVD VMVQLLHQHS GVPKNKIIGL GGVLDTSRLK YYISQKLNVC PRDVNAHIVG AHGNKMVLLK RYITVGGIPL QEFINNKLIS DAELEAIFDR TVNTALEIVN LHASPYVAPA AAIIEMAESY LKDLKKVLIC STLLEGQYGH SDIFGGTPVV LGANGVEQVI ELQLNSEEKA KFDEAIAETK RMKALA //