LDH_PLAFD
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 03-AUG-2022, entry version 117.
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}.
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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; -; 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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 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
