ID G5D071_PLAVI Unreviewed; 316 AA.
AC G5D071;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00016495};
GN Name=ldh {ECO:0000313|EMBL:AEP83562.1};
OS Plasmodium vivax (malaria parasite P. vivax).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5855 {ECO:0000313|EMBL:AEP83562.1};
RN [1] {ECO:0000313|EMBL:AEP83562.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ori-1 {ECO:0000313|EMBL:AEP83562.1};
RX PubMed=24953504; DOI=10.1016/j.meegid.2014.06.004;
RA Keluskar P., Singh V., Gupta P., Ingle S.;
RT "Plasmodium falciparum and Plasmodium vivax specific lactate dehydrogenase:
RT Genetic polymorphism study from Indian isolates.";
RL Infect. Genet. Evol. 26:313-322(2014).
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 Evidence={ECO:0000256|ARBA:ARBA00001763};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|RuleBase:RU003369}.
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DR EMBL; JN547221; AEP83562.1; -; Genomic_DNA.
DR AlphaFoldDB; G5D071; -.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT DOMAIN 6..149
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 154..311
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 125..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 316 AA; 34332 MW; 3906AF9E10D5E939 CRC64;
MTPKPKIVLV GSGMIGGVRA TLIVQKNLWD VVMFDVVKNM PQGKALDMSH SNVMAYSNCK
VTGSNSYDDL KGADVVIVTA GFTKAPGKGN KEWNRDDLLP LNNKIMIEIG GHIKNLCPNA
FIIVVTNPVD VMVQLLFEHS GVPKNKIIGL GGVLDTSRLK YYISQKLNVC PRDVNALIVG
AHGNKIVLLK RYITVGGIPL QEFINNKKIT DEEVEGIFDR TVNTASEIVN LLASPYVAPA
AAIIEMAESY LKDIKKVLVC STLLEGQYGH SNIFGGTPLV IGGTGVEQVI ELQLNAEEKT
KFDEAVAETK RMKALI
//
