ID A0A2S0D668_PLAVI Unreviewed; 316 AA. AC A0A2S0D668; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 03-MAY-2023, entry version 13. DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00016495}; 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:ARE68696.1}; RN [1] {ECO:0000313|EMBL:ARE68696.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=VMM2 {ECO:0000313|EMBL:ARE68696.1}; RA Na B.-K., Kim T.I., Kang J.-M., Lee J.; RT "Lactate dehydrogenases of Plasmodium vivax and Plasmodium falciparum RT Myanmar isolates."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. 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}. 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; KX885924; ARE68696.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2S0D668; -. DR VEuPathDB; PlasmoDB:PVP01_1229400; -. DR VEuPathDB; PlasmoDB:PVW1_120043900; -. DR VEuPathDB; PlasmoDB:PVX_116615; -. 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:SF16; 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..310 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; 34164 MW; 6D5CE21BFB91C910 CRC64; MTPKPKIVLV GSGMIGGVMA TLIVQKNLGD VVMFDVVKNM PQGKALDTSH SNVMAYSNCK VTGSNSCDDL KGADVVIVTA GFTKAPGKSD KEWNRDDLLP LNNKIMIEIG GHIKNLCPNA FIIVVTNPVD VMVQLLFEHS GVPKNKIIGL GGVLDTSRLK YYISQKLNVC PRDVNALIVG AHGNKMVLLK RYITVGGIPL QEFINNKKIT DEEVEGIFDR TVNTALEIVN LLASPYVAPA AAIIEMAESY LKDIKKVLVC STLLEGQYGH SNIFGGTPLV IGGTGVEQVI ELQLNAEEKT EFDEAVAETK RMKALI //