ID A0A2S0D668_PLAVI Unreviewed; 316 AA. AC A0A2S0D668; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 25-MAY-2022, entry version 9. 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 -!- 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 VEuPathDB; PlasmoDB:PVP01_1229400; -. 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; -; 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 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}. FT DOMAIN 6..149 FT /note="Ldh_1_N" FT /evidence="ECO:0000259|Pfam:PF00056" FT DOMAIN 154..310 FT /note="Ldh_1_C" FT /evidence="ECO:0000259|Pfam:PF02866" FT ACT_SITE 182 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1" FT BINDING 95 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 127 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 158 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" 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 //