ID   W8E175_9APIC            Unreviewed;       241 AA.
AC   W8E175;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00016495};
DE   Flags: Fragment;
GN   Name=ldh {ECO:0000313|EMBL:AHJ59785.1};
OS   Plasmodium sp. WL-2014a.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium.
OX   NCBI_TaxID=1462435 {ECO:0000313|EMBL:AHJ59785.1};
RN   [1] {ECO:0000313|EMBL:AHJ59785.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DGptt540_LDH_SGA5.94 {ECO:0000313|EMBL:AHJ59785.1};
RX   PubMed=24557500; DOI=10.1038/ncomms4346;
RA   Sundararaman S.A., Plenderleith L.J., Liu W., Loy E., Learn G.H., Li Y.,
RA   Shaw K.S., Ayouba A., Peeters M., Speede S., Shaw G.M., Bushman F.D.,
RA   Brisson D., Rayner J.C., Sharp P.M., Hahn B.H.;
RT   "African origin of the malaria parasite Plasmodium vivax.";
RL   Nat. Commun. 5:3346-3346(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; KF618584; AHJ59785.1; -; Genomic_DNA.
DR   AlphaFoldDB; W8E175; -.
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   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   Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT   DOMAIN          3..94
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          99..240
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AHJ59785.1"
FT   NON_TER         241
FT                   /evidence="ECO:0000313|EMBL:AHJ59785.1"
SQ   SEQUENCE   241 AA;  26165 MW;  DE27375368757465 CRC64;
     YSNCKVTGSN SYDDLKGADV VIVTAGFTKA PGKSDKEWNR DDLLPLNNKI MIEIGGHIKN
     LCPNAFIIVV TNPVDVMVQL LFEHSGVPKN KIIGLGGVLD TSRLKYYISQ KLNVCPRDVN
     ALIVGAHGNK MVLLKRYITV GGIPLQEFIN NKKITDEEVE AIFDRTVNTA LEIVNLLASP
     YVAPAAAIIE MAESYLKDIK KVLVCSTLLE GQYGHSNIFG GTPLVIGGTG VEQVIELQLN
     A
//