ID   LDH_PLABE               Reviewed;         316 AA.
AC   P84793; Q4Z783;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=L-lactate dehydrogenase;
DE            EC=1.1.1.27;
OS   Plasmodium berghei.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5821;
RN   [1] {ECO:0000312|EMBL:AAR99063.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NK65 {ECO:0000312|EMBL:AAR99063.1};
RA   Matuschewski K., Brown S.M., Nussenzweig V., Kappe S.H.I.;
RT   "A screen for stage-specific gene expression in Plasmodium oocyst
RT   sporozoites.";
RL   Submitted (OCT-2003) 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:0000250|UniProtKB:Q7SI97};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q7SI97}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000255}.
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; AY437808; AAR99063.1; -; Genomic_DNA.
DR   AlphaFoldDB; P84793; -.
DR   SMR; P84793; -.
DR   VEuPathDB; PlasmoDB:PBANKA_1340100; -.
DR   OMA; ASCAEYI; -.
DR   UniPathway; UPA00554; UER00611.
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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Pyruvate.
FT   CHAIN           1..316
FT                   /note="L-lactate dehydrogenase"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000227538"
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
FT   BINDING         13..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
FT   BINDING         34..36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
FT   BINDING         67
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
FT   BINDING         79..83
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
FT   BINDING         125..127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
FT   BINDING         150
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
FT   BINDING         182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SI97"
SQ   SEQUENCE   316 AA;  34424 MW;  582283BBAF946F26 CRC64;
     MAPKAKIVLV GSGMIGGVMA TLIVQKNLGD VVMFDIVKNM PHGKALDTSH TNVMAYSNCK
     VSGSNTYDDL KDADVVIVTA GFTKAPGKSD KEWNRDDLLP LNNKIMIEIG GHIKNNCPNA
     FIIVVTNPVD VMVQLLHQHS GVPKNKIVGL GGVLDTSRLK YYISQKLNVC PRDVNAHIVG
     AHGNKMVLLK RYITVGGIPL QEFINNKKIT DQELDAIFDR TINTALEIVN LHASPYVAPA
     AAIIEMAESY IRDLRKVLIC STLLEGQYGH KDIFAGTPLV IGGNGVEQVI ELQLNADEKK
     KFDEAVAETS RMKALI