ID   LDH_BOTBR               Reviewed;         316 AA.
AC   P93052; Q7M1E9;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=L-lactate dehydrogenase;
DE            Short=LDH;
DE            EC=1.1.1.27;
OS   Botryococcus braunii (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Elliptochloris clade; Botryococcus.
OX   NCBI_TaxID=38881;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Race A;
RA   Vioque J., Sirakova T., Kolattukudy P.E.;
RT   "Malate dehydrogenase gene from Botryococcus braunii.";
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-27.
RX   PubMed=7649295; DOI=10.1016/0014-5793(95)00781-4;
RA   Wang X., Kolattukudy P.E.;
RT   "Solubilization and purification of aldehyde-generating fatty acyl-CoA
RT   reductase from green alga Botryococcus braunii.";
RL   FEBS Lett. 370:15-18(1995).
RN   [3]
RP   PROBABLE FUNCTION.
RX   PubMed=11435413; DOI=10.1101/gr.gr-1776r;
RA   Louis A., Ollivier E., Aude J.-C., Risler J.-L.;
RT   "Massive sequence comparisons as a help in annotating genomic sequences.";
RL   Genome Res. 11:1296-1303(2001).
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   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally (Ref.1) thought to be a malate dehydrogenase or
CC       an NADH-dependent acyl-CoA reductase. {ECO:0000305|PubMed:7649295}.
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DR   EMBL; U80676; AAB38970.1; -; Genomic_DNA.
DR   AlphaFoldDB; P93052; -.
DR   SMR; P93052; -.
DR   BioCyc; MetaCyc:MON-17304; -.
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   HAMAP; MF_00487; Malate_dehydrog_3; 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.
DR   TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..316
FT                   /note="L-lactate dehydrogenase"
FT                   /id="PRO_0000168492"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..39
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        6
FT                   /note="Y -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="G -> W (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   316 AA;  32875 MW;  436AC40FB7A07A19 CRC64;
     MARKKYALIG AGNIGGTLAH LAALKGLGDI VLFDVVEGVP QGKALDLSQC GPVEGFDANI
     KGSNDYADIA GADVIIVTAG VARKPGMSRD DLLGINLKVM KAVGEGIRDN APDAFVICIT
     NPLDAMVWAL REFSGLPANK VVGMAGVLDS GRFSHFLAEE FGVSVNSVLG GHGDNMVPVL
     EYSTVSGIPV SELIEMGFST KEKVDEIIKR TRGGGGEIVA LLKTGSAYYA PATSGIAMAE
     AYLYDQKRIL PAAAHLSGEY GIDNLYVGVP VVIGANGVEK VVEVKLSDEA KANLQVSVDA
     VKELLVACKG IDESLA