LDH1_LACLA
ID LDH1_LACLA Reviewed; 325 AA.
AC Q01462;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=L-lactate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00488};
DE Short=L-LDH 1 {ECO:0000255|HAMAP-Rule:MF_00488};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN Name=ldh1 {ECO:0000255|HAMAP-Rule:MF_00488}; Synonyms=ldh, ldhA;
GN OrderedLocusNames=LL1331; ORFNames=L0017;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LM0230;
RX PubMed=1400245; DOI=10.1128/jb.174.21.6956-6964.1992;
RA Llanos R.M., Hillier A.J., Davidson B.E.;
RT "Cloning, nucleotide sequence, expression, and chromosomal location of ldh,
RT the gene encoding L-(+)-lactate dehydrogenase, from Lactococcus lactis.";
RL J. Bacteriol. 174:6956-6964(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1452029; DOI=10.1016/0378-1119(92)90049-u;
RA Griffin H.G., Swindell S.R., Gasson M.G.;
RT "Cloning and sequence analysis of the gene encoding L-lactate dehydrogenase
RT from Lactococcus lactis: evolutionary relationships between 21 different
RT LDH enzymes.";
RL Gene 122:193-197(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BU2-60, and IL1403;
RX PubMed=8081494; DOI=10.1099/00221287-140-6-1301;
RA Swindell S.R., Griffin H.G., Gasson M.J.;
RT "Cloning, sequencing and comparison of three lactococcal L-lactate
RT dehydrogenase genes.";
RL Microbiology 140:1301-1305(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1117M, 112, BEN121, and BO34;
RX PubMed=9023947; DOI=10.1128/aem.63.2.694-702.1997;
RA Urbach E., Daniels B., Salama M.S., Sandine W.E., Giovannoni S.J.;
RT "The ldh phylogeny for environmental isolates of Lactococcus lactis is
RT consistent with rRNA genotypes but not with phenotypes.";
RL Appl. Environ. Microbiol. 63:694-702(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000255|HAMAP-Rule:MF_00488}.
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:0000255|HAMAP-Rule:MF_00488};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC bisphosphate (FBP). {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305}.
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DR EMBL; M95919; AAA25172.1; -; Genomic_DNA.
DR EMBL; M88490; AAA25187.1; -; Genomic_DNA.
DR EMBL; L07920; AAA99896.1; -; Genomic_DNA.
DR EMBL; U04315; AAA61963.1; -; Genomic_DNA.
DR EMBL; U02386; AAA61962.1; -; Genomic_DNA.
DR EMBL; U78632; AAB51676.1; -; Genomic_DNA.
DR EMBL; U78636; AAB51680.1; -; Genomic_DNA.
DR EMBL; U78637; AAB51681.1; -; Genomic_DNA.
DR EMBL; U78638; AAB51682.1; -; Genomic_DNA.
DR EMBL; U78634; AAB51678.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05429.1; -; Genomic_DNA.
DR PIR; A45246; A45246.
DR PIR; C86791; C86791.
DR PIR; JN0449; JN0449.
DR RefSeq; NP_267487.1; NC_002662.1.
DR RefSeq; WP_003131075.1; NC_002662.1.
DR AlphaFoldDB; Q01462; -.
DR SMR; Q01462; -.
DR STRING; 272623.L0017; -.
DR PaxDb; Q01462; -.
DR EnsemblBacteria; AAK05429; AAK05429; L0017.
DR GeneID; 60355791; -.
DR GeneID; 61109609; -.
DR GeneID; 66442314; -.
DR KEGG; lla:L0017; -.
DR PATRIC; fig|272623.7.peg.1438; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_1_1_9; -.
DR OMA; ASCAEYI; -.
DR SABIO-RK; Q01462; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_00488; Lactate_dehydrog; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR011304; L-lactate_DH.
DR InterPro; IPR018177; L-lactate_DH_AS.
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; 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; TIGR01771; L-LDH-NAD; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..325
FT /note="L-lactate dehydrogenase 1"
FT /id="PRO_0000168351"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 43
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 82..83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 121..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 123..126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 151..154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 156
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 171
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT MOD_RES 223
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT CONFLICT 270
FT /note="C -> F (in Ref. 1; AAA25172/AAA99896 and 4;
FT AAB51678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 35051 MW; 8BFA78343AF13003 CRC64;
MADKQRKKVI LVGDGAVGSS YAFALVNQGI AQELGIVDLF KEKTQGDAED LSHALAFTSP
KKIYSADYSD ASDADLVVLT SGAPQKPGET RLDLVEKNLR ITKDVVTKIV ASGFKGIFLV
AANPVDILTY ATWKFSGFPK NRVVGSGTSL DTARFRQALA EKVDVDARSI HAYIMGEHGD
SEFAVWSHAN VAGVKLEQWF QENDYLNEAE IVELFESVRD AAYSIIAKKG ATFYGVAVAL
ARITKAILDD EHAVLPVSVF QDGQYGVSDC YLGQPAVVGA EGVVNPIHIP LNDAEMQKME
ASGAQLKAII DEAFAKEEFA SAVKN
