LDH_LACLN
ID LDH_LACLN Reviewed; 314 AA.
AC D8KFT1; A2RIA3; Q7WYP6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00488};
DE Short=L-LDH {ECO:0000255|HAMAP-Rule:MF_00488};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN Name=ldh {ECO:0000255|HAMAP-Rule:MF_00488};
GN Synonyms=ldhB {ECO:0000303|PubMed:12867459}; OrderedLocusNames=LLNZ_02045;
OS Lactococcus lactis subsp. cremoris (strain NZ9000).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=746361;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=NZ9000;
RX PubMed=12867459; DOI=10.1128/jb.185.15.4499-4507.2003;
RA Bongers R.S., Hoefnagel M.H.N., Starrenburg M.J.C., Siemerink M.A.J.,
RA Arends J.G.A., Hugenholtz J., Kleerebezem M.;
RT "IS981-mediated adaptive evolution recovers lactate production by ldhB
RT transcription activation in a lactate dehydrogenase-deficient strain of
RT Lactococcus lactis.";
RL J. Bacteriol. 185:4499-4507(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ9000;
RX PubMed=20639323; DOI=10.1128/jb.00533-10;
RA Linares D.M., Kok J., Poolman B.;
RT "Genome sequences of Lactococcus lactis MG1363 (revised) and NZ9000 and
RT comparative physiological studies.";
RL J. Bacteriol. 192:5806-5812(2010).
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 ECO:0000269|PubMed:12867459};
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}.
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DR EMBL; AY230155; AAO60056.1; -; Genomic_DNA.
DR EMBL; CP002094; ADJ59411.1; -; Genomic_DNA.
DR RefSeq; WP_011834445.1; NC_017949.1.
DR AlphaFoldDB; D8KFT1; -.
DR SMR; D8KFT1; -.
DR KEGG; lln:LLNZ_02045; -.
DR PATRIC; fig|746361.3.peg.404; -.
DR HOGENOM; CLU_045401_1_1_9; -.
DR OMA; RVIGNGC; -.
DR OrthoDB; 870724at2; -.
DR BioCyc; LLAC746361:LLNZ_RS02020-MON; -.
DR SABIO-RK; D8KFT1; -.
DR UniPathway; UPA00554; UER00611.
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 1: Evidence at protein level;
KW Allosteric enzyme; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein.
FT CHAIN 1..314
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000402184"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 42
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 104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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"
SQ SEQUENCE 314 AA; 34398 MW; 9D5114712ACB75A4 CRC64;
MKITSRKVVV IGTGFVGTSI AYSMINQGLV NELVLIDVNQ DKAEGEALDL LDGISWAQEN
VIVRAGNYKD CENADIVVIT AGVNQKPGQS RLDLVNTNAK IMRSIVTQVM DSGFDGIFVI
ASNPVDILTY VAWETSGLDQ SRIVGTGTTL DTTRFRKELA TKLEIDPRSV HGYIIGEHGD
SEVAVWSHTT IGGKPILEFI VKNKKIGLED LSNLSNKVKN AAYEIIDKKQ ATYYGIGMST
ARIVKAILNN EQVILPVSAY LRGEYGQEGV FTGVPSVVNQ NGVREIIELN IDAYEMKQFE
KSVSQLKEVI ESIK
