LDH_LACHE
ID LDH_LACHE Reviewed; 323 AA.
AC O32765;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:9212432};
DE Short=L-LDH {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:9212432};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:9212432};
GN Name=ldh {ECO:0000255|HAMAP-Rule:MF_00488};
GN Synonyms=ldhL {ECO:0000303|PubMed:9212432};
OS Lactobacillus helveticus (Lactobacillus suntoryeus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21 AND 59-87,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=53/7;
RX PubMed=9212432; DOI=10.1128/aem.63.7.2850-2856.1997;
RA Savijoki K., Palva A.;
RT "Molecular genetic characterization of the L-lactate dehydrogenase gene
RT (ldhL) of Lactobacillus helveticus and biochemical characterization of the
RT enzyme.";
RL Appl. Environ. Microbiol. 63:2850-2856(1997).
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:9212432}.
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:9212432};
CC -!- ACTIVITY REGULATION: Under neutral conditions, the reaction is
CC stimulated 4-fold by fructose 1,6-bisphosphate (FBP), however the L-
CC lactate dehydrogenase is a nonallosteric enzyme. Calcium and zinc ions
CC at 1 mM stimulate the activity almost 2-fold. Weakly inhibited by
CC cadmium, cobalt and copper ions. {ECO:0000269|PubMed:9212432}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for pyruvate {ECO:0000269|PubMed:9212432};
CC Note=kcat is 643 sec(-1) for pyruvate as substrate.
CC {ECO:0000269|PubMed:9212432};
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:9212432};
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 ECO:0000269|PubMed:9212432}.
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; Z81318; CAB03618.1; -; Genomic_DNA.
DR RefSeq; WP_012211363.1; NZ_WCHF01000009.1.
DR AlphaFoldDB; O32765; -.
DR SMR; O32765; -.
DR STRING; 326425.lhe_1813; -.
DR eggNOG; COG0039; Bacteria.
DR OMA; ASCAEYI; -.
DR SABIO-RK; O32765; -.
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 Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9212432"
FT CHAIN 2..323
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000168348"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 83..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 122..124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 124..127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 152..155
FT /ligand="substrate"
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 323 AA; 35111 MW; 835E52465AA4C35A CRC64;
MAREEKPRKV ILVGDGAVGS TFAFSMVQQG IAEELGIIDI AKEHVEGDAI DLADATPWTS
PKNIYAADYP DCKDADLVVI TAGAPQKPGE TRLDLVNKNL KILSSIVEPV VESGFEGIFL
VVANPVDILT HATWRMSGFP KDRVIGSGTS LDTGRLQKVI GKMENVDPSS VNAYMLGEHG
DTEFPAWSYN NVAGVKVADW VKAHNMPESK LEDIHQEVKD MAYDIINKKG ATFYGIGTAS
AMIAKAILND EHRVLPLSVP MDGEYGLHDL HIGTPAVVGR KGLEQVIEMP LSDKEQELMT
ASADQLKKVM DKAFKETGVK VRQ
