LDH_LACPE
ID LDH_LACPE Reviewed; 320 AA.
AC P56511; P26299;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:1840590};
DE Short=L-LDH {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:1840590};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1425707};
GN Name=ldh {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:1840590};
GN Synonyms=ldhL {ECO:0000303|PubMed:1840590};
OS Lactiplantibacillus pentosus (Lactobacillus pentosus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1589;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-24, AND SUBUNIT.
RC STRAIN=ATCC 8041 / DSM 20314 / BCRC 11053 / JCM 1558 / KCTC 3120 / LMG
RC 10755 / NBRC 106467 / NCDO 363 / NCIMB 8026 / 124-2;
RX PubMed=1840590; DOI=10.1016/s0021-9258(18)98939-8;
RA Ohta T., Taguchi H.;
RT "D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid
RT dehydrogenase family. Cloning, sequencing, and expression in Escherichia
RT coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum.";
RL J. Biol. Chem. 266:12588-12594(1991).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP ASP-172, ACTIVITY REGULATION, AND ACTIVE SITE.
RC STRAIN=ATCC 8041 / DSM 20314 / BCRC 11053 / JCM 1558 / KCTC 3120 / LMG
RC 10755 / NBRC 106467 / NCDO 363 / NCIMB 8026 / 124-2;
RX PubMed=1425707; DOI=10.1111/j.1432-1033.1992.tb17373.x;
RA Taguchi H., Ohta T.;
RT "Unusual amino acid substitution in the anion-binding site of Lactobacillus
RT plantarum non-allosteric L-lactate dehydrogenase.";
RL Eur. J. Biochem. 209:993-998(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD, ACTIVE SITE,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=11807949; DOI=10.1002/prot.1165;
RA Uchikoba H., Fushinobu S., Wakagi T., Konno M., Taguchi H., Matsuzawa H.;
RT "Crystal structure of non-allosteric L-lactate dehydrogenase from
RT Lactobacillus pentosus at 2.3 A resolution: specific interactions at
RT subunit interfaces.";
RL Proteins 46:206-214(2002).
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1425707}.
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:1425707};
CC -!- ACTIVITY REGULATION: The quaternary structure is constitutionally
CC similar to the active conformation of allosteric LDHs, and the
CC regulation is independent of the fructose 1,6-bisphosphate-binding
CC site. {ECO:0000269|PubMed:11807949, ECO:0000269|PubMed:1425707}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for pyruvate (at pH 5) {ECO:0000269|PubMed:1425707};
CC Vmax=1650 umol/min/mg enzyme for pyruvate (at pH 5)
CC {ECO:0000269|PubMed:1425707};
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:11807949, ECO:0000305|PubMed:1840590}.
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}.
CC -!- CAUTION: Was originally (PubMed:1840590 and PubMed:1425707) thought to
CC originate from L.plantarum. {ECO:0000305}.
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DR EMBL; D90340; BAA14353.1; -; Genomic_DNA.
DR PIR; B40885; B40885.
DR RefSeq; WP_050337700.1; NZ_WHJB01000026.1.
DR PDB; 1EZ4; X-ray; 2.30 A; A/B/C/D=3-319.
DR PDBsum; 1EZ4; -.
DR AlphaFoldDB; P56511; -.
DR SMR; P56511; -.
DR STRING; 1589.GCA_001188985_00048; -.
DR GeneID; 49392872; -.
DR SABIO-RK; P56511; -.
DR UniPathway; UPA00554; UER00611.
DR EvolutionaryTrace; P56511; -.
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 3D-structure; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase;
KW Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1840590"
FT CHAIN 2..320
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000168356"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000305|PubMed:11807949, ECO:0000305|PubMed:1425707,
FT ECO:0007744|PDB:1EZ4"
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 ECO:0000269|PubMed:11807949, ECO:0007744|PDB:1EZ4"
FT BINDING 44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000269|PubMed:11807949, ECO:0007744|PDB:1EZ4"
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 ECO:0000269|PubMed:11807949, ECO:0007744|PDB:1EZ4"
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 ECO:0000269|PubMed:11807949, ECO:0007744|PDB:1EZ4"
FT BINDING 122..124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000269|PubMed:11807949, ECO:0007744|PDB:1EZ4"
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 ECO:0000269|PubMed:11807949, ECO:0007744|PDB:1EZ4"
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"
FT MUTAGEN 172
FT /note="D->H: Shows a significant FBP-induced
FT thermostabilization as in the cases of many allosteric
FT LDHs, indicating the binding of fructose 1,6-bisphosphate
FT (FBP). However, the mutant is still a non-allosteric enzyme
FT and shows essentially the same FBP-independent catalytic
FT activity as the wild-type."
FT /evidence="ECO:0000269|PubMed:1425707"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 208..229
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 268..279
FT /evidence="ECO:0007829|PDB:1EZ4"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:1EZ4"
FT HELIX 293..317
FT /evidence="ECO:0007829|PDB:1EZ4"
SQ SEQUENCE 320 AA; 34220 MW; 03A413F98C186BA1 CRC64;
MSSMPNHQKV VLVGDGAVGS SYAFAMAQQG IAEEFVIVDV VKDRTKGDAL DLEDAQAFTA
PKKIYSGEYS DCKDADLVVI TAGAPQKPGE SRLDLVNKNL NILSSIVKPV VDSGFDGIFL
VAANPVDILT YATWKFSGFP KERVIGSGTS LDSSRLRVAL GKQFNVDPRS VDAYIMGEHG
DSEFAAYSTA TIGTRPVRDV AKEQGVSDDD LAKLEDGVRN KAYDIINLKG ATFYGIGTAL
MRISKAILRD ENAVLPVGAY MDGQYGLNDI YIGTPAIIGG TGLKQIIESP LSADELKKMQ
DSAATLKKVL NDGLAELENK
