LDH1_LACPL
ID LDH1_LACPL Reviewed; 320 AA.
AC P56512; F9UL11; P26299; Q8GMW6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
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};
GN Synonyms=l-ldhL, ldh, ldhL, ldhL1; OrderedLocusNames=lp_0537;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DG301;
RX PubMed=8300514; DOI=10.1128/jb.176.3.596-601.1994;
RA Ferain T., Garmyn D., Bernard N., Hols P., Delcour J.;
RT "Lactobacillus plantarum ldhL gene: overexpression and deletion.";
RL J. Bacteriol. 176:596-601(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=L137;
RA Kim J., Tsutsui M., Yamashita M., Murooka Y.;
RT "Expression of Derf 7 gene in Lactobacillus plantarum.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-320.
RA Ham J., Kim H., Kim H.;
RT "Expression of LDH gene in Candida kefyr isolated from Mongolian Koumiss.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD16691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X70926; CAA50277.1; -; Genomic_DNA.
DR EMBL; AB177763; BAD16691.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL935263; CCC78026.1; -; Genomic_DNA.
DR EMBL; AF548372; AAN40797.1; -; Genomic_DNA.
DR PIR; A36957; A36957.
DR RefSeq; WP_003642078.1; NC_004567.2.
DR RefSeq; YP_004888540.1; NC_004567.2.
DR AlphaFoldDB; P56512; -.
DR SMR; P56512; -.
DR STRING; 220668.lp_0537; -.
DR EnsemblBacteria; CCC78026; CCC78026; lp_0537.
DR GeneID; 57024312; -.
DR GeneID; 66448588; -.
DR KEGG; lpl:lp_0537; -.
DR PATRIC; fig|220668.9.peg.444; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_1_1_9; -.
DR OMA; ASCAEYI; -.
DR PhylomeDB; P56512; -.
DR BioCyc; LPLA220668:G1GW0-447-MON; -.
DR BRENDA; 1.1.1.27; 2849.
DR SABIO-RK; P56512; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000000432; 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 Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..320
FT /note="L-lactate dehydrogenase 1"
FT /id="PRO_0000168357"
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 44
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"
FT CONFLICT 54
FT /note="D -> H (in Ref. 1; CAA50277)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="K -> Q (in Ref. 2; BAD16691)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="S -> C (in Ref. 1; CAA50277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 34206 MW; 34B8A5FD12A64EBC CRC64;
MSSMPNHQKV VLVGDGAVGS SYAFAMAQQG IAEEFVIVDV VKDRTKGDAL DLEDAQAFTA
PKKIYSGEYS DCKDADLVVI TAGAPQKPGE SRLDLVNKNL NILSSIVKPV VDSGFDGIFL
VAANPVDILT YATWKFSGFP KDRVIGSGTS LDSSRLRVAL GKQFNVDPRS VDAYIMGEHG
DSEFAAYSTA TIGTRPVRDV AKEQGVSDED LAKLEDGVRN KAYDIINLKG ATFYGIGTAL
MRISKAILRD ENAVLPVGAY MDGQYGLNDI YIGTPAVIGG TGLKQIIESP LSADELKKMQ
DSAATLKKVL NDGLAELENK
