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LDH1_LACJO
ID   LDH1_LACJO              Reviewed;         323 AA.
AC   P62052;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 131.
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}; OrderedLocusNames=LJ_0274;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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}.
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DR   EMBL; AE017198; AAS08257.1; -; Genomic_DNA.
DR   RefSeq; WP_004898900.1; NC_005362.1.
DR   AlphaFoldDB; P62052; -.
DR   SMR; P62052; -.
DR   STRING; 257314.LJ_0274; -.
DR   EnsemblBacteria; AAS08257; AAS08257; LJ_0274.
DR   GeneID; 64333080; -.
DR   GeneID; 66434604; -.
DR   KEGG; ljo:LJ_0274; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_1_1_9; -.
DR   OMA; ASCAEYI; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000000581; 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..323
FT                   /note="L-lactate dehydrogenase 1"
FT                   /id="PRO_0000168349"
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         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         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;  35079 MW;  B45657BECF852F85 CRC64;
     MSEEKIHKII LVGDGAVGST YAFSLVQQGI AQELGIVDIV KERTQGDAID LADATPWIAP
     KTIYSAEYSD AKDADLVVIS AGAPQKPGET RLDLVNKNLK ILSSIVEPIV ESGFNGIFLV
     AANPVDILTH ATWRMSGFPK DRVIGSGTSL DTGRLQKVIG EMEHVDPRSV NAYMLGEHGD
     TEFPVWSYNN VGGVKVSDWV KAHPEVGENK LEAIHKEVAD MAYDIINKKG ATFYGIGTAL
     AFITKAILNN EHRVLPLSVP MDGEYGLHDI HIGTPAVVGR HGLEQVIEMP LNADEQAKME
     ASAKQLKEVM DKAFKETGVK VRQ
 
 
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