ID LDH1_STAA1 Reviewed; 317 AA. AC A7WXP7; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 02-SEP-2026, entry version 101. 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 OrderedLocusNames=SAHV_0240; OS Staphylococcus aureus (strain Mu3 / ATCC 700698). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=418127; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu3 / ATCC 700698; RX PubMed=17954695; DOI=10.1128/aac.00534-07; RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.; RT "Mutated response regulator graR is responsible for phenotypic conversion RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate RT resistance to vancomycin-intermediate resistance."; RL Antimicrob. Agents Chemother. 52:45-53(2008). CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate (Potential). CC Appears to be the primary factor that allows S.aureus growth during CC nitrosative stress in both aerobically and anaerobically cultured cells CC (By similarity). {ECO:0000250|UniProtKB:Q5HJD7, ECO:0000255|HAMAP- CC Rule:MF_00488}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-lactate + NAD(+) = pyruvate + NADH + H(+); 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP009324; BAF77123.1; -; Genomic_DNA. DR RefSeq; WP_001031880.1; NC_009782.1. DR AlphaFoldDB; A7WXP7; -. DR SMR; A7WXP7; -. DR KEGG; saw:SAHV_0240; -. DR HOGENOM; CLU_045401_1_1_9; -. DR UniPathway; UPA00554; UER00611. DR AbasyAtlas; A7WXP7; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR GO; GO:0006089; P:lactate metabolic process; IEA:TreeGrafter. DR CDD; cd05291; HicDH_like; 1. DR FunFam; 3.40.50.720:FF:000018; Malate dehydrogenase; 1. DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01771; L-LDH-NAD; 1. DR NCBIfam; NF000824; PRK00066.1; 1. DR NCBIfam; NF004863; PRK06223.1; 1. DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1. DR PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1. 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; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00064; L_LDH; 1. PE 3: Inferred from homology; KW Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Stress response. FT CHAIN 1..317 FT /note="L-lactate dehydrogenase 1" FT /id="PRO_0000343838" FT ACT_SITE 179 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 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 317 AA; 34569 MW; CDDE4813AF6CB226 CRC64; MNKFKGNKVV LIGNGAVGSS YAFSLVNQSI VDELVIIDLD TEKVRGDVMD LKHATPYSPT TVRVKAGEYS DCHDADLVVI CAGAAQKPGE TRLDLVSKNL KIFKSIVGEV MASKFDGIFL VATNPVDILA YATWKFSGLP KERVIGSGTI LDSARFRLLL SEAFDVAPRS VDAQIIGEHG DTELPVWSHA NIAGQPLKTL LEQRPEGKAQ IEQIFVQTRD AAYDIIQAKG ATYYGVAMGL ARITEAIFRN EDAVLTVSAL LEGEYDEEDV YIGVPAVINR NGIRNVVEIP LNDEEQSKFA HSAKTLKDIM AEAEELK //