ID LDH2_STAA3 Reviewed; 319 AA. AC Q2FDQ7; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 116. DE RecName: Full=L-lactate dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00488}; DE Short=L-LDH 2 {ECO:0000255|HAMAP-Rule:MF_00488}; DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488}; GN Name=ldh2 {ECO:0000255|HAMAP-Rule:MF_00488}; GN OrderedLocusNames=SAUSA300_2537; OS Staphylococcus aureus (strain USA300). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate (Potential). CC Contributes to S.aureus growth during nitrosative stress in both CC aerobically and anaerobically cultured cells, despite playing a CC secondary role in this resistance mechanism (By similarity). CC {ECO:0000250|UniProtKB:Q5HCV0, ECO:0000255|HAMAP-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; CP000255; ABD22153.1; -; Genomic_DNA. DR RefSeq; WP_000846637.1; NZ_CP027476.1. DR AlphaFoldDB; Q2FDQ7; -. DR SMR; Q2FDQ7; -. DR GeneID; 98346916; -. DR KEGG; saa:SAUSA300_2537; -. DR HOGENOM; CLU_045401_1_1_9; -. DR UniPathway; UPA00554; UER00611. DR Proteomes; UP000001939; Chromosome. 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 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; Reference proteome; KW Stress response. FT CHAIN 1..319 FT /note="L-lactate dehydrogenase 2" FT /id="PRO_0000237560" FT ACT_SITE 178 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488" FT BINDING 16 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488" FT BINDING 37 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488" FT BINDING 42 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 231 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488" FT MOD_RES 222 FT /note="Phosphotyrosine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488" SQ SEQUENCE 319 AA; 34420 MW; 7779343BCA8006C4 CRC64; MKTFGKKVVL IGDGSVGSSY AFAMVTQGVA DEFVIIDIAK DKVKADVQDL NHGTVHSPSP VDVKAGEYED CKDADLVVIT AGAPQKPGET RLQLVEKNTK IMKSIVKSVM DSGFDGYFLI AANPVDILTR FVKEYTGLPA ERVIGSGTVL DSARLQYLIS QELGVAPSSV DASIIGEHGD TELAVWSQAN VAGISVYDTL KEQTGSEAKA EEIYVNTRDA AYEIIQAKGS TYYGIALALM RISKAILNNE NNVLNVSIQL DGQYGGHKGV YLGVPTLVNQ HGAVKIYEMP LSAEEQALFD KSVKTLEDTF DSIKYLLED //