ID LDH2_BACC1 Reviewed; 314 AA. AC P62048; DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2004, sequence version 1. DT 02-SEP-2026, entry version 129. 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=BCE_5032; OS Bacillus cereus (strain ATCC 10987 / NRS 248). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=222523; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10987 / NRS 248; RX PubMed=14960714; DOI=10.1093/nar/gkh258; RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.; RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic RT adaptations and a large plasmid related to Bacillus anthracis pXO1."; RL Nucleic Acids Res. 32:977-988(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(+) = 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 -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6- CC bisphosphate (FBP). {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}. 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; AE017194; AAS43933.1; -; Genomic_DNA. DR AlphaFoldDB; P62048; -. DR SMR; P62048; -. DR KEGG; bca:BCE_5032; -. DR HOGENOM; CLU_045401_1_1_9; -. DR UniPathway; UPA00554; UER00611. 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; 3.90.110.10:FF:000005; L-lactate dehydrogenase; 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 Allosteric enzyme; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein. FT CHAIN 1..314 FT /note="L-lactate dehydrogenase 2" FT /id="PRO_0000168319" 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 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 156 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488" FT BINDING 171 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" 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 314 AA; 34606 MW; 82075E6DCC076A76 CRC64; MKKGINRVVL VGTGAVGCSY AYSMINQGVA EEFVLVDVNE AKAEGEAMDL SHAVPFSPSP TKVWSGSYAD CKDADLVVIT AGLPQKPGET RLDLVEKNTK IFKQIVRGIM DSGFDGIFLI ATNPVDILTY VTWKESGLPK ERVIGSGTTL DSARFRYMLG DYLDVDPRNV HAYIVGEHGD TELPVWSHAT IGVQKLETIL ANNEQYKQED LDKIFENVRD AAYHIIERKG ATYYGIGMSL LRVTKAILNN ENSVLTVSAY LEGQYGEKDA YVGVPAVINR EGVREIVELE LNEDEKAKFA HSVKVLKETM APVL //