ID A0A160VM29_PROFR Unreviewed; 321 AA. AC A0A160VM29; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 03-AUG-2022, entry version 21. DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967}; DE EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967}; GN Name=ldh {ECO:0000313|EMBL:CUW15044.1}; GN ORFNames=PFREUDJS001_001231 {ECO:0000313|EMBL:CUW15044.1}; OS Propionibacterium freudenreichii subsp. shermanii. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Propionibacterium. OX NCBI_TaxID=1752 {ECO:0000313|EMBL:CUW15044.1, ECO:0000313|Proteomes:UP000076747}; RN [1] {ECO:0000313|Proteomes:UP000076747} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Laine P.K.S.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00001763}; CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate CC from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC {ECO:0000256|ARBA:ARBA00006054}. 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; LN997841; CUW15044.1; -; Genomic_DNA. DR RefSeq; WP_013161172.1; NZ_OVTV01000173.1. DR EnsemblBacteria; CUW15044; CUW15044; PFREUDJS001_001231. DR GeneID; 61222056; -. DR PATRIC; fig|1752.46.peg.1269; -. DR OMA; ASCAEYI; -. DR UniPathway; UPA00554; UER00611. DR Proteomes; UP000076747; Chromosome i. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro. DR Gene3D; 3.90.110.10; -; 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 NAD {ECO:0000256|ARBA:ARBA00023027}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}. FT DOMAIN 12..148 FT /note="Ldh_1_N" FT /evidence="ECO:0000259|Pfam:PF00056" FT DOMAIN 152..318 FT /note="Ldh_1_C" FT /evidence="ECO:0000259|Pfam:PF02866" FT ACT_SITE 182 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1" FT BINDING 95 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 127 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 158 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" SQ SEQUENCE 321 AA; 34075 MW; 521470C2799E9653 CRC64; MSNAPLRRDL PKVGIVGAGQ VGSALAYACL IRDTAPIISL YDIDKLRVDA QVADLAHGSI FAEPEVIGGA DVSSMRDCDV IVITSGAPQK PGQSRLDLAG INAKIIADVM PKMLEVSPDA LYVIVANPCD VLAVVAQKVS GLPTNRVFAT GTGLDTARLR HLIARRAHVR ERNVEAVMAG EHGDTEFALW SSARIGVTPI LEWTDEQGNR PFTDASTNEI AKDVADAAYQ VIAGKGSTNY AIGLSGSFLL DQLLSATPSM LPVSSILDDY YGISDVALSV PTLISNQGIV RPIEVPMTDR EHQELTASAN VLKDTIKSIG Y //