ID LLDD_ESCF3 Reviewed; 396 AA. AC B7LTL2; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 02-SEP-2026, entry version 85. DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01559}; DE EC=1.1.-.- {ECO:0000255|HAMAP-Rule:MF_01559}; GN Name=lldD {ECO:0000255|HAMAP-Rule:MF_01559}; GN OrderedLocusNames=EFER_3599; OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585054; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Catalyzes the conversion of L-lactate to pyruvate. Is coupled CC to the respiratory chain. {ECO:0000255|HAMAP-Rule:MF_01559}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-lactate + A = pyruvate + AH2; Xref=Rhea:RHEA:45816, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16651, CC ChEBI:CHEBI:17499; Evidence={ECO:0000255|HAMAP-Rule:MF_01559}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01559}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01559}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01559}. CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01559}. 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; CU928158; CAQ91071.1; -; Genomic_DNA. DR RefSeq; WP_000586937.1; NC_011740.1. DR AlphaFoldDB; B7LTL2; -. DR SMR; B7LTL2; -. DR GeneID; 75059796; -. DR KEGG; efe:EFER_3599; -. DR HOGENOM; CLU_020639_0_0_6; -. DR OrthoDB; 9770452at2; -. DR Proteomes; UP000000745; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; IEA:TreeGrafter. DR GO; GO:0009060; P:aerobic respiration; IEA:TreeGrafter. DR GO; GO:0006089; P:lactate metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1. DR FunFam; 3.20.20.70:FF:000029; L-lactate dehydrogenase; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01559; L_lact_dehydr; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN. DR InterPro; IPR000262; FMN-dep_DH. DR InterPro; IPR037396; FMN_HAD. DR InterPro; IPR008259; FMN_hydac_DH_AS. DR InterPro; IPR020920; LldD. DR NCBIfam; NF033901; L_lactate_LldD; 1. DR NCBIfam; NF008398; PRK11197.1; 1. DR PANTHER; PTHR10578:SF85; L-LACTATE DEHYDROGENASE; 1. DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1. DR Pfam; PF01070; FMN_dh; 1. DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1. DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Flavoprotein; FMN; Membrane; KW Oxidoreductase; Reference proteome. FT CHAIN 1..396 FT /note="L-lactate dehydrogenase" FT /id="PRO_0000383431" FT DOMAIN 1..380 FT /note="FMN hydroxy acid dehydrogenase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT ACT_SITE 275 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT BINDING 24 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT BINDING 106 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT BINDING 127 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT BINDING 129 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT BINDING 155 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT BINDING 251 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT BINDING 278 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" FT BINDING 306..330 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01559" SQ SEQUENCE 396 AA; 42781 MW; 5DAF272781BD17F6 CRC64; MIISAASDYR AAAQRILPPF LFHYIDGGAY AEYTLRRNVE DLSQVALRQR VLKNMSDLSL ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAGAADAHG IPFTLSTVSV CPIEEVAPTI KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR RYWQAVTHPQ WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLANNFDP SISWKDLEWI RDFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD IAILADSGIR NGLDVVRMIA LGADTVLLGR AYLYALATAG KAGVANLLNL IEKEMKVAMT LTGAKSISEI SQDSLVQELD KALPAALAPL AKGNAA //