ID LLDD_ECOSE Reviewed; 396 AA. AC B6I3I4; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 79. 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=ECSE_3887; OS Escherichia coli (strain SE11). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=409438; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE11; RX PubMed=18931093; DOI=10.1093/dnares/dsn026; RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.; RT "Complete genome sequence and comparative analysis of the wild-type RT commensal Escherichia coli strain SE11 isolated from a healthy adult."; RL DNA Res. 15:375-386(2008). 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 = AH2 + pyruvate; 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; AP009240; BAG79411.1; -; Genomic_DNA. DR RefSeq; WP_000586964.1; NC_011415.1. DR AlphaFoldDB; B6I3I4; -. DR SMR; B6I3I4; -. DR GeneID; 75202177; -. DR KEGG; ecy:ECSE_3887; -. DR HOGENOM; CLU_020639_0_0_6; -. DR Proteomes; UP000008199; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004457; F:lactate dehydrogenase activity; IEA:InterPro. DR GO; GO:0019516; P:lactate oxidation; IEA:UniProtKB-UniRule. DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 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 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. FT CHAIN 1..396 FT /note="L-lactate dehydrogenase" FT /id="PRO_0000383422" 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; 42758 MW; CA0D8E208613BF83 CRC64; MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR ILKNMSDLSL ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAKAADAHG IPFTLSTVSV CPIEEVAPAI KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR RYLQAVTHPQ WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLGNNFDP SISWKDLEWI RDFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD IAILADSGIR NGLDVVRMIA LGADTVLLGR AFLYALATAG QAGVANLLNL IEKEMKVAMT LTGAKSISEI TQDSLVQGLG KELPTALAPM AKGNAA //