ID LLDD_VIBCH Reviewed; 378 AA. AC Q9KKW6; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 115. 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=VC_A0984; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=243277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A., RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). 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; AE003853; AAF96880.1; -; Genomic_DNA. DR PIR; B82392; B82392. DR RefSeq; NP_233368.1; NC_002506.1. DR RefSeq; WP_000587013.1; NZ_LT906615.1. DR AlphaFoldDB; Q9KKW6; -. DR SMR; Q9KKW6; -. DR STRING; 243277.VC_A0984; -. DR DNASU; 2612817; -. DR EnsemblBacteria; AAF96880; AAF96880; VC_A0984. DR GeneID; 66940974; -. DR KEGG; vch:VC_A0984; -. DR PATRIC; fig|243277.26.peg.3592; -. DR eggNOG; COG1304; Bacteria. DR HOGENOM; CLU_020639_0_0_6; -. DR Proteomes; UP000000584; Chromosome 2. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0019516; P:lactate oxidation; IBA:GO_Central. 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; Reference proteome. FT CHAIN 1..378 FT /note="L-lactate dehydrogenase" FT /id="PRO_0000206352" FT DOMAIN 1..378 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 378 AA; 41291 MW; 8310DF5B3F217ADC CRC64; MIISASTDYR AAAKAKLPPF LFHYIDGGSY GEHTLRRNTD DLADIALRQR VLSDMSELSL ETELFGEKMA LPIALSPVGL TGMYARRGEV QAAQAAEAKG IPFTLSTVSV CPIEEVAPSI HRPIWFQLYV LKDRGFMKNV LERAKAAGVK NLVFTVDMPV PGARYRDMHS GMSGPNAAMR RVLQAMAHPS WAWDVGLLGK PHDLGNISKY RGSPTKLEDY IGWLGANFDP SISWKDLEWI RDFWDGPMII KGILDTEDAK DAVRFGADGI VVSNHGGRQL DGVLSTVQAL PAIADAVKGD LKILVDSGIR TGLDVVRMLA LGADCTMLGR SFIYALAAQG RAGVENLLDL YEKEMRVAMT LTGAKSIAEL SRDSLVKR //