ID LLDD_SALPA Reviewed; 396 AA. AC Q5PLQ7; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 27-MAR-2024, entry version 97. 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}; Synonyms=lctD; GN OrderedLocusNames=SPA3546; OS Salmonella paratyphi A (strain ATCC 9150 / SARB42). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=295319; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9150 / SARB42; RX PubMed=15531882; DOI=10.1038/ng1470; RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F., RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., RA Warren W., Florea L., Spieth J., Wilson R.K.; RT "Comparison of genome degradation in Paratyphi A and Typhi, human- RT restricted serovars of Salmonella enterica that cause typhoid."; RL Nat. Genet. 36:1268-1274(2004). 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; CP000026; AAV79347.1; -; Genomic_DNA. DR RefSeq; WP_000586998.1; NC_006511.1. DR AlphaFoldDB; Q5PLQ7; -. DR SMR; Q5PLQ7; -. DR KEGG; spt:SPA3546; -. DR HOGENOM; CLU_020639_0_0_6; -. DR Proteomes; UP000008185; 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_0000206345" 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; 42700 MW; 1CFC8958AEB781CA CRC64; MIISAASDYR AAAQRTLPPF LFHYIDGGAY AEYTLRRNVE DLSQVALRQR VLKNMSDLSL ETTLFNETLS MPVALAPVGL CGMYARRGEV QAAAAADAKG IPFTLSTVSV CPIEEVAPTI QRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR RYWQAVMHPK WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLANNFDP SISWKDLEWI REFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD IAILADSGIR NGLDVVRMIA LGADTVLLGR AYLYALATAG KAGVANLLDL VEKEMKVAMT LTGAKSISEI SGDSLVQELG KSLPAALAPM SKGDAA //