ID LLDD_XANVE Reviewed; 388 AA. AC A7IMB0; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 02-SEP-2026, entry version 90. 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=Xaut_3929; OS Xanthobacter versatilis. OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Xanthobacteraceae; Xanthobacter. OX NCBI_TaxID=78245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1158 / DSM 118458 / Py2; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.; RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000781; ABS69153.1; -; Genomic_DNA. DR RefSeq; WP_012115901.1; NZ_JBAFUZ010000002.1. DR AlphaFoldDB; A7IMB0; -. DR SMR; A7IMB0; -. DR STRING; 78245.Xaut_3929; -. DR KEGG; xau:Xaut_3929; -. DR eggNOG; COG1304; Bacteria. DR HOGENOM; CLU_020639_0_0_5; -. DR OrthoDB; 9770452at2; -. DR PhylomeDB; A7IMB0; -. DR Proteomes; UP000002417; 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..388 FT /note="L-lactate dehydrogenase" FT /id="PRO_0000383452" 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 388 AA; 42335 MW; FECA89D3F350ED3E CRC64; MIISSSSDYR EAARRRLPPF LFHYIDGGAY AEATLRRNVE DLSDLALRQR VLKSVGEVDL STTLLKQQLS MPVGLAPVGL TGMYARRGEV QAAQAATQKG IPFTLSTVSV CSIEEVQSQV GKPIWFQLYV LKDRGFMKNA LERAWAAGIR TLVFTVDMPV PGARYRDAHS GMSGPNAAFR RMVQAVLHPF WAYDVGLMGT PHDLGNVSAY RKEKTSLEDY VGWLGNNFDP SIGWKDLEWI REFWKGPMVI KGILDPEDAR DAVRFGADGI IVSNHGGRQL DGVLSSARAM PAIADAVKGE MTLLADSGIR SGLDVVRMLA QGADGVLLGR AFVYALAAAG RAGVENLLDI IAKEMRVAMT LTGARAISDI SRDSLVREIE RPLARAAQ //