ID LLDD_BARHE Reviewed; 383 AA. AC Q6G4R2; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 107. 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=BH02710; OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / CCUG 30454 / Houston OS 1) (Rochalimaea henselae). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=283166; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49882 / DSM 28221 / CCUG 30454 / Houston 1; RX PubMed=15210978; DOI=10.1073/pnas.0305659101; RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., RA La Scola B., Holmberg M., Andersson S.G.E.; RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative RT of the zoonotic agent Bartonella henselae."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(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; BX897699; CAF27083.1; -; Genomic_DNA. DR RefSeq; WP_011180221.1; NZ_LRIJ02000001.1. DR AlphaFoldDB; Q6G4R2; -. DR SMR; Q6G4R2; -. DR PaxDb; 283166-BH02710; -. DR EnsemblBacteria; CAF27083; CAF27083; BH02710. DR GeneID; 64156570; -. DR KEGG; bhe:BH02710; -. DR eggNOG; COG1304; Bacteria. DR OrthoDB; 9770452at2; -. DR Proteomes; UP000000421; 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..383 FT /note="L-lactate dehydrogenase" FT /id="PRO_0000206331" 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 383 AA; 42129 MW; CCEA4E2FEFB6AF1A CRC64; MIISSTLDYR KAAKRRLPPF LFHYIDGGAY AEETMRRNYA DLQALALRQR ILRGVGEVDL STKLFDQTLD LPIILAPVGL TGMYARRGEV QAARAAVAKG IPFTLSSVSV CPIAEVQKAV GSAFWFQLYV LKDRGFMRDV LERSWASGVR TLVFTVDMPV PGARYRDAHS GMSGSYAGLR RILQAFIHPH WAWNVGIMGR PHDLGNVSTY LQKKIALDDY IGWLGANFDP SIGWHDLQWI RDFWKGKMIL KGILDPEDAR EAIQFGADGI VVSNHGGRQL DGVLSTVRAL PAIAEAVKSD LTILVDSGVR SGLDVVRMIA QGADAVMIGR AFVYALAAAG EKGVAHLIDL FANEMRVAMT LTGVRAIKEI TRESLASPDV FEQ //