ID   LLDD_SALPB              Reviewed;         396 AA.
AC   A9MVJ5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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}; OrderedLocusNames=SPAB_04590;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-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 = 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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000886; ABX69903.1; -; Genomic_DNA.
DR   RefSeq; WP_000586990.1; NC_010102.1.
DR   AlphaFoldDB; A9MVJ5; -.
DR   SMR; A9MVJ5; -.
DR   KEGG; spq:SPAB_04590; -.
DR   PATRIC; fig|1016998.12.peg.4316; -.
DR   HOGENOM; CLU_020639_0_0_6; -.
DR   OMA; FTRLMQT; -.
DR   BioCyc; SENT1016998:SPAB_RS18665-MON; -.
DR   Proteomes; UP000008556; 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; -; 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   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 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_0000383445"
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;  42744 MW;  93DD694CCA854963 CRC64;
     MIISAASDYR AAAQRTLPPF LFHYIDGGAY AEYTLRRNVE DLSQVALRQR VLKNMSDLSL
     ETTLFNETLS MPVALAPVGL CGMYARRGEV QAAAAADAKG IPFTLSTVSV CPIEEVAPTI
     KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR
     RYWQAVMHPK WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLANNFDP SISWKDLEWI
     REFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD
     IAILADSGIR NGLDVVRMIA LGADTVLLGR AYLYALATAG KAGVANLLDL IEKEMKVAMT
     LTGAKSISEI SGDSLVQELG KSLPTALAPM SKGDAA