ID   LLDD_CITK8              Reviewed;         396 AA.
AC   A8ARJ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=CKO_05061;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-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; 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}.
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DR   EMBL; CP000822; ABV16104.1; -; Genomic_DNA.
DR   RefSeq; WP_012135742.1; NC_009792.1.
DR   AlphaFoldDB; A8ARJ1; -.
DR   SMR; A8ARJ1; -.
DR   STRING; 290338.CKO_05061; -.
DR   GeneID; 45138518; -.
DR   KEGG; cko:CKO_05061; -.
DR   HOGENOM; CLU_020639_0_0_6; -.
DR   OrthoDB; 9770452at2; -.
DR   Proteomes; UP000008148; 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; Reference proteome.
FT   CHAIN           1..396
FT                   /note="L-lactate dehydrogenase"
FT                   /id="PRO_1000068978"
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;  42759 MW;  967F029FE15DC35A CRC64;
     MIISAASDYR AAAQRILPPF LFHYIDGGAY AEYTLRRNVE DLSEVALRQR VLKNMSDLSL
     ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAAAADAKG IPFTLSTVSV CPIEEVAPTI
     KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAALR
     RYWQAATHPQ WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLANNFDP SISWKDLEWI
     REFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD
     IAILADSGIR NGLDVVRMIA LGADSVLLGR AYLYALATAG QAGVANLLDL IEKEMKVAMT
     LTGAKSISEI SRDSLVQELG KSLPAALAPL TQGDAA
//