ID   LLDD_HAEI8              Reviewed;         381 AA.
AC   Q4QJK8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=NTHI2049;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX88789.1; -; Genomic_DNA.
DR   RefSeq; WP_011272772.1; NC_007146.2.
DR   AlphaFoldDB; Q4QJK8; -.
DR   SMR; Q4QJK8; -.
DR   GeneID; 72526038; -.
DR   KEGG; hit:NTHI2049; -.
DR   HOGENOM; CLU_020639_0_0_6; -.
DR   Proteomes; UP000002525; 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..381
FT                   /note="L-lactate dehydrogenase"
FT                   /id="PRO_0000206340"
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   381 AA;  41954 MW;  E1A7C64FB5E0C32D CRC64;
     MIISSASDYR EAARRRVPPF MFHYADGGSY AEQTLARNVS DLENIALRQR VLKDMSELDT
     SIELFGEKLS MPTILAPVGA CGMYARRGEV QAAQAADNKG VPFTLSTVSI CPIEEVAPAI
     KRPMWFQLYV LKDRGFMKNA LERAKAAGCS TLVFTVDMPT PGARYRDMHS GMSGPYKEIR
     RVLQGFTHPF WAYDVGIKGK PHTLGNVSTY MGRQIGLDDY IGWLTENFDP SISWKDLEWI
     REFWEGPMVI KGILDPEDAK DAVRFGADGI VVSNHGGRQL DGVLSSARAL PPIADAVKGD
     IKIIADSGIR NGLDIVRMLA LGADATMLGR AFVYALGAAG RQGVENMLDI FKKEMRVAMT
     LTSNRTIVDI KPEALVDLSK L
//