ID   LLDD_PSEMY              Reviewed;         379 AA.
AC   A4XYG7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, 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=Pmen_3635;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-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   -!- SUBUNIT: Homotetramer. {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}.
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; CP000680; ABP86383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4XYG7; -.
DR   SMR; A4XYG7; -.
DR   STRING; 399739.Pmen_3635; -.
DR   KEGG; pmy:Pmen_3635; -.
DR   PATRIC; fig|399739.8.peg.3684; -.
DR   eggNOG; COG1304; Bacteria.
DR   HOGENOM; CLU_020639_0_0_6; -.
DR   OrthoDB; 9770452at2; -.
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..379
FT                   /note="L-lactate dehydrogenase"
FT                   /id="PRO_1000068991"
FT   DOMAIN          1..379
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   379 AA;  40949 MW;  49E1743B64C68E3B CRC64;
     MIISASTDYR AAAERKLPPF LFHYADGGAY AEHTLRRNVA DLSNIELRQR VLKNMSELDL
     STELFGEKMS MPVGLAPVGL TGMYARRGEV QAAKAAAAKG IPFTLSTVSV CPIEEVAPAI
     DRPMWFQLYV LKDRGFMRNA LERAKAAGCS TLVFTVDMPV PGARYRDAHS GMSGPNGPLR
     RVLQAMTHPQ WAWDVGVMGK PHDLGNISAY RGNPTGLADY IGWLGANFDP SISWKDLEWI
     RDFWDGPMVI KGILDPEDAR DAVTFGADGI IVSNHGGRQL DGVLSSARAL PAIADAVKGE
     LKILADSGIR TGLDVVRMLA LGADTVLLGR AFIYALAVAG QAGVSNLLDL IEKEMRVAMV
     LTGAKSIAEI TSDLLVKER
//