LLDD_VIBCH
ID LLDD_VIBCH Reviewed; 378 AA.
AC Q9KKW6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=VC_A0984;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003853; AAF96880.1; -; Genomic_DNA.
DR PIR; B82392; B82392.
DR RefSeq; NP_233368.1; NC_002506.1.
DR RefSeq; WP_000587013.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KKW6; -.
DR SMR; Q9KKW6; -.
DR STRING; 243277.VC_A0984; -.
DR DNASU; 2612817; -.
DR EnsemblBacteria; AAF96880; AAF96880; VC_A0984.
DR GeneID; 57742342; -.
DR GeneID; 66940974; -.
DR KEGG; vch:VC_A0984; -.
DR PATRIC; fig|243277.26.peg.3592; -.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_020639_0_0_6; -.
DR OMA; FTRLMQT; -.
DR BioCyc; VCHO:VCA0984-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0019516; P:lactate oxidation; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..378
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000206352"
FT DOMAIN 1..378
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 378 AA; 41291 MW; 8310DF5B3F217ADC CRC64;
MIISASTDYR AAAKAKLPPF LFHYIDGGSY GEHTLRRNTD DLADIALRQR VLSDMSELSL
ETELFGEKMA LPIALSPVGL TGMYARRGEV QAAQAAEAKG IPFTLSTVSV CPIEEVAPSI
HRPIWFQLYV LKDRGFMKNV LERAKAAGVK NLVFTVDMPV PGARYRDMHS GMSGPNAAMR
RVLQAMAHPS WAWDVGLLGK PHDLGNISKY RGSPTKLEDY IGWLGANFDP SISWKDLEWI
RDFWDGPMII KGILDTEDAK DAVRFGADGI VVSNHGGRQL DGVLSTVQAL PAIADAVKGD
LKILVDSGIR TGLDVVRMLA LGADCTMLGR SFIYALAAQG RAGVENLLDL YEKEMRVAMT
LTGAKSIAEL SRDSLVKR
