LLDD_HAEIN
ID LLDD_HAEIN Reviewed; 381 AA.
AC P46454;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=HI_1739.1;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION.
RA Koonin E.V., Rudd K.E.;
RL Submitted (SEP-1995) to UniProtKB.
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; L42023; AAC23385.1; -; Genomic_DNA.
DR PIR; T09429; T09429.
DR RefSeq; NP_439882.1; NC_000907.1.
DR RefSeq; WP_005693904.1; NC_000907.1.
DR AlphaFoldDB; P46454; -.
DR SMR; P46454; -.
DR STRING; 71421.HI_1739.1; -.
DR EnsemblBacteria; AAC23385; AAC23385; HI_1739.1.
DR KEGG; hin:HI_1739.1; -.
DR PATRIC; fig|71421.8.peg.1821; -.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_020639_0_0_6; -.
DR OMA; FTRLMQT; -.
DR PhylomeDB; P46454; -.
DR BioCyc; HINF71421:G1GJ1-1761-MON; -.
DR Proteomes; UP000000579; Chromosome.
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..381
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000206339"
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; 41965 MW; E1BC62B0A1A6482D 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 AFVYALGAEG RQGVENMLDI FKKEMHVAMT
LTSNRTIADI KPEALVDLSK L
