ID   LDH1_LISMF              Reviewed;         313 AA.
AC   Q724K3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 38.
DE   RecName: Full=L-lactate dehydrogenase 1;
DE            Short=L-LDH 1;
DE            EC=1.1.1.27;
GN   Name=ldh1; OrderedLocusNames=LMOf2365_0221;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
CC       lactate from pyruvate: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
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DR   EMBL; AE017262; AAT03008.1; -; Genomic_DNA.
DR   RefSeq; YP_012831.1; -.
DR   HSSP; P16115; 1A5Z.
DR   GeneID; 2797324; -.
DR   GenomeReviews; AE017262_GR; LMOf2365_0221.
DR   KEGG; lmf:LMOf2365_0221; -.
DR   TIGR; LMOf2365_0221; -.
DR   HOGENOM; Q724K3; -.
DR   BioCyc; LMON265669:LMOF2365_0221-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0019642; P:anaerobic glycolysis; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00488; -; 1.
DR   InterPro; IPR001557; L-lactate/malate_DHase.
DR   InterPro; IPR011304; L-lactate_DHase.
DR   InterPro; IPR001236; Lactate/malate_DHase.
DR   InterPro; IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase;
KW   Phosphoprotein.
FT   CHAIN         1    313       L-lactate dehydrogenase 1.
FT                                /FTId=PRO_0000168363.
FT   NP_BIND      13     41       NAD (By similarity).
FT   ACT_SITE    176    176       Proton acceptor.
FT   BINDING      89     89       Substrate (By similarity).
FT   BINDING     121    121       NAD or substrate (By similarity).
FT   BINDING     152    152       Substrate (By similarity).
FT   BINDING     227    227       Substrate (By similarity).
FT   MOD_RES     218    218       Phosphotyrosine (By similarity).
SQ   SEQUENCE   313 AA;  34192 MW;  B05D3AEFAAADBBB1 CRC64;
     MKDHQKIILV GDGAVGSSYA FACVNLSIGQ EFGIIDIDKD RTIGDAMDLS HAVPFSTPKK
     IYSANYSDCH DADLVVVTAG TAQKPGETRL DLVNRNIKIM KGIVDEVMAS GFDGIFLIAS
     NPVDILTYAT WKFSGLPKER VIGSGTSLDT ARFRMSIADY LKVDARNVHG YILGEHGDTE
     FPAWSHTTVG GLPITEWISE DEQGAMDTIF VSVRDAAYEI INKKGATFYG VAAALARITK
     AILNNENAIL PLSVYLDGHY GMNDIYIGAP AVVNRQGVRH IVEMNLNDKE KEQMKNSADT
     LKKVLDDAMK QID
//