ID   LDH1_CLOAB              Reviewed;         313 AA.
AC   Q97MD1;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=L-lactate dehydrogenase 1;
DE            Short=L-LDH 1;
DE            EC=1.1.1.27;
GN   Name=ldh1; Synonyms=ldh; OrderedLocusNames=CA_C0267;
OS   Clostridium acetobutylicum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   MEDLINE=21359325; PubMed=11466286;
RX   DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q.,
RA   Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I.,
RA   Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P.,
RA   Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK78248.1; -; Genomic_DNA.
DR   PIR; E96932; E96932.
DR   RefSeq; NP_346908.1; -.
DR   HSSP; P00344; 2LDB.
DR   GeneID; 1116450; -.
DR   GenomeReviews; AE001437_GR; CA_C0267.
DR   KEGG; cac:CAC0267; -.
DR   NMPDR; fig|272562.1.peg.437; -.
DR   HOGENOM; Q97MD1; -.
DR   OMA; Q97MD1; VHAYVLG.
DR   BioCyc; CACE272562:CAC0267-MON; -.
DR   BRENDA; 1.1.1.27; 2866.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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_DH.
DR   InterPro; IPR011304; L-lactate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
DR   InterPro; IPR001236; Lactate/malate_DH.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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_0000168333.
FT   NP_BIND      13     41       NAD (By similarity).
FT   ACT_SITE    176    176       Proton acceptor (By similarity).
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     231    231       Substrate (By similarity).
FT   MOD_RES     222    222       Phosphotyrosine (By similarity).
SQ   SEQUENCE   313 AA;  34181 MW;  C98FD402E62F45D2 CRC64;
     MKKNTKISVI GAGFVGSSTV FALMNGGLAS EIVIVDVNKD KAEGEAMDLS HGAAFVKPVV
     VKSGDYKDTE GSDIVIITAG AAQKPGETRL ELINKNYNIF KSIVPEVVKY NPNAILLVVS
     NPVDILTYIT YKLSGFPKSR VIGSGTVLDT SRFRYMLSEH FEIDVRNIHT YIMGEHGDSE
     IATWSLTNIA GMDVNEYCEA SCKKCDGSLK YKIYDDVKNA AYHVIEKKGA TYYAVALAVK
     RIVEAILRDE NSILTVSSLL EGQYGIKDVY MGVPSIVGIN GVKDIIEVPL NDEEKNNLTD
     SAKTLKESLD SIF
//