ID   LDH2_CLOAB              Reviewed;         320 AA.
AC   Q97DC6;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-NOV-2008, entry version 49.
DE   RecName: Full=L-lactate dehydrogenase 2;
DE            Short=L-LDH 2;
DE            EC=1.1.1.27;
GN   Name=ldh2; OrderedLocusNames=CA_C3552;
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; AAK81477.1; -; Genomic_DNA.
DR   PIR; B97336; B97336.
DR   RefSeq; NP_350137.1; -.
DR   HSSP; P00338; 1I10.
DR   GeneID; 1119734; -.
DR   GenomeReviews; AE001437_GR; CA_C3552.
DR   KEGG; cac:CAC3552; -.
DR   NMPDR; fig|272562.1.peg.3666; -.
DR   HOGENOM; Q97DC6; -.
DR   BioCyc; CACE272562:CAC3552-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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN         1    320       L-lactate dehydrogenase 2.
FT                                /FTId=PRO_0000168334.
FT   NP_BIND      14     42       NAD (By similarity).
FT   ACT_SITE    181    181       Proton acceptor (By similarity).
FT   BINDING      94     94       Substrate (By similarity).
FT   BINDING     126    126       NAD or substrate (By similarity).
FT   BINDING     157    157       Substrate (By similarity).
FT   BINDING     235    235       Substrate (By similarity).
SQ   SEQUENCE   320 AA;  34845 MW;  24B11585F6AA5247 CRC64;
     MNFVKNKLVV VGAGMVGSAV LNSVLSLNLL SEVVIIDIND NKAKGEALDA SHTTSFAYSP
     NVKVRAGNYE DCADAQIIVI TAGPSLKPDD KLDRLVLADT NVKVTDSIMK NICKYTKDAI
     IIVVTNPVDI ATYYCQNNFD YPKNKIIGTG TLLDTARMRK IIGKKYNVDS KNVHGYVLGE
     HGGSSFTSWS DVNIAGIPFN QLNDIFKDHY KVDKDEVDKE VRDSGIEVLK LKGYTSAGIA
     MSVSRLVKAM LLNEQSILPV SSTLEGEYGI NDVALSIPCI ITSNGIEKKL EIPLSKDEVE
     KLNKSADNLK SIIKGLNTNK
//