ID   LDH1_BACCR              Reviewed;         314 AA.
AC   Q81EP4;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=L-lactate dehydrogenase 1;
DE            Short=L-LDH 1;
DE            EC=1.1.1.27;
GN   Name=ldh1; OrderedLocusNames=BC_1924;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22608415; PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP08895.1; -; Genomic_DNA.
DR   RefSeq; NP_831694.1; -.
DR   HSSP; P00344; 2LDB.
DR   GeneID; 1204273; -.
DR   GenomeReviews; AE016877_GR; BC_1924.
DR   KEGG; bce:BC1924; -.
DR   HOGENOM; Q81EP4; -.
DR   OMA; Q81EP4; KEEHVPQ.
DR   BioCyc; BCER226900:BC_1924-MON; -.
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    314       L-lactate dehydrogenase 1.
FT                                /FTId=PRO_0000168321.
FT   NP_BIND      14     42       NAD (By similarity).
FT   ACT_SITE    178    178       Proton acceptor (By similarity).
FT   BINDING      91     91       Substrate (By similarity).
FT   BINDING     123    123       NAD or substrate (By similarity).
FT   BINDING     154    154       Substrate (By similarity).
FT   BINDING     232    232       Substrate (By similarity).
FT   MOD_RES     223    223       Phosphotyrosine (By similarity).
SQ   SEQUENCE   314 AA;  34789 MW;  19DC3B1C2083AB2B CRC64;
     MKKGINRVVL VGTGAVGCSY AYCMINQAVA EEFVLVDVNE AKAEGEAMDL SHAVPFAPAP
     TRVWKGSYED CKDADLVVIT AGLPQKPGET RLDLVEKNAK IFKQIVRSIM DSGFDGIFLI
     ATNPVDILTY VTWKESGLPK ERVIGSGTTL DSARFRYMLG EYFDIGPHNI HAYIIGEHGD
     TELPVWSHVS VGIQKLQTLL EKDNTYNQED LDKIFINVRD AAYHIIERKG ATYYGIGMSL
     LRVTKAILND ENSVLTVSAY LEGQYGQKDV YIGVPAVLNR GGVREILEVE LSEDEELKFD
     HSVQVLKETM APVL
//