ID   LDH1_STAAW              Reviewed;         317 AA.
AC   P65257; Q99WY2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   04-NOV-2008, entry version 32.
DE   RecName: Full=L-lactate dehydrogenase 1;
DE            Short=L-LDH 1;
DE            EC=1.1.1.27;
GN   Name=ldhA; Synonyms=lctE; OrderedLocusNames=MW0217;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Appears to be the primary factor that allows S.aureus
CC       growth during nitrosative stress in both aerobically and
CC       anaerobically cultured cells (By similarity).
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; BA000033; BAB94082.1; -; Genomic_DNA.
DR   RefSeq; NP_645032.1; -.
DR   HSSP; P00344; 2LDB.
DR   GeneID; 1004969; -.
DR   GenomeReviews; BA000033_GR; MW0217.
DR   KEGG; sam:MW0217; -.
DR   HOGENOM; P65257; -.
DR   BioCyc; SAUR196620:MW0217-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
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   GO; GO:0006950; P:response to stress; 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; Stress response.
FT   CHAIN         1    317       L-lactate dehydrogenase 1.
FT                                /FTId=PRO_0000168387.
FT   NP_BIND      15     43       NAD (By similarity).
FT   ACT_SITE    179    179       Proton acceptor (By similarity).
FT   BINDING      92     92       Substrate (By similarity).
FT   BINDING     124    124       NAD or substrate (By similarity).
FT   BINDING     155    155       Substrate (By similarity).
FT   BINDING     232    232       Substrate (By similarity).
FT   MOD_RES     223    223       Phosphotyrosine (By similarity).
SQ   SEQUENCE   317 AA;  34569 MW;  CDDE4813AF6CB226 CRC64;
     MNKFKGNKVV LIGNGAVGSS YAFSLVNQSI VDELVIIDLD TEKVRGDVMD LKHATPYSPT
     TVRVKAGEYS DCHDADLVVI CAGAAQKPGE TRLDLVSKNL KIFKSIVGEV MASKFDGIFL
     VATNPVDILA YATWKFSGLP KERVIGSGTI LDSARFRLLL SEAFDVAPRS VDAQIIGEHG
     DTELPVWSHA NIAGQPLKTL LEQRPEGKAQ IEQIFVQTRD AAYDIIQAKG ATYYGVAMGL
     ARITEAIFRN EDAVLTVSAL LEGEYDEEDV YIGVPAVINR NGIRNVVEIP LNDEEQSKFA
     HSAKTLKDIM AEAEELK
//