ID   LDH2_STAAR              Reviewed;         319 AA.
AC   Q6GDK1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=L-lactate dehydrogenase 2;
DE            Short=L-LDH 2;
DE            EC=1.1.1.27;
GN   Name=ldh2; OrderedLocusNames=SAR2680;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Contributes to S.aureus growth during nitrosative stress
CC       in both aerobically and anaerobically cultured cells, despite
CC       playing a secondary role in this resistance mechanism (By
CC       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; BX571856; CAG41657.1; -; Genomic_DNA.
DR   RefSeq; YP_042022.1; -.
DR   GeneID; 2859696; -.
DR   GenomeReviews; BX571856_GR; SAR2680.
DR   KEGG; sar:SAR2680; -.
DR   HOGENOM; Q6GDK1; -.
DR   OMA; Q6GDK1; ATIAYAC.
DR   BioCyc; SAUR282458:SAR2680-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   GO; GO:0006950; P:response to stress; 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; Stress response.
FT   CHAIN         1    319       L-lactate dehydrogenase 2.
FT                                /FTId=PRO_0000168384.
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     231    231       Substrate (By similarity).
FT   MOD_RES     222    222       Phosphotyrosine (By similarity).
SQ   SEQUENCE   319 AA;  34420 MW;  7779343BCA8006C4 CRC64;
     MKTFGKKVVL IGDGSVGSSY AFAMVTQGVA DEFVIIDIAK DKVKADVQDL NHGTVHSPSP
     VDVKAGEYED CKDADLVVIT AGAPQKPGET RLQLVEKNTK IMKSIVKSVM DSGFDGYFLI
     AANPVDILTR FVKEYTGLPA ERVIGSGTVL DSARLQYLIS QELGVAPSSV DASIIGEHGD
     TELAVWSQAN VAGISVYDTL KEQTGSEAKA EEIYVNTRDA AYEIIQAKGS TYYGIALALM
     RISKAILNNE NNVLNVSIQL DGQYGGHKGV YLGVPTLVNQ HGAVKIYEMP LSAEEQALFD
     KSVKTLEDTF DSIKYLLED
//