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LDH2_BACCZ
ID   LDH2_BACCZ              Reviewed;         314 AA.
AC   Q632G8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=L-lactate dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00488};
DE            Short=L-LDH 2 {ECO:0000255|HAMAP-Rule:MF_00488};
DE            EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN   Name=ldh2 {ECO:0000255|HAMAP-Rule:MF_00488}; OrderedLocusNames=BCE33L4624;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
CC   -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC       {ECO:0000255|HAMAP-Rule:MF_00488}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC         Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00488};
CC   -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC       bisphosphate (FBP). {ECO:0000255|HAMAP-Rule:MF_00488}.
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000255|HAMAP-Rule:MF_00488}.
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DR   EMBL; CP000001; AAU15649.1; -; Genomic_DNA.
DR   RefSeq; WP_000715339.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q632G8; -.
DR   SMR; Q632G8; -.
DR   EnsemblBacteria; AAU15649; AAU15649; BCE33L4624.
DR   GeneID; 45024729; -.
DR   GeneID; 56654635; -.
DR   GeneID; 67509515; -.
DR   KEGG; bcz:BCE33L4624; -.
DR   PATRIC; fig|288681.22.peg.736; -.
DR   OMA; SICKYIL; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000002612; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_00488; Lactate_dehydrog; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR011304; L-lactate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein.
FT   CHAIN           1..314
FT                   /note="L-lactate dehydrogenase 2"
FT                   /id="PRO_0000237537"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         37
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         68
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         82..83
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         121..123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         123..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         146
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         151..154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         156
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         171
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   MOD_RES         223
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
SQ   SEQUENCE   314 AA;  34620 MW;  82075E6DCDDC1A76 CRC64;
     MKKGINRVVL VGTGAVGCSY AYSMINQGVA EEFVLVDVNE AKAEGEAMDL SHAVPFSPSP
     TKVWSGSYAD CKDADLVVIT AGLPQKPGET RLDLVEKNTK IFKQIVRGIM DSGFDGIFLI
     ATNPVDILTY VTWKESGLPK ERVIGSGTTL DSARFRYMLG DYLDVDPRNV HAYIVGEHGD
     TELPVWSHAT IGVQKLETIL ANNEQYKQED LDKIFENVRD AAYHIIERKG ATYYGIGMSL
     LRVTKAILNN ENSVLTVSAY LEGQYGEKDA YVGVPAVINR EGVREIVELE LNEEEKAKFA
     HSVKVLKETM APVL
 
 
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