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LDH1_STAA3
ID   LDH1_STAA3              Reviewed;         317 AA.
AC   Q2FK29;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=L-lactate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00488};
DE            Short=L-LDH 1 {ECO:0000255|HAMAP-Rule:MF_00488};
DE            EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN   Name=ldh1 {ECO:0000255|HAMAP-Rule:MF_00488};
GN   OrderedLocusNames=SAUSA300_0235;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
CC   -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate (Potential).
CC       Appears to be the primary factor that allows S.aureus growth during
CC       nitrosative stress in both aerobically and anaerobically cultured cells
CC       (By similarity). {ECO:0000250|UniProtKB:Q5HJD7, ECO:0000255|HAMAP-
CC       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   -!- 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, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD22054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000255; ABD22054.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001031882.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FK29; -.
DR   SMR; Q2FK29; -.
DR   EnsemblBacteria; ABD22054; ABD22054; SAUSA300_0235.
DR   KEGG; saa:SAUSA300_0235; -.
DR   HOGENOM; CLU_045401_1_1_9; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000001939; 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   Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Stress response.
FT   CHAIN           1..317
FT                   /note="L-lactate dehydrogenase 1"
FT                   /id="PRO_0000237559"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         43
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         69
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         83..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         122..124
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         124..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         152..155
FT                   /ligand="substrate"
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   317 AA;  34583 MW;  CDDE481269B7DE56 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 LEGEYEEEDV YIGVPAVINR NGIRNVVEIP LNDEEQSKFA
     HSAKTLKDIM AEAEELK
 
 
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