LDH1_STAAC
ID LDH1_STAAC Reviewed; 317 AA.
AC Q5HJD7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=L-lactate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:18356528};
DE Short=L-LDH 1 {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:18356528};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN Name=ldh1 {ECO:0000255|HAMAP-Rule:MF_00488}; OrderedLocusNames=SACOL0222;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP FUNCTION IN NITROSATIVE STRESS, AND INDUCTION.
RX PubMed=18356528; DOI=10.1126/science.1155207;
RA Richardson A.R., Libby S.J., Fang F.C.;
RT "A nitric oxide-inducible lactate dehydrogenase enables Staphylococcus
RT aureus to resist innate immunity.";
RL Science 319:1672-1676(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE,
RP ACTIVE SITE, AND SUBUNIT.
RA Schramm V.L., Almo S.C., Gutierrez J.A., Ho M.;
RT "Crystal structure of lactate dehydrogenase from Staphylococcus aureus
RT complexed with NAD and pyruvate.";
RL Submitted (MAY-2008) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE,
RP ACTIVE SITE, AND SUBUNIT.
RA Ho M.-C., Almo S.C., Schramm V.L.;
RT "Crystal structure of lactate dehydrogenase mutant (A85R) from
RT staphylococcus aureus complexed with NAD and pyruvate.";
RL Submitted (APR-2009) to the PDB data bank.
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 (PubMed:18356528). {ECO:0000255|HAMAP-Rule:MF_00488,
CC ECO:0000269|PubMed:18356528}.
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 ECO:0000305|Ref.3, ECO:0000305|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- INDUCTION: By nitrosative stress and anaerobiosis. Expression is not
CC detected during aerobic growth. {ECO:0000269|PubMed:18356528}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000255|HAMAP-Rule:MF_00488}.
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DR EMBL; CP000046; AAW38779.1; -; Genomic_DNA.
DR RefSeq; WP_001031882.1; NC_002951.2.
DR PDB; 3D0O; X-ray; 1.80 A; A/B=1-317.
DR PDB; 3D4P; X-ray; 1.80 A; A/B=1-317.
DR PDB; 3H3J; X-ray; 1.80 A; A/B=1-317.
DR PDBsum; 3D0O; -.
DR PDBsum; 3D4P; -.
DR PDBsum; 3H3J; -.
DR AlphaFoldDB; Q5HJD7; -.
DR SMR; Q5HJD7; -.
DR EnsemblBacteria; AAW38779; AAW38779; SACOL0222.
DR KEGG; sac:SACOL0222; -.
DR HOGENOM; CLU_045401_1_1_9; -.
DR OMA; ASCAEYI; -.
DR UniPathway; UPA00554; UER00611.
DR EvolutionaryTrace; Q5HJD7; -.
DR Proteomes; UP000000530; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein;
KW Stress response.
FT CHAIN 1..317
FT /note="L-lactate dehydrogenase 1"
FT /id="PRO_0000168379"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000305|Ref.3, ECO:0000305|Ref.4, ECO:0007744|PDB:3D4P,
FT ECO:0007744|PDB:3H3J"
FT BINDING 16..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:3D4P, ECO:0007744|PDB:3H3J"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PDB:3D4P,
FT ECO:0007744|PDB:3H3J"
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 ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PDB:3D4P,
FT ECO:0007744|PDB:3H3J"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:3H3J"
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 ECO:0000305|Ref.4, ECO:0007744|PDB:3H3J"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:3H3J"
FT BINDING 152..155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000305|Ref.3, ECO:0000305|Ref.4, ECO:0007744|PDB:3D4P,
FT ECO:0007744|PDB:3H3J"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PDB:3D4P,
FT ECO:0007744|PDB:3H3J"
FT MOD_RES 223
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3D0O"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 268..279
FT /evidence="ECO:0007829|PDB:3D0O"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3D0O"
FT HELIX 293..311
FT /evidence="ECO:0007829|PDB:3D0O"
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
