LDH_STRP4
ID LDH_STRP4 Reviewed; 328 AA.
AC B5E4V6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00488};
DE Short=L-LDH {ECO:0000255|HAMAP-Rule:MF_00488};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN Name=ldh {ECO:0000255|HAMAP-Rule:MF_00488}; OrderedLocusNames=SPG_1112;
OS Streptococcus pneumoniae serotype 19F (strain G54).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=512566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RX PubMed=11442348; DOI=10.1089/10766290152044995;
RA Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT clinical isolate.";
RL Microb. Drug Resist. 7:99-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RA Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA Tettelin H., Oggioni M.;
RT "Pneumococcal beta glucoside metabolism investigated by whole genome
RT comparison.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001015; ACF56088.1; -; Genomic_DNA.
DR RefSeq; WP_000204727.1; NC_011072.1.
DR AlphaFoldDB; B5E4V6; -.
DR SMR; B5E4V6; -.
DR GeneID; 60233374; -.
DR GeneID; 66806332; -.
DR KEGG; spx:SPG_1112; -.
DR HOGENOM; CLU_045401_1_1_9; -.
DR OMA; ASCAEYI; -.
DR UniPathway; UPA00554; UER00611.
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..328
FT /note="L-lactate dehydrogenase"
FT /id="PRO_1000126159"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 85..86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 124..126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 126..129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 154..157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 159
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 174
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 235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT MOD_RES 226
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
SQ SEQUENCE 328 AA; 35355 MW; 617AAE9603D503B7 CRC64;
MTSTKQHKKV ILVGDGAVGS SYAFALVNQG IAQELGIIEI PQLHEKAVGD ALDLSHALAF
TSPKKIYAAQ YSDCADADLV VITAGAPQKP GETRLDLVGK NLAINKSIVT QVVESGFKGI
FLVAANPVDV LTYSTWKFSG FPKERVIGSG TSLDSARFRQ ALAEKLDVDA RSVHAYIMGE
HGDSEFAVWS HANIAGVNLE EFLKDTQNVQ EAELIELFEG VRDAAYTIIN KKGATYYGIA
VALARITKAI LDDENAVLPL SVFQEGQYGV ENVFIGQPAV VGAHGIVRPV NIPLNDAETQ
KMQASAKELQ AIIDEAWKNP EFQEASKN
