ID A0A1X6WP42_9ENTE Unreviewed; 321 AA.
AC A0A1X6WP42;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|HAMAP-Rule:MF_00488};
DE Short=L-LDH {ECO:0000256|HAMAP-Rule:MF_00488};
DE EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|HAMAP-Rule:MF_00488};
GN Name=ldh {ECO:0000256|HAMAP-Rule:MF_00488};
GN ORFNames=FM121_08175 {ECO:0000313|EMBL:SLM86049.1};
OS Vagococcus fluvialis bH819.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1255619 {ECO:0000313|EMBL:SLM86049.1, ECO:0000313|Proteomes:UP000195918};
RN [1] {ECO:0000313|Proteomes:UP000195918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bH819 {ECO:0000313|Proteomes:UP000195918};
RA Dridi B.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000256|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:0000256|ARBA:ARBA00001763, ECO:0000256|HAMAP-
CC Rule:MF_00488};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC bisphosphate (FBP). {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000256|ARBA:ARBA00006054, ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00488}.
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DR EMBL; FWFD01000012; SLM86049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6WP42; -.
DR OrthoDB; 9802969at2; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000195918; Unassembled WGS sequence.
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 CDD; cd05291; HicDH_like; 1.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01771; L-LDH-NAD; 1.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 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 SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00488};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00488};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00488, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00488,
KW ECO:0000256|RuleBase:RU003369};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00488};
KW Reference proteome {ECO:0000313|Proteomes:UP000195918}.
FT DOMAIN 10..147
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 150..318
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 15..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 45
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 84..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 123..125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 125..128
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 153..156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 158
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 173
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT MOD_RES 225
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
SQ SEQUENCE 321 AA; 35189 MW; C8A812F72DF69A32 CRC64;
MTIQTFTHQK IIVIGNGAVG SSYTFALVTQ NIAQEIGIID IDTNKAEGDA IDLSHALAFT
SPKKIYAAQY SDCHDADIVV ITAGAAQKPG ETRLDLVNKN LKIFQDIVKN IVDSGFNGIF
LVATNPVDIL TYATWKFSGF PQHKIIGSGT SLDSARYRQA IAELVGVDAR NVHGYILGEH
GDTEFPVWSH ANIAGLQIYE WVKDHPDVDE EELVNLFFKV RDAAYTIIEK KGATFYGIAV
SLARITKAIL NDENAVLPLS VYLDGHYGLS DIFIGAPAVI NRTGVHDVIE IPLTDAEQEK
FDYSAKKLKE IMDDAFNELG N
//
