AC   MF_00488;
DC   Protein; auto
TR   HAMAP; MF_00488; -; 1; level=0
XX
Names: Lactate_dehydrog
XX
ID   LDH
DE   RecName: Full=L-lactate dehydrogenase;
DE            Short=L-LDH;
DE            EC=1.1.1.27;
GN   Name=ldh;
XX
CC   -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
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;
case <FTGroup:1>
CC   -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC       bisphosphate (FBP).
end case
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
XX
DR   Pfam; PF02866; Ldh_1_C; 1; trigger=no
DR   Pfam; PF00056; Ldh_1_N; 1; trigger=no
DR   PRINTS; PR00086; LLDHDRGNASE; 1; trigger=no
DR   NCBIfam; TIGR01771; L-LDH-NAD; 1; trigger=no
DR   NCBIfam; TIGR01763; MalateDH_bact; 1; trigger=no
DR   PROSITE; PS00064; L_LDH; 1; trigger=no
XX
case <FTGroup:1>
KW   Allosteric enzyme
end case
KW   Cytoplasm
KW   Oxidoreductase
KW   NAD
case <FTTag:Phosphotyrosine>
KW   Phosphoprotein
end case
case <OS:Staphylococcus aureus>
KW   Stress response
end case
XX
GO   GO:0004459; F:L-lactate dehydrogenase activity
GO   GO:0006096; P:glycolytic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: LDH_GEOSE (P00344)
FT   BINDING         83..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: G-[AVL]
FT   BINDING         122..124
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: [AIV]-x-N
FT   BINDING         124..127
FT                   /ligand="substrate"
FT   Condition: N-x-x-D
FT   BINDING         152..155
FT                   /ligand="substrate"
FT   Condition: D-x-x-R
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: V
FT   BINDING         38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: [DNE]
FT   BINDING         43
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: [RK]
FT   BINDING         69
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: Y
FT   BINDING         86
FT                   /ligand="substrate"
FT   Condition: Q
FT   BINDING         92
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: [ST]
FT   BINDING         147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: [ST]
FT   BINDING         157
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT   Optional; Group: 1; Condition: [RK]
FT   BINDING         172
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT   Optional; Group: 1; Condition: H
FT   BINDING         233
FT                   /ligand="substrate"
FT   Condition: T
FT   From: LDH_BACSU (P13714)
FT   MOD_RES         223
FT                   /note="Phosphotyrosine"
FT   Tag: Phosphotyrosine; Optional; Condition: Y
XX
Size: 304-330;
Related: MF_00487; MF_01516; MF_01517;
Template: P0CW93; P00344; P00343; O32765; P16115;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACAN, BACC1, BACCR, BACCZ, BACHK, BIFLO, CLOAB, ENTFA, LACAC,
 LACJO, LACLA, LACLC, LACPL, LISIN, LISMO, STAA1, STAA2, STAA3, STAA8, STAA9,
 STAAB, STAAC, STAAE, STAAM, STAAN, STAAR, STAAS, STAAT, STAAW
Plasmid: None
Comments: None
XX
# Revision 1.49 2023/06/01
//