HAMAP rule MF_00488
General rule information
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| Accession | MF_00488 |
| Dates | 23-NOV-2001 (Created)
1-JUN-2023 (Last updated, Version 49) |
| Name | Lactate_dehydrog |
| Scope(s) |
Bacteria |
| Template(s) | P0CW93 (LDH2_BIFLO); P00344 (LDH_GEOSE); P00343 (LDH_LACCA); O32765 (LDH_LACHE); P16115 (LDH_THEMA); [ Recover all ] |
| Triggered by |
HAMAP; MF_00488 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | LDH |
| Protein name | RecName: Full=L-lactate dehydrogenase; Short=L-LDH; EC=1.1.1.27; |
| Gene name | Name=ldh; |
Comments
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| FUNCTION | Catalyzes the conversion of lactate to pyruvate. |
| CATALYTIC ACTIVITY | Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; |
| case <FTGroup:1> | |
| ACTIVITY REGULATION | Allosterically activated by fructose 1,6- bisphosphate (FBP). |
| end case | |
| PATHWAY | Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. |
| SUBUNIT | Homotetramer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the LDH/MDH superfamily. LDH family. |
Keywords
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| case <FTGroup:1> | |
| Allosteric enzyme | |
| end case | |
| Cytoplasm | |
| Oxidoreductase | |
| NAD | |
| case <FTTag:Phosphotyrosine> | |
| Phosphoprotein | |
| end case | |
| case <OS:Staphylococcus aureus> | |
| Stress response | |
| end case | |
Gene Ontology
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| GO:0004459; Molecular function:L-lactate dehydrogenase activity |
| GO:0006096; Biological process:glycolytic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF02866; Ldh_1_C; 1; |
| Pfam | PF00056; Ldh_1_N; 1; |
| PRINTS | PR00086; LLDHDRGNASE; 1; |
| NCBIfam | TIGR01771; L-LDH-NAD; 1; |
| NCBIfam | TIGR01763; MalateDH_bact; 1; |
| PROSITE | PS00064; L_LDH; 1; |
Features
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| From: LDH_GEOSE (P00344) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 83 | 84 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-[AVL] | ||||||||
| BINDING | 122 | 124 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
[AIV]-x-N | ||||||||
| BINDING | 124 | 127 | /ligand="substrate" | N-x-x-D | ||||||||
| BINDING | 152 | 155 | /ligand="substrate" | D-x-x-R | ||||||||
| ACT_SITE | 179 | 179 | /note="Proton acceptor" | H | ||||||||
| BINDING | 17 | 17 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
V | ||||||||
| BINDING | 38 | 38 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
[DNE] | ||||||||
| BINDING | 43 | 43 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
[RK] | ||||||||
| BINDING | 69 | 69 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
Y | ||||||||
| BINDING | 86 | 86 | /ligand="substrate" | Q | ||||||||
| BINDING | 92 | 92 | /ligand="substrate" | R | ||||||||
| BINDING | 105 | 105 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
[ST] | ||||||||
| BINDING | 147 | 147 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
[ST] | ||||||||
| BINDING | 157 | 157 | /ligand="beta-D-fructose 1,6-bisphosphate" /ligand_id="ChEBI:CHEBI:32966" /ligand_note="allosteric activator" |
[RK] | 1 | |||||||
| BINDING | 172 | 172 | /ligand="beta-D-fructose 1,6-bisphosphate" /ligand_id="ChEBI:CHEBI:32966" /ligand_note="allosteric activator" |
H | 1 | |||||||
| BINDING | 233 | 233 | /ligand="substrate" | T | ||||||||
| From: LDH_BACSU (P13714) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| MOD_RES | 223 | 223 | /note="Phosphotyrosine" | Phosphotyrosine | Y | |||||||
Additional information
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| Size range | 304-330 amino acids |
| Related rules |
MF_00487 MF_01516 MF_01517 |
| Fusion | Nter: None Cter: None |