HAMAP rule MF_02128
General rule information
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Accession | MF_02128 |
Dates | 3-JAN-2012 (Created)
1-JUN-2023 (Last updated, Version 10) |
Name | TMP_kinase |
Scope(s) |
Bacteria Archaea |
Template(s) | O67883 (THIL_AQUAE); P55881 (THIL_SALTY); P0AGG0 (THIL_ECOLI); A3MTW6 (THIL_PYRCJ); [ Recover all ] |
Triggered by |
HAMAP; MF_02128 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | THIL |
Protein name | RecName: Full=Thiamine-monophosphate kinase; Short=TMP kinase; Short=Thiamine-phosphate kinase; EC=2.7.4.16; |
Gene name | Name=thiL; |
Comments
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FUNCTION | Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. |
CATALYTIC ACTIVITY | Reaction=ATP + thiamine phosphate = ADP + thiamine diphosphate; Xref=Rhea:RHEA:15913, ChEBI:CHEBI:30616, ChEBI:CHEBI:37575, ChEBI:CHEBI:58937, ChEBI:CHEBI:456216; EC=2.7.4.16; |
PATHWAY | Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1. |
MISCELLANEOUS | Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate. |
SIMILARITY | Belongs to the thiamine-monophosphate kinase family. |
Keywords
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Gene Ontology
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GO:0000287; Molecular function:magnesium ion binding |
GO:0005524; Molecular function:ATP binding |
GO:0009030; Molecular function:thiamine-phosphate kinase activity |
GO:0009229; Biological process:thiamine diphosphate biosynthetic process |
Cross-references
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Pfam | PF00586; AIRS; 1; |
Pfam | PF02769; AIRS_C; 1; |
NCBIfam | TIGR01379; ThiL; 1; |
PIRSF | PIRSF005303; Thiam_monoph_kin; 1; |
Features
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From: THIL_AQUAE (O67883) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 118 | 119 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G-[ND] | ||||||||
BINDING | 27 | 27 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="3" |
[DE] | ||||||||
BINDING | 27 | 27 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="4" |
[DE] | ||||||||
BINDING | 41 | 41 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="4" |
[TS] | ||||||||
BINDING | 42 | 42 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
[TS] | ||||||||
BINDING | 43 | 43 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
D | ||||||||
BINDING | 43 | 43 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
D | ||||||||
BINDING | 71 | 71 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
D | ||||||||
BINDING | 71 | 71 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="3" |
D | ||||||||
BINDING | 71 | 71 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="4" |
D | ||||||||
BINDING | 119 | 119 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
[ND] | ||||||||
BINDING | 207 | 207 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="3" |
D | ||||||||
BINDING | 210 | 210 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="5" |
D | ||||||||
BINDING | 50 | 50 | /ligand="substrate" | [HD] | ||||||||
BINDING | 101 | 101 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
Y | ||||||||
BINDING | 142 | 142 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[RK] | ||||||||
BINDING | 209 | 209 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[ST] | ||||||||
BINDING | 260 | 260 | /ligand="substrate" | [ED] | ||||||||
BINDING | 303 | 303 | /ligand="substrate" | [WYF] |
Additional information
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Size range | 286-352 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |