HAMAP rule MF_00089
General rule information
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Accession | MF_00089 |
Dates | 1-JUN-2001 (Created) 1-JUN-2023 (Last updated, Version 40) |
Name | ThiC |
Scope | Bacteria
Archaea |
Templates | Q9A6Q5 (THIC_CAUVC); Q9L9I7 (THIC_SALTY); P30136 (THIC_ECOLI); P45740 (THIC_BACSU): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
Gene name |
|
Comments
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Function | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. |
Catalytic activity | RHEA:24840: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine
EC 4.1.99.17 |
case <FTGroup:2>
Cofactor | [4Fe-4S] cluster Note: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. |
end case
Pathway | Cofactor biosynthesis; thiamine diphosphate biosynthesis. |
case <OC:Pseudomonadota>
Subunit | Homodimer. |
end case
Similarity | Belongs to the ThiC family. |
Keywords
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case <FTGroup:2>
end case
case <FTGroup:1>
end case
Gene Ontology
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case <FTGroup:1>
GO:0008270; Molecular function: zinc ion binding.
end case
GO:0016829; Molecular function: lyase activity.
case <FTGroup:2>
GO:0051536; Molecular function: iron-sulfur cluster binding.
end case
GO:0009228; Biological process: thiamine biosynthetic process.
Cross-references
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Features
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From: THIC_CAUVC (Q9A6Q5) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 333 | 335 | /ligand="substrate | S-[RKY]-G | ||||||||
BINDING | 374 | 377 | /ligand="substrate | [DN]-x-x-R | ||||||||
BINDING | 417 | 417 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105 | H | 1 | |||||||
BINDING | 481 | 481 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105 | H | 1 | |||||||
BINDING | 561 | 561 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_note="4Fe-4S-S-AdoMet | C | 2 | |||||||
BINDING | 564 | 564 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_note="4Fe-4S-S-AdoMet | C | 2 | |||||||
BINDING | 569 | 569 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_note="4Fe-4S-S-AdoMet | C | 2 | |||||||
BINDING (Optional) | 219 | 219 | /ligand="substrate | N | ||||||||
BINDING | 248 | 248 | /ligand="substrate | M | ||||||||
BINDING | 277 | 277 | /ligand="substrate | Y | ||||||||
BINDING | 313 | 313 | /ligand="substrate | H | ||||||||
BINDING | 413 | 413 | /ligand="substrate | E | ||||||||
BINDING | 440 | 440 | /ligand="substrate | [YF] |
Additional information
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Size range | 424-721 amino acids |
Related rules | None |
Fusion | Nter: MF_00097 (thiE); Cter: None |
Comments | Possible N-terminal domain in some bacterial ThiC. Fused with ThiE (thiamine-phosphate pyrophosphorylase, MF_00097) in BIFLO. |