HAMAP rule MF_00917
General rule information
[?]
Accession | MF_00917 |
Dates | 8-FEB-2012 (Created) 1-JUN-2023 (Last updated, Version 12) |
Name | QueE |
Scope | Bacteria
Archaea |
Templates | O31677 (QUEE_BACSU); A0A0H3KB22 (QUEE_BURM1): [Recover all] |
Triggered by |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Identifier |
|
case <OC:Bacteria>
Protein name |
|
else case <OC:Archaea>
Protein name |
|
end case
Gene name |
|
Comments
[?]
Function | Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. |
Catalytic activity | RHEA:27974: 6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-deazaguanine + NH4(+)
EC 4.3.99.3 |
Cofactor | [4Fe-4S] cluster Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. |
S-adenosyl-L-methionine Note: Binds 1 S-adenosyl-L-methionine per subunit. |
|
Mg(2+) | |
Pathway | Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. |
Subunit | Homodimer. |
Similarity | Belongs to the radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family. |
Keywords
[?]
case <OC:Bacteria>
end case
Gene Ontology
[?]
GO:0000287; Molecular function: magnesium ion binding.
GO:0016840; Molecular function: carbon-nitrogen lyase activity.
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding.
GO:1904047; Molecular function: S-adenosyl-L-methionine binding.
GO:0016840; Molecular function: carbon-nitrogen lyase activity.
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding.
GO:1904047; Molecular function: S-adenosyl-L-methionine binding.
case <OC:Bacteria>
GO:0008616; Biological process: queuosine biosynthetic process.
end case
Cross-references
[?]
Pfam | PF04055; Radical_SAM; 1; |
NCBIfam | TIGR04508; queE_Cx14CxxC; 1; |
TIGR03365; Bsubt_queE; 1; | |
TIGR04322; rSAM_QueE_Ecoli; 1; | |
TIGR03963; rSAM_QueE_Clost; 1; | |
PIRSF | PIRSF000370; QueE; 1; |
Features
[?]
From: QUEE_BURM1 (A0A0H3KB22) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 12 | 14 | /ligand="substrate | x-x-G | ||||||||
BINDING | 48 | 50 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789 | [FYW]-x-D | ||||||||
BINDING (Optional) | 133 | 135 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789 | S-x-K | ||||||||
BINDING (Optional) | 173 | 176 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789 | Q-x-x-D | ||||||||
BINDING | 31 | 31 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_note="4Fe-4S-S-AdoMet | C | ||||||||
BINDING | 46 | 46 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_note="4Fe-4S-S-AdoMet | C | ||||||||
BINDING | 49 | 49 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_note="4Fe-4S-S-AdoMet | C | ||||||||
BINDING (Optional) | 51 | 51 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420 | [TS] | ||||||||
BINDING | 27 | 27 | /ligand="substrate | R | ||||||||
BINDING | 90 | 90 | /ligand="substrate | [TS] | ||||||||
BINDING | 92 | 92 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789 | G | ||||||||
BINDING (Optional) | Cter | Cter | /ligand="substrate | P |
Additional information
[?]
Size range | 180-290 amino acids |
Related rules | None |
Fusion | None |