HAMAP rule MF_02115
General rule information
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| Accession | MF_02115 |
| Dates | 16-FEB-2011 (Created)
1-JUN-2023 (Last updated, Version 13) |
| Name | FAD_synth_arch |
| Scope(s) |
Archaea |
| Template(s) | Q58579 (RIBL_METJA); Q979C2 (RIBL_THEVO); [ Recover all ] |
| Triggered by |
HAMAP; MF_02115 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | RIBL |
| Protein name | RecName: Full=FAD synthase; EC=2.7.7.2; AltName: Full=FMN adenylyltransferase; AltName: Full=Flavin adenine dinucleotide synthase; |
| Gene name | Name=ribL; |
Comments
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| FUNCTION | Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme. |
| CATALYTIC ACTIVITY | Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; |
| COFACTOR | Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; |
| PATHWAY | Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. |
| SUBUNIT | Homodimer. |
| SIMILARITY | Belongs to the archaeal FAD synthase family. |
Keywords
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Gene Ontology
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| GO:0003919; Molecular function:FMN adenylyltransferase activity |
| GO:0005524; Molecular function:ATP binding |
| GO:0006747; Biological process:FAD biosynthetic process |
| GO:0046444; Biological process:FMN metabolic process |
Cross-references
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Features
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| From: RIBL_THEVO (Q979C2) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 9 | 10 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[VTA]-F | ||||||||
| BINDING | 14 | 17 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
H-x-x-H | ||||||||
| BINDING | 93 | 93 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[DN] | ||||||||
| BINDING | 120 | 120 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[YHF] | ||||||||
Additional information
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| Size range | 137-174 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |