A0A3D6EHZ8 · A0A3D6EHZ8_9BACT
- ProteinMultifunctional fusion protein
- GenemqnE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids712 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Radical SAM enzyme that catalyzes the addition of the adenosyl radical to the double bond of 3-[(1-carboxyvinyl)oxy]benzoate, leading to aminodeoxyfutalosine (AFL), a key intermediate in the formation of menaquinone (MK, vitamin K2) from chorismate.
Catalytic activity
- (S)-dihydroorotate + a quinone = a quinol + orotate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FMN per subunit.
Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Quinol/quinone metabolism; menaquinone biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 62-66 | FMN (UniProtKB | ChEBI) | ||||
Sequence: AGLDK | ||||||
Binding site | 66 | substrate | ||||
Sequence: K | ||||||
Binding site | 86 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 111-115 | substrate | ||||
Sequence: NRMGF | ||||||
Binding site | 139 | FMN (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 172 | FMN (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 172 | substrate | ||||
Sequence: N | ||||||
Active site | 175 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 177 | substrate | ||||
Sequence: N | ||||||
Binding site | 214 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 242 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 243-244 | substrate | ||||
Sequence: NT | ||||||
Binding site | 269 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 298 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 319-320 | FMN (UniProtKB | ChEBI) | ||||
Sequence: YS | ||||||
Binding site | 407 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 411 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 414 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity | |
Molecular Function | aminodeoxyfutalosine synthase activity | |
Molecular Function | dihydroorotate dehydrogenase (quinone) activity | |
Molecular Function | iron ion binding | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | menaquinone biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameDihydroorotate dehydrogenase (quinone)
- EC number
- Alternative names
- Recommended nameAminodeoxyfutalosine synthase
- EC number
- Short namesAFL synthase ; Aminofutalosine synthase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Acidobacteriota > Holophagae > Holophagales > Holophagaceae
Accessions
- Primary accessionA0A3D6EHZ8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 393-627 | Radical SAM core | ||||
Sequence: AYYVMSRRLSYTNVCYTHCQFCAFQAKPGDPRAYALSAEQIIAELEKPENAGVRELHMTSGHNPKLKIDYFEDLFTKIKTRFPSIHLKVFTMIEMDYYARISGLSTDAFLDRCMAAGLESCPGGGAEIFDEELREQICIGKKDAQVWLDTAELCHRKGLPTNCTMLYGHIEEAKHRVDHLLRLRDLQDRSQAAGYQGFLAFIPLAYQNEDNELSATHVIHETTGTQDLREIAVAR |
Sequence similarities
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Belongs to the radical SAM superfamily. MqnE family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length712
- Mass (Da)77,919
- Last updated2019-01-16 v1
- Checksum5A973EBB8BC70518