R8BEE4 · R8BEE4_PHAM7
- ProteinMultifunctional fusion protein
- GeneLIA1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1223 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalyzes the hydroxylation of the N6-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
Catalytic activity
- [eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-hypusine + A + H2O
Cofactor
Note: Binds 2 Fe2+ ions per subunit.
Pathway
Phospholipid metabolism; phosphatidylcholine biosynthesis.
Protein modification; eIF5A hypusination.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 963 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 964 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 996 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 997 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1128 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1129 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1161 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1162 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | nucleus | |
Molecular Function | deoxyhypusine monooxygenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphatidylethanolamine N-methyltransferase activity | |
Biological Process | methylation | |
Biological Process | peptidyl-lysine modification to peptidyl-hypusine | |
Biological Process | phosphatidylcholine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameDeoxyhypusine hydroxylase
- EC number
- Short namesDOHH
- Alternative names
- Recommended namePhosphatidylethanolamine N-methyltransferase
- EC number
- Short namesPE methyltransferase ; PEAMT ; PEMT
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Togniniales > Togniniaceae > Phaeoacremonium
Accessions
- Primary accessionR8BEE4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endomembrane system ; Multi-pass membrane protein
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 37-54 | Helical | ||||
Sequence: ALVLAILALHILAAYLLP | ||||||
Transmembrane | 61-81 | Helical | ||||
Sequence: VFAAIFLWWRASYNIGIGVLL | ||||||
Transmembrane | 147-167 | Helical | ||||
Sequence: VVDLILMCDFVSYCLFAIVCA | ||||||
Transmembrane | 174-195 | Helical | ||||
Sequence: GLSLFLGRWVVGIALFGFNLWV | ||||||
Transmembrane | 332-350 | Helical | ||||
Sequence: YAVILLVFYTVCMTVFTPT | ||||||
Transmembrane | 356-379 | Helical | ||||
Sequence: ALFVLHALFWRLWYSVGLGIMLNL | ||||||
Transmembrane | 496-529 | Helical | ||||
Sequence: VMGLAGLWGAALITWSRAIFLLAIVSQILTLGFI |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 281-311 | Disordered | ||||
Sequence: YNPPPPRVRSDGGRESFGSQESETKPPNQEV | ||||||
Compositional bias | 295-311 | Polar residues | ||||
Sequence: ESFGSQESETKPPNQEV | ||||||
Region | 1044-1070 | Disordered | ||||
Sequence: EQRKQEKLRQSDFASVDPAPPMPESKR |
Sequence similarities
Belongs to the class VI-like SAM-binding methyltransferase superfamily. CHO2 family.
Belongs to the deoxyhypusine hydroxylase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,223
- Mass (Da)137,257
- Last updated2013-07-24 v1
- Checksum8167885D5A326FE7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 295-311 | Polar residues | ||||
Sequence: ESFGSQESETKPPNQEV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KB933264 EMBL· GenBank· DDBJ | EON97668.1 EMBL· GenBank· DDBJ | Genomic DNA |