P40487 · DPH1_YEAST
- Protein2-(3-amino-3-carboxypropyl)histidine synthase subunit 1
- GeneDPH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids425 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (PubMed:15485916, PubMed:24422557, PubMed:27694803, PubMed:31463593, PubMed:34154323).
In association with DPH2, transfers a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:15485916, PubMed:24422557, PubMed:27694803, PubMed:31463593, PubMed:34154323).
In association with DPH2, transfers a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:15485916, PubMed:24422557, PubMed:27694803, PubMed:31463593, PubMed:34154323).
Miscellaneous
Present with 2526 molecules/cell in log phase SD medium.
Catalytic activity
- L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + S-methyl-5'-thioadenosine + H+
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
Protein modification; peptidyl-diphthamide biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 133 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 239 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 368 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 2-(3-amino-3-carboxypropyl)histidine synthase complex | |
Cellular Component | cytoplasm | |
Molecular Function | 2-(3-amino-3-carboxypropyl)histidine synthase activity | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Biological Process | protein histidyl modification to diphthamide |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-(3-amino-3-carboxypropyl)histidine synthase subunit 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP40487
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Increases translational -1 frameshifting (PubMed:18627462).
Abolishes the formation of the 2-(3-amino-3-carboxypropyl)histidine synthase complex (PubMed:18627462).
Resistance to sordarin and zymocin (PubMed:18627462).
Abolishes the formation of the 2-(3-amino-3-carboxypropyl)histidine synthase complex (PubMed:18627462).
Resistance to sordarin and zymocin (PubMed:18627462).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 133 | Resistance to diphtheria toxin. | |||
Mutagenesis | 239 | Resistance to diphtheria toxin. Abolishes [4Fe-4S] cluster binding and catalytic activity; when associated with S-368. | |||
Mutagenesis | 368 | Resistance to diphtheria toxin. Abolishes [4Fe-4S] cluster binding and catalytic activity; when associated with S-239. | |||
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 8 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000083381 | 1-425 | 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 | ||
Modified residue | 44 | Phosphoserine | |||
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of DPH1, DPH2, KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 (PubMed:15485916, PubMed:18627462, PubMed:23645155, PubMed:24422557, PubMed:27694803, PubMed:31463593).
Interacts with DPH2; the interaction is direct (PubMed:15485916, PubMed:23645155, PubMed:31463593).
Interacts with KTI11/DPH3 (PubMed:12940988, PubMed:18627462, PubMed:23645155, PubMed:27694803).
Interacts with DPH2; the interaction is direct (PubMed:15485916, PubMed:23645155, PubMed:31463593).
Interacts with KTI11/DPH3 (PubMed:12940988, PubMed:18627462, PubMed:23645155, PubMed:27694803).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | P40487 | DPH2 P32461 | 4 | EBI-25162, EBI-6090 | |
BINARY | P40487 | KTI11 Q3E840 | 2 | EBI-25162, EBI-2055307 |
Complex viewer
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-29 | Disordered | |||
Region | 1-60 | Required for function but dispensable for interaction with DPH2 and DPH3 | |||
Region | 366-425 | Required for function but dispensable for interaction with DPH2 and DPH3 | |||
Sequence similarities
Belongs to the DPH1/DPH2 family. DPH1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length425
- Mass (Da)48,311
- Last updated1995-02-01 v1
- Checksum22E93852E03C6722
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z38125 EMBL· GenBank· DDBJ | CAA86277.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006942 EMBL· GenBank· DDBJ | DAA08450.1 EMBL· GenBank· DDBJ | Genomic DNA |