A0A366R2X6 · A0A366R2X6_9HYPO
- ProteinUridylate kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids225 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.
Catalytic activity
- ATP + UMP = ADP + UDP
Cofactor
Note: Binds 1 Mg2+ ion per monomer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 40-45 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAGKGT | ||||||
Binding site | 66 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 88-90 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: LIV | ||||||
Binding site | 121-124 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GFPR | ||||||
Binding site | 128 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 159 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 165 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 176 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 204 | ATP (UniProtKB | ChEBI) | ||||
Sequence: P |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | (d)CMP kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | UMP kinase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | CDP biosynthetic process | |
Biological Process | UDP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUridylate kinase
- EC number
- Short namesUK
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium > Fusarium incarnatum-equiseti species complex
Accessions
- Primary accessionA0A366R2X6
Proteomes
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-25 | Disordered | ||||
Sequence: MPAVPQDAPESAGQIPAPQKSTPTF | ||||||
Region | 60-90 | NMPbind | ||||
Sequence: SAGDLLRAEQERPGSQYGDLIKDYIRNGLIV | ||||||
Region | 158-168 | LID | ||||
Sequence: ERGKTSGREDD |
Domain
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence similarities
Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length225
- Mass (Da)24,581
- Last updated2018-11-07 v1
- Checksum70058597DB56D01C