A0AAE1H791 · A0AAE1H791_9NEOP
- ProteinUMP-CMP kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1092 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 CMP as phosphate acceptors.
Catalytic activity
- CMP + ATP = CDP + ADP
Cofactor
Note: Binds 1 Mg2+ ion per monomer.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 249 | ||||
Active site | 405 | ||||
Active site | 433 | ||||
Binding site | 910-915 | ATP (UniProtKB | ChEBI) | |||
Binding site | 936 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 958-960 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 985-988 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 992 | CMP (UniProtKB | ChEBI) | |||
Binding site | 1026 | ATP (UniProtKB | ChEBI) | |||
Binding site | 1033 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 1044 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 1072 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | (d)CMP kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent cysteine-type endopeptidase activity | |
Molecular Function | UMP/dUMP kinase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | phosphorylation | |
Biological Process | proteolysis | |
Biological Process | pyrimidine nucleotide biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUMP-CMP kinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Thysanoptera > Terebrantia > Thripoidea > Thripidae > Frankliniella
Accessions
- Primary accessionA0AAE1H791
Proteomes
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 29-115 | Disordered | |||
Compositional bias | 80-100 | Basic and acidic residues | |||
Domain | 194-493 | Calpain catalytic | |||
Domain | 777-812 | EF-hand | |||
Region | 930-960 | NMPbind | |||
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.
Belongs to the peptidase C2 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,092
- Mass (Da)122,568
- Last updated2024-05-29 v1
- MD5 Checksum0B4A2C316E3B93EEA3FE9B912903EAF2
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 80-100 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAHWGI010000488 EMBL· GenBank· DDBJ | KAK3916097.1 EMBL· GenBank· DDBJ | Genomic DNA |