J3LV62 · J3LV62_ORYBR
- ProteinUMP-CMP kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids523 (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.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic activity
- CMP + ATP = CDP + ADP
Cofactor
Note: Binds 1 Mg2+ ion per monomer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 349-354 | ATP (UniProtKB | ChEBI) | |||
Binding site | 375 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 396-398 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 423-426 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 430 | CMP (UniProtKB | ChEBI) | |||
Binding site | 462 | ATP (UniProtKB | ChEBI) | |||
Binding site | 466 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 477 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 505 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Cellular Component | nucleus | |
Molecular Function | adenylate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | CMP kinase activity | |
Molecular Function | dCMP kinase activity | |
Molecular Function | UMP kinase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | phosphorylation | |
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
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza
Accessions
- Primary accessionJ3LV62
Proteomes
Genome annotation databases
Interaction
Structure
Family & Domains
Features
Showing features for coiled coil.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Coiled coil | 65-92 | ||||
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.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length523
- Mass (Da)59,481
- Last updated2012-10-03 v1
- Checksum3C6B6F8DC5627259
Keywords
- Technical term