A0A178VKQ6 · A0A178VKQ6_ARATH
- ProteinUMP-CMP kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids816 (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
- ATP + CMP = ADP + CDP
Cofactor
Note: Binds 1 Mg2+ ion per monomer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 643-648 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSGKGT | ||||||
Binding site | 669 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 690-692 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: RIV | ||||||
Binding site | 717-720 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GFPR | ||||||
Binding site | 724 | CMP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 756 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 760 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 771 | a ribonucleoside 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 799 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | CMP kinase activity | |
Molecular Function | dCMP kinase activity | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | UMP kinase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
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
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionA0A178VKQ6
Proteomes
Expression
Gene expression databases
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 37-306 | Dynamin-type G | ||||
Sequence: WEALPTVAVVGGQSSGKSSVLESIVGRDFLPRGSGIVTRRPLVLQLHKTDDGTEEYAEFLHLPKKQFTDFALVRREIQDETDRITGKNKQISPVPIHLSIYSPNVVNLTLIDLPGLTKVAVEGQPETIAEDIESMVRTYVDKPNCIILAISPANQDIATSDAIKLAKDVDPTGERTFGVLTKLDLMDKGTNALEVLEGRSYRLQHPWVGIVNRSQADINKNVDMMLARRKEREYFDTSPDYGHLASKMGSEYLAKLLSKHLESVIRTRIP | ||||||
Domain | 532-625 | GED | ||||
Sequence: FRRIASNVSAYVNMVSDTLRNTIPKACVYCQVRQAKLALLNYFYSQISKREGKQLGQLLDEDPALMDRRLECAKRLELYKKARDEIDAVAWDEH |
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 TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length816
- Mass (Da)91,480
- Last updated2016-09-07 v1
- Checksum941BC1DE69BDB038