O65583 · UKL4_ARATH
- ProteinUridine kinase-like protein 4
- GeneUKL4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids469 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Involved in the pyrimidine salvage pathway. The uracil phosphoribosyltransferase (UPRT) activity, that catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate, is unsure.
Catalytic activity
- diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Cofactor
Note: Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP.
Activity regulation
Allosterically activated by GTP.
Pathway
Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 283 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 292 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 326-329 | GTP (UniProtKB | ChEBI) | ||||
Sequence: CKRL | ||||||
Binding site | 336 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 361 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 381 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 387 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 392-395 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: TGNS | ||||||
Binding site | 457-459 | uracil (UniProtKB | ChEBI) | ||||
Sequence: GEF | ||||||
Binding site | 458 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | cytidine kinase activity | |
Molecular Function | GTP binding | |
Molecular Function | uracil phosphoribosyltransferase activity | |
Molecular Function | uridine kinase activity | |
Biological Process | CTP salvage | |
Biological Process | UMP salvage |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUridine kinase-like protein 4
Including 2 domains:
- Recommended nameUridine kinase
- EC number
- Short namesUK
- Recommended namePutative uracil phosphoribosyltransferase
- EC number
- Short namesUPRTase
- 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 accessionO65583
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000120784 | 1-469 | Uridine kinase-like protein 4 | |||
Sequence: MGSKSVVDMIEAASRAHFSGLHVNGHMNGLEPSALKETTSASEDIQRQPFVIGVAGGAASGKTTVCDMIIQQLHDQRVVLINLDSFYHNLTEEELARVHEYNFDHPDAFDTEHLLSCMEKLRQGQAVDIPKYDFKTYRSSVFRRVNPTDVIILEGILLFHDPRVRKLMNMKIFVCTDADVRLARRIKRDTVENGRDIGTVLDQYSKFVKPAFDDFILPTKKYADIIIPRGGDNHVAIDLIVQHICTKLGQHDLCKIYPNLYVIHSTFQIRGMHTLIRDSQTTKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVITPTGCVYSGVDFCKRLCGVSVIRSGESMENALRACCKGIKIGKILIHREGDNGQQLVYEKLPNDISERHVLLLDPILGTGNSAVEAINLLISKGVPEGNIIFLNLISAPQGVHVVCKKFPRIKIVTSEIDNGLNEEFRVIPGMGEFGDRYFGTDDD |
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 46-249 | Uridine kinase | ||||
Sequence: QRQPFVIGVAGGAASGKTTVCDMIIQQLHDQRVVLINLDSFYHNLTEEELARVHEYNFDHPDAFDTEHLLSCMEKLRQGQAVDIPKYDFKTYRSSVFRRVNPTDVIILEGILLFHDPRVRKLMNMKIFVCTDADVRLARRIKRDTVENGRDIGTVLDQYSKFVKPAFDDFILPTKKYADIIIPRGGDNHVAIDLIVQHICTKLG | ||||||
Region | 259-469 | Uracil phosphoribosyltransferase | ||||
Sequence: NLYVIHSTFQIRGMHTLIRDSQTTKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVITPTGCVYSGVDFCKRLCGVSVIRSGESMENALRACCKGIKIGKILIHREGDNGQQLVYEKLPNDISERHVLLLDPILGTGNSAVEAINLLISKGVPEGNIIFLNLISAPQGVHVVCKKFPRIKIVTSEIDNGLNEEFRVIPGMGEFGDRYFGTDDD |
Sequence similarities
In the N-terminal section; belongs to the uridine kinase family.
In the C-terminal section; belongs to the UPRTase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)52,639
- Last updated2010-06-15 v2
- ChecksumE5A6357C1DF76BC7
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 94 | in Ref. 5; BAF00520 | ||||
Sequence: E → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL022223 EMBL· GenBank· DDBJ | CAA18219.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161565 EMBL· GenBank· DDBJ | CAB79506.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE85211.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE85212.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | ANM66905.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | ANM66906.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY086133 EMBL· GenBank· DDBJ | AAM63338.1 EMBL· GenBank· DDBJ | mRNA | ||
BT022059 EMBL· GenBank· DDBJ | AAY25471.1 EMBL· GenBank· DDBJ | mRNA | ||
AK228608 EMBL· GenBank· DDBJ | BAF00520.1 EMBL· GenBank· DDBJ | mRNA | ||
AF116860 EMBL· GenBank· DDBJ | AAD28199.1 EMBL· GenBank· DDBJ | mRNA |