A0A6N8FTQ7 · A0A6N8FTQ7_9CHRO
- ProteinBifunctional pantoate ligase/cytidylate kinase
- GenepanC/cmk
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids526 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively.
Catalytic activity
- (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H+
Pathway
Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 44-51 | ATP (UniProtKB | ChEBI) | ||||
Sequence: MGALHAGH | ||||||
Active site | 51 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 75 | (R)-pantoate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 75 | beta-alanine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 165-168 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GQKD | ||||||
Binding site | 171 | (R)-pantoate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 194 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 202-205 | ATP (UniProtKB | ChEBI) | ||||
Sequence: MSSR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | (d)CMP kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | pantoate-beta-alanine ligase activity | |
Biological Process | pantothenate biosynthetic process | |
Biological Process | pyrimidine nucleotide metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional pantoate ligase/cytidylate kinase
Including 2 domains:
- Recommended namePantothenate synthetase
- EC number
- Short namesPS
- Alternative names
- Recommended nameCytidylate kinase
- EC number
- Short namesCK
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Chroococcales > Chroococcaceae > Gloeocapsopsis > Gloeocapsopsis dulcis
Accessions
- Primary accessionA0A6N8FTQ7
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-295 | Pantoate--beta-alanine ligase | ||||
Sequence: MRLFTTIAALRCYLDCRSADNHLTPEELSSGCSSSQSVGLVPTMGALHAGHLSLIQRARQENETVIVSIFVNPLQFGPNEDYQSYPRTLERDRELCKQVGVDALFVPTPAEMGIDKPSTFLTQVIPPIEMTSVLCGRSRPGHFQGVATIVTKLLNVVQPDRAYFGQKDGQQLAIIRRVVNDLNIPVEMIGCPIVRETSGLAMSSRNQYLTPAQREEAAVLYRSLQQAKQAFDTGEYFSKALIETVKKEVATASAVTLEYVELVHPLTLMPLEKIEESGMLAIAARVGTARLIDNV | ||||||
Region | 296-526 | Cytidylate kinase | ||||
Sequence: ILQNRQPIIAIDGPAGAGKSTVARQVAAKLGLLYLDTGAMYRALTWLVLQLGISFDDCTAIAELASLSQIQLVPEVDLESPQRVWINNQEVTQAIRTIEVTSQVSAIAAQPAVRKALVQKQQAFGKEGGLVAEGRDIGTQVFPDADLKIFLTASVQERAKRRQQDFEQGQINISLTQLEKDIAERDKKDSTREVSPLQKAADAIEVQTDGKKVAEVIAEIIDYYHQRLSRQ | ||||||
Domain | 304-521 | Cytidylate kinase | ||||
Sequence: IAIDGPAGAGKSTVARQVAAKLGLLYLDTGAMYRALTWLVLQLGISFDDCTAIAELASLSQIQLVPEVDLESPQRVWINNQEVTQAIRTIEVTSQVSAIAAQPAVRKALVQKQQAFGKEGGLVAEGRDIGTQVFPDADLKIFLTASVQERAKRRQQDFEQGQINISLTQLEKDIAERDKKDSTREVSPLQKAADAIEVQTDGKKVAEVIAEIIDYYHQ |
Sequence similarities
Belongs to the cytidylate kinase family. Type 1 subfamily.
Belongs to the pantothenate synthetase family.
In the C-terminal section; belongs to the cytidylate kinase family. Type 1 subfamily.
In the N-terminal section; belongs to the pantothenate synthetase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length526
- Mass (Da)57,878
- Last updated2020-10-07 v1
- ChecksumEEAD9272099CEBBD