B0BZH9 · PUR9_ACAM1
- ProteinBifunctional purine biosynthesis protein PurH
- GenepurH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids524 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- (6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide + (6S)-5,6,7,8-tetrahydrofolate
Pathway
Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | IMP cyclohydrolase activity | |
Molecular Function | phosphoribosylaminoimidazolecarboxamide formyltransferase activity | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional purine biosynthesis protein PurH
Including 2 domains:
- Recommended namePhosphoribosylaminoimidazolecarboxamide formyltransferase
- EC number
- Alternative names
- Recommended nameIMP cyclohydrolase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Acaryochloridales > Acaryochloridaceae > Acaryochloris
Accessions
- Primary accessionB0BZH9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000076472 | 1-524 | Bifunctional purine biosynthesis protein PurH | |||
Sequence: MTRLALLSTSDKTGLVELAQQLVNEYGFTLVSSGGTAVTIEKAGLPVTKVSDYTGSPEILGGRVKTLHPRIHGGILARRSLESDVQDLTENNIQGIDLVVVNLYPFEETIAKQKAQGITDPDQALADAVEQIDIGGPTMIRAAAKNHAHVTVLCDPQQYASYLQELKHGEGETSLPFRQACALKVFERMASYDRAIATHLRQSLATTDSQTQLSILGTAKQTLRYGENPHQNAVWYQESDTASGWAAAQQLQGKELSYNNLVDLEAARRVIAEFAQAETQPTVAILKHNNPCGVAQGETLLQAYEKALAADSVSAFGGIVAMNRAIDTDTAQVLTKTFLECIVAPECQPEAAAVLQAKSNLRVLVLPDLVSGPAVTVKAIAGGWLAQAADETLTPPADWQIVTQAKPTEAQLAELLFAWKVVKHVKSNAIVVTKDHTTLGVGAGQMNRVGSVNIALQQAGEKAQGGTLASDGFFPFDDSVRTAAAAGITAIIQPGGSIRDKDSIQAADELGIVMAFTGTRHFLH |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-154 | MGS-like | ||||
Sequence: MTRLALLSTSDKTGLVELAQQLVNEYGFTLVSSGGTAVTIEKAGLPVTKVSDYTGSPEILGGRVKTLHPRIHGGILARRSLESDVQDLTENNIQGIDLVVVNLYPFEETIAKQKAQGITDPDQALADAVEQIDIGGPTMIRAAAKNHAHVTVLC |
Domain
The IMP cyclohydrolase activity resides in the N-terminal region.
Sequence similarities
Belongs to the PurH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length524
- Mass (Da)55,848
- Last updated2008-02-26 v1
- ChecksumE979D0DFD30BA415
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000828 EMBL· GenBank· DDBJ | ABW30724.1 EMBL· GenBank· DDBJ | Genomic DNA |