Q9RHX6 · PUR9_CORAM
- ProteinBifunctional purine biosynthesis protein PurH
- GenepurH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids516 (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 = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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 | |
---|---|---|
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 > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium
Accessions
- Primary accessionQ9RHX6
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000192087 | 1-516 | Bifunctional purine biosynthesis protein PurH | |||
Sequence: MSDDRKQIKRALISVYDKTGLEELARTLDSAGVEIVSTGSTAAKIADLGINVTPVESLTGFPECLEGRVKTLHPRVHAGILADTRKPDHLNQLEELEIEPFQLVVVNLYPFKETVASGADFDGCVEQIDIGGPSMVRAAAKNHPSVAVVVDPARYGDIAEAVAQGGFDLAQRRQLAATAFKHTADYDVAVSGWFAQQLADDSVASAELEGDALRYGENPHQQASIVREGTTGVANAKQLHGKEMSYNNYQDADAAWRAAWDHERPCVAIIKHANPCGIAVSDESIAAAHAAAHACDPMSAFGGVIAVNREVTKEMATQVADIFTEVIIAPSYEDGAVEILQGKKNIRILVAEHEVPAVEVKEISGGRLLQEADVYQAEGDKASSWTLAAGEAASEEKLAELEFAWRAVRSVKSNAILLAHEGATVGVGMGQVNRVDSAKLAVDRANTLADSAERARGSVAASDAFFPFADGLQVLIDAGVSAVVQPGGSIRDEEVIAAAEAAGITMYFTGTRHFAH |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-150 | MGS-like | ||||
Sequence: MSDDRKQIKRALISVYDKTGLEELARTLDSAGVEIVSTGSTAAKIADLGINVTPVESLTGFPECLEGRVKTLHPRVHAGILADTRKPDHLNQLEELEIEPFQLVVVNLYPFKETVASGADFDGCVEQIDIGGPSMVRAAAKNHPSVAVVV |
Domain
The IMP cyclohydrolase activity resides in the N-terminal region.
Sequence similarities
Belongs to the PurH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length516
- Mass (Da)54,757
- Last updated2000-05-01 v1
- Checksum14EF915D6DB72B93