A0A0Q5AMK9 · A0A0Q5AMK9_9MICO
- ProteinPhosphoribosylamine--glycine ligase
- GenepurD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids423 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H+ + N1-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Cofactor
Protein has several cofactor binding sites:
Pathway
Purine metabolism; IMP biosynthesis via de novo pathway; N1-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | phosphoribosylamine-glycine ligase activity | |
Biological Process | 'de novo' IMP biosynthetic process | |
Biological Process | purine nucleobase biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoribosylamine--glycine ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Rathayibacter
Accessions
- Primary accessionA0A0Q5AMK9
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 107-312 | ATP-grasp | ||||
Sequence: KRVMDMARVPTGRATRVSTLVDASRVIDEFGAPYVVKADGLAAGKGVLVTESRSAAVAHAEFWLQSGDVLIEEFLAGQEVSLFLLSDGHDVVPLSPAQDYKRLGDGDEGPNTGGMGAYSPLPWLADRWADERAFVDEVIDTVAIPTIRQLERERTPFVGLLYCGLIVTDDGIRVIEFNARFGDPETQVVLPRLASPLSALLHAAAT |
Sequence similarities
Belongs to the GARS family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length423
- Mass (Da)44,837
- Last updated2016-01-20 v1
- Checksum7EAC007AE640024C
Keywords
- Technical term