P52421 · PUR2_VIGUN
- ProteinPhosphoribosylamine--glycine ligase
- GenePUR2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids311 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
Catalytic activity
- 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H+ + N1-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
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
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
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 lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Vigna
Accessions
- Primary accessionP52421
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000151518 | 1-311 | Phosphoribosylamine--glycine ligase | |||
Sequence: DPRVRKQYIQEQGAPIVIKADGLAAGKGVTVAMTLEEAYKAVDSMLVQGDFGSAGCRVIVEEFLEGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTKELQSIVMDSIIIPTVKGMSAEGSKFVGVLYAGLMIEKKSGMPKLIEYNVRFGDPECQVLMVRLESDLVQVLLAACRGELNGVSLKWSPGSAMVVVMASKGYPGSYQKGTVIENLEEAEAVAPGIKIFHAGTAFDSEGRFIATGGRVLGVTAKGNDLEEACDRAYLAVENVNWPGGFLPSGYWLESSTSETSMLERE |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-191 | ATP-grasp | ||||
Sequence: DPRVRKQYIQEQGAPIVIKADGLAAGKGVTVAMTLEEAYKAVDSMLVQGDFGSAGCRVIVEEFLEGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTKELQSIVMDSIIIPTVKGMSAEGSKFVGVLYAGLMIEKKSGMPKLIEYNVRFGDPECQVLMVRLESDLVQVLLAACR |
Sequence similarities
Belongs to the GARS family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length311
- Mass (Da)33,070
- Last updated1996-10-01 v1
- ChecksumB0CA31A1E2FCB227
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: D |