| IED ID | IndEnz0002009464 |
| Enzyme Type ID | protease009464 |
| Protein Name |
Bifunctional purine biosynthetic protein ADE5,7 Includes: Phosphoribosylamine--glycine ligase EC 6.3.4.13 Glycinamide ribonucleotide synthetase GAR synthetase GARS Phosphoribosylglycinamide synthetase ; Phosphoribosylformylglycinamidine cyclo-ligase EC 6.3.3.1 AIR synthase AIR synthetase AIRS Phosphoribosyl-aminoimidazole synthetase |
| Gene Name | ADE57 ADE5,7 CNAG_06314 |
| Organism | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Tremellomycetes Tremellales (jelly fungi) Cryptococcaceae Cryptococcus Cryptococcus neoformans species complex Cryptococcus neoformans (Filobasidiella neoformans) Cryptococcus neoformans var. grubii (Filobasidiella neoformans var. grubii) Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
| Enzyme Sequence | MPEITAFPQPKSDLSILLLGAGGREHALAFKLAQSSRVARIVVCPGNGGTALMGGKVSNLALPWGAPPAFRSIVEWAQKENIDLVVPGPEQPLVDGVEGAFKKVGIPVFGPSPAAAMLEGSKSLSKEFMARHNIPTAAFRSFTSTQYEDAVAYIKSKPFTSGRSVIKASGLAAGKGVLIPETDEEAFAALKSVMVDKEFGDAGDEVVVEEYLSGPEISVLAFSDGYTIVPMPAAQDHKRIGEGDTGLNTGGMGAYAPAPIATKEIMERCVKDVLEPTIKGMREDGYPFVGMLFTGFMITADGPRVLEYNVRFGDPETQALMLLLDEQTDLAEVLLACVERRLDSIKLGYKQGYAVSVVLASEGYPGSYPKGLPMTLNPTPEGVEVFHAGTKRSDNVTVTDGGRVLAVCASAPTLRAAVDLAYSGISQISFQGQTFRRDIAYRALSSEPPAEPKGLTYAAAGVSVDAGNDLVEAIKPVVKATRRPGADSDIGGFGGAFDLAKAGYKDPILVSGTDGVGTKLRVALDHGKHNTVGIDLVAMSVNDLIVQGAEPLYFLDYYACSKLDVPVAADVITGIAEGCLQAGCALIGGETAEMPGMYHGDDYDLAGFAVGVVERAQILPTPDIASGDVLLALSSSGPHSNGFSLIRKIVSLSNLSLHDTAPWDKNTSVGDALLTPTKVYIKPLLPGIKSGLYKGMSHITGGGFTENIPRIFSSASNLGVKLDLTSYSLPAIWKWLMRAGNVEAKEMVRTFNCGVGMIIIVAKDKADAALSSLKENGEEAWVIGEVQEKKGVEYVGLDKFGL |
| Enzyme Length | 802 |
| Uniprot Accession Number | J9VYP5 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; Evidence={ECO:0000250|UniProtKB:P20772}; CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; Evidence={ECO:0000269|PubMed:34416230}; |
| DNA Binding | |
| EC Number | 6.3.4.13; 6.3.3.1 |
| Enzyme Function | FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities. {ECO:0000269|PubMed:34416230}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000305|PubMed:34416230}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. {ECO:0000305}. |
| nucleotide Binding | NP_BIND 157..218; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00409 |
| Features | Chain (1); Domain (1); Metal binding (2); Nucleotide binding (1); Region (2) |
| Keywords | 3D-structure;ATP-binding;Cytoplasm;Ligase;Magnesium;Manganese;Metal-binding;Multifunctional enzyme;Nucleotide-binding;Purine biosynthesis |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20772}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 7LVO; 7LVP; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 84,591 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48 uM for ATP (at 37 degrees Celsius) {ECO:0000269|PubMed:34416230}; KM=496 uM for glycine (at 37 degrees Celsius) {ECO:0000269|PubMed:34416230}; KM=131 uM for phosphoribosyl-amine (at 37 degrees Celsius) {ECO:0000269|PubMed:34416230}; Note=kcat is 27.3 sec(-1) for phosphoribosylamine--glycine ligase activity (at 37 degrees Celsius). {ECO:0000269|PubMed:34416230}; |
| Metal Binding | METAL 307; /note=Magnesium or manganese; /evidence=ECO:0000255|PROSITE-ProRule:PRU00409; METAL 309; /note=Magnesium or manganese; /evidence=ECO:0000255|PROSITE-ProRule:PRU00409 |
| Rhea ID | RHEA:23032; RHEA:17453 |
| Cross Reference Brenda |