SPM_004365


  Uniprot: A0A037UP69
Description: phosphoribosylpyrophosphate synthetase
EC number: 2.7.6.1
Annotation score: 3 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_00583}; ; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00583}
Enzyme regulation: 
Function [CC]: FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate. Catalyzes the transfer of pyrophosphoryl group from ATP to ribose-5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP. {ECO:0000256|HAMAP-Rule:MF_00583}.
Pathway: PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00583}.
Active site: 
Binding site: BINDING 106 106 Ribose-5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00583}.; BINDING 132 132 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.; BINDING 176 176 Ribose-5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00583}.
Calcium binding: 
DNA binding: 
Metal binding: METAL 130 130 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00583}.; METAL 132 132 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00583}.; METAL 141 141 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00583}.; METAL 145 145 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00583}.
Nucleotide binding: NP_BIND 39 41 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.; NP_BIND 98 101 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
Site: 
Gene names (primary): prs
Gene names (synonym): 
Mass: 37,823
Subunit structure [CC]: 
Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; ribose phosphate diphosphokinase activity [GO:0004749]; 5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; nucleotide biosynthetic process [GO:0009165]; ribonucleoside monophosphate biosynthetic process [GO:0009156]
Gene ontology IDs: GO:0000287; GO:0004749; GO:0005524; GO:0005737; GO:0006015; GO:0009156; GO:0009165; GO:0016301
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family. {ECO:0000256|HAMAP-Rule:MF_00583}.
Protein families: Ribose-phosphate pyrophosphokinase family
Coiled coil: 
Domain [FT]: DOMAIN 8 122 Pribosyltran_N. {ECO:0000259|Pfam:PF13793}.
Motif: 
Region: REGION 202 204 Ribose-5-phosphate binding. {ECO:0000256|HAMAP-Rule:MF_00583}.; REGION 229 236 Ribose-5-phosphate binding. {ECO:0000256|HAMAP-Rule:MF_00583}.; REGION 319 321 Ribose-5-phosphate binding. {ECO:0000256|HAMAP-Rule:MF_00583}.
EMBL: AGBZ02000003
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92408
UniPathway: 
CDD: 
Gene3D: cd06223
HAMAP: 3.40.50.2020
InterPro: MF_00583_B
PANTHER: IPR000842;IPR029099;IPR000836;IPR029057;IPR005946
PIRSF: 
PRINTS: 
PROSITE: 
Pfam: PS00114
ProDom: PF14572;PF13793
SMART: 
SUPFAM: 
TIGRFAMs: SSF53271
35008-36031(-)

>nucleotide sequence
TTACTTTTTTATTTTCTCAATTATTTTTTTTATTTGTTCATTACATTTTGAATAAACATC
CGATAAACTACGTTTTTCAATCATTGCTTTAATCATTTGTGAAATTAAATCAGCAATTGA
AATGATTTCTAACCCATCAAATAATCGGTCTTGATTAATATCAATTGTATTTGTAACAAT
AACTTTTTTAACTGTCCCATCATTAATAAGTTCTGTTAAACGTTCTTTTGCTGGGGGTGA
AAATACCCCATGACATGCTAATAAATAAACTGCTTTTGCCCCATGCTGTTTTAACGCTTT
TGCTGCATTACAAATTGTTCCAGCCGTATCAATCATATCATCAACAATAAAACAAATACG
GTCTTTAACATCTCCTAAAATAAATTGAACTTCACTAACATTTGGTTTTGGCCGGCGCTT
ATCAATTACTGCAATATTCCCAGCCAAATTCCCTAAACGATTAGCCACATCTCGTGCCCG
TACTAATCCACCATGATCTGGAGAAACAATTGTTACTTCTTCTTTAAGATGATCTTCTTC
AATTTTTCGAACAATTGTTCTTACTAATTCTTGTGTTGAACGTAAATCATCAACTGGAAC
ATCAAAAAATCCCATTGATTGTGGTGAATGTAAATCAACAGTCATTACTCTTGTTGCCCC
CGCTGTTGTTAACATATTTGCCACTAATTTACATGTAATTGGTTGACGACCGCGTGCTTT
TCGGTCTTGACGAGCATATCCAAAATAAGGAATGATCACATTAATGCTTTGTGCACTACC
ACGTTTTAGAGCATCAATCGCAATTAATAATTCCATTAAATTTTCATTAACTGGTCAAGA
TGTTGACTGAATAATATAAACATCTTTTCCCCGTACTGAATTCATTGCGCGCACCAAAAT
TTCACCATCAGCAAAACGAACAGTTTCCATTTCTTGTCTTGTTACACCTAAAATTTTACA
AATTTCATCTGCTAATTTTATTCCAGCAGACAGGCCATATATACTAAAACTTTTTTCTTC
CAT


>protein sequence
MEEKSFSIYGLSAGIKLADEICKILGVTRQEMETVRFADGEILVRAMNSVRGKDVYIIQS
TSWPVNENLMELLIAIDALKRGSAQSINVIIPYFGYARQDRKARGRQPITCKLVANMLTT
AGATRVMTVDLHSPQSMGFFDVPVDDLRSTQELVRTIVRKIEEDHLKEEVTIVSPDHGGL
VRARDVANRLGNLAGNIAVIDKRRPKPNVSEVQFILGDVKDRICFIVDDMIDTAGTICNA
AKALKQHGAKAVYLLACHGVFSPPAKERLTELINDGTVKKVIVTNTIDINQDRLFDGLEI
ISIADLISQMIKAMIEKRSLSDVYSKCNEQIKKIIEKIKK






















© Fisunov Lab of Proteomics, 2016.