ID KPRS_FUSNN STANDARD; PRT; 316 AA. AC Q8RHM2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE Ribose-phosphate pyrophosphokinase (EC 2.7.6.1) (RPPK) (Phosphoribosyl DE pyrophosphate synthetase) (P-Rib-PP synthetase) (PRPP synthetase). GN Name=prs; OrderedLocusNames=FN1992; OS Fusobacterium nucleatum (subsp. nucleatum). OC Bacteria; Fusobacteria; Fusobacterales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=76856; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 25586; RX MEDLINE=21886394; PubMed=11889109; RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., RA Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., RA Larsen N., D'Souza M., Walunas T., Pusch G., Haselkorn R., RA Fonstein M., Kyrpides N.C., Overbeek R.; RT "Genome sequence and analysis of the oral bacterium Fusobacterium RT nucleatum strain ATCC 25586."; RL J. Bacteriol. 184:2005-2018(2002). CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Utilized by both the de novo and the salvage pathways by CC which endogenously formed or exogenously added pyrimidine, purine, CC or pyridine bases are converted to the corresponding CC ribonucleoside monophosphates. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE010501; AAL94082.1; -. DR HSSP; P14193; 1IBS. DR HAMAP; MF_00583; -; 1. DR InterPro; IPR000842; PRPP_synthetase. DR InterPro; IPR000836; PRtransferase. DR InterPro; IPR005946; RibP_Ppkin. DR Pfam; PF00156; Pribosyltran; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHETASE; 1. KW Complete proteome; Kinase; Magnesium; Nucleotide biosynthesis; KW Transferase. FT DOMAIN 216 229 Binding of phosphoribosylpyrophosphate FT (Potential). FT METAL 131 131 Magnesium (Potential). FT METAL 133 133 Magnesium (Potential). FT METAL 142 142 Magnesium (Potential). FT METAL 146 146 Magnesium (Potential). SQ SEQUENCE 316 AA; 35109 MW; 74E240407A01ED84 CRC64; MINFNNVKIF SGNSNLELAK KIAEKAGLQL GKAEIQRFKD GEVYIEIEET VRGRDVFVVQ STSEPVNENL MELLIFVDAL KRASAKTINV IIPYYGYARQ DRKSKPREPI TSKLVANLLT TAGVNRVVAM DLHADQIQGF FDIPLDHMQA LPLMARYFKE KGFKGDEVVV VSPDVGGVKR ARKLAEKLDC KIAIIDKRRP KPNMSEVMNL IGEVEGKIAI FIDDMIDTAG TITNGADAIA QRGAKEVYAC CTHAVFSDPA IERLEKSVLK EIVITDSIAL PERKKIDKIK ILSVDSVFAN AIDRITNNQS VSELFN //