UPP_SACS2
ID UPP_SACS2 Reviewed; 216 AA.
AC Q980Q4;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Uracil phosphoribosyltransferase;
DE EC=2.4.2.9;
DE AltName: Full=UMP pyrophosphorylase;
DE AltName: Full=UPRTase;
GN Name=upp; OrderedLocusNames=SSO0231;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP KINETIC PARAMETERS, ACTIVITY REGULATION, AND REACTION MECHANISM.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=15752360; DOI=10.1111/j.1742-4658.2005.04576.x;
RA Jensen K.F., Arent S., Larsen S., Schack L.;
RT "Allosteric properties of the GTP activated and CTP inhibited uracil
RT phosphoribosyltransferase from the thermoacidophilic archaeon Sulfolobus
RT solfataricus.";
RL FEBS J. 272:1440-1453(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH UMP AND CTP, AND
RP REACTION MECHANISM.
RX PubMed=15654744; DOI=10.1021/bi048041l;
RA Arent S., Harris P., Jensen K.F., Larsen S.;
RT "Allosteric regulation and communication between subunits in uracil
RT phosphoribosyltransferase from Sulfolobus solfataricus.";
RL Biochemistry 44:883-892(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH GTP;
RP 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE; RIBOSE-5-PHOSPHATE AND DIPHOSPHATE,
RP AND REACTION MECHANISM.
RX PubMed=19683539; DOI=10.1016/j.jmb.2009.08.019;
RA Christoffersen S., Kadziola A., Johansson E., Rasmussen M., Willemoes M.,
RA Jensen K.F.;
RT "Structural and kinetic studies of the allosteric transition in Sulfolobus
RT solfataricus uracil phosphoribosyltransferase: Permanent activation by
RT engineering of the C-terminus.";
RL J. Mol. Biol. 393:464-477(2009).
CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC ribose 1-diphosphate (PRPP) to UMP and diphosphate.
CC {ECO:0000269|PubMed:15752360}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC Evidence={ECO:0000269|PubMed:15752360};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC {ECO:0000250};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by CTP
CC and UMP in combination. {ECO:0000269|PubMed:15752360}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55 uM for 5-phospho-alpha-D-ribose 1-diphosphate (in the presence
CC of 1 mM GTP) {ECO:0000269|PubMed:15752360};
CC KM=19 uM for 5-phospho-alpha-D-ribose 1-diphosphate (without GTP)
CC {ECO:0000269|PubMed:15752360};
CC KM=27 uM for uracil (in the presence of 1 mM GTP)
CC {ECO:0000269|PubMed:15752360};
CC KM=1.4 uM for uracil (without GTP) {ECO:0000269|PubMed:15752360};
CC Vmax=15.8 umol/min/mg enzyme (in the presence of 1 mM GTP)
CC {ECO:0000269|PubMed:15752360};
CC Vmax=0.92 umol/min/mg enzyme (without GTP)
CC {ECO:0000269|PubMed:15752360};
CC pH dependence:
CC Optimum pH is 5.0-5.6 at 60 degrees Celsius.
CC {ECO:0000269|PubMed:15752360};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15752360}.
CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000305}.
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DR EMBL; AE006641; AAK40574.1; -; Genomic_DNA.
DR PIR; G90164; G90164.
DR RefSeq; WP_009990487.1; NC_002754.1.
DR PDB; 1VST; X-ray; 2.80 A; A=1-216.
DR PDB; 1XTT; X-ray; 1.80 A; A/B/C/D=1-216.
DR PDB; 1XTU; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-216.
DR PDB; 1XTV; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-216.
DR PDB; 3G6W; X-ray; 2.90 A; A/B/C/D=1-216.
DR PDBsum; 1VST; -.
DR PDBsum; 1XTT; -.
DR PDBsum; 1XTU; -.
DR PDBsum; 1XTV; -.
DR PDBsum; 3G6W; -.
DR AlphaFoldDB; Q980Q4; -.
DR SMR; Q980Q4; -.
DR STRING; 273057.SSO0231; -.
DR EnsemblBacteria; AAK40574; AAK40574; SSO0231.
DR GeneID; 44129202; -.
DR KEGG; sso:SSO0231; -.
DR PATRIC; fig|273057.12.peg.229; -.
DR eggNOG; arCOG04128; Archaea.
DR HOGENOM; CLU_067096_2_0_2; -.
DR InParanoid; Q980Q4; -.
DR OMA; TYATRMP; -.
DR PhylomeDB; Q980Q4; -.
DR BRENDA; 2.4.2.9; 6163.
DR UniPathway; UPA00574; UER00636.
DR EvolutionaryTrace; Q980Q4; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006223; P:uracil salvage; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01218_A; Upp_A; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR034331; Upp_A.
DR InterPro; IPR005765; Ura_phspho_trans.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01091; upp; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Glycosyltransferase; GTP-binding;
KW Magnesium; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..216
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000120927"
FT BINDING 29..30
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT BINDING 30..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 37
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT BINDING 80
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 87..96
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT BINDING 105
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 140..148
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 203
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT BINDING 208..210
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT BINDING 209
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1XTT"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:1XTT"
FT HELIX 25..44
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1XTT"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:1XTT"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1XTT"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1XTT"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1XTT"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:1XTT"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1XTT"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:1XTT"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1XTT"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:1XTT"
SQ SEQUENCE 216 AA; 24150 MW; 08F934237C3FD158 CRC64;
MPLYVIDKPI TLHILTQLRD KYTDQINFRK NLVRLGRILG YEISNTLDYE IVEVETPLGV
KTKGVDITDL NNIVIINILR AAVPLVEGLL KAFPKARQGV IGASRVEVDG KEVPKDMDVY
IYYKKIPDIR AKVDNVIIAD PMIATASTML KVLEEVVKAN PKRIYIVSII SSEYGVNKIL
SKYPFIYLFT VAIDPELNNK GYILPGLGDA GDRAFG
