UPP_AQUAE
ID UPP_AQUAE Reviewed; 208 AA.
AC O67914;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01218};
DE EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01218};
DE AltName: Full=UMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01218};
DE AltName: Full=UPRTase {ECO:0000255|HAMAP-Rule:MF_01218};
GN Name=upp {ECO:0000255|HAMAP-Rule:MF_01218}; Synonyms=uraP;
GN OrderedLocusNames=aq_2163;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Structure of aq2163 protein from Aquifex aeolicus.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000255|HAMAP-
CC Rule:MF_01218}.
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:0000255|HAMAP-Rule:MF_01218};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01218};
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC {ECO:0000255|HAMAP-Rule:MF_01218};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP.
CC {ECO:0000255|HAMAP-Rule:MF_01218}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01218}.
CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP-
CC Rule:MF_01218}.
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DR EMBL; AE000657; AAC07880.1; -; Genomic_DNA.
DR PIR; F70485; F70485.
DR RefSeq; NP_214483.1; NC_000918.1.
DR RefSeq; WP_010881419.1; NC_000918.1.
DR PDB; 2E55; X-ray; 2.15 A; A/B/C/D=1-208.
DR PDBsum; 2E55; -.
DR AlphaFoldDB; O67914; -.
DR SMR; O67914; -.
DR STRING; 224324.aq_2163; -.
DR EnsemblBacteria; AAC07880; AAC07880; aq_2163.
DR KEGG; aae:aq_2163; -.
DR PATRIC; fig|224324.8.peg.1671; -.
DR eggNOG; COG0035; Bacteria.
DR HOGENOM; CLU_067096_2_0_0; -.
DR InParanoid; O67914; -.
DR OMA; TYATRMP; -.
DR OrthoDB; 1581906at2; -.
DR UniPathway; UPA00574; UER00636.
DR EvolutionaryTrace; O67914; -.
DR Proteomes; UP000000798; 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; IEA:UniProtKB-UniRule.
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_B; Upp_B; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR034332; Upp_B.
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..208
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000120792"
FT BINDING 77
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 102
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 128..136
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 191
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 196..198
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 197
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:2E55"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:2E55"
FT HELIX 24..42
FT /evidence="ECO:0007829|PDB:2E55"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2E55"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2E55"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2E55"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2E55"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:2E55"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:2E55"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2E55"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2E55"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:2E55"
SQ SEQUENCE 208 AA; 23533 MW; 87B9CFEFEA9CFF77 CRC64;
MIVELSHPLI KHKVNTARIQ DTSAEKLRKT LKELGFMLVY EALKDILLEE KEVRTWIGNK
RFNYLNEEEI VFVPILRAGL SFLEGALQVV PNAKVGFLGI KRNEETLESH IYYSRLPELK
GKIVVILDPM LATGGTLEVA LREILKHSPL KVKSVHAIAA PEGLKRIEEK FKEVEIFVGN
VDERLNDKGY IIPGLGDIGD RLYAVSVY
