UPP_THEMA
ID UPP_THEMA Reviewed; 209 AA.
AC Q9WZI0;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
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}; OrderedLocusNames=TM_0721;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of uracil phosphoribosyltransferase (TM0721) from
RT Thermotoga maritima at 2.30 A resolution.";
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; AE000512; AAD35803.1; -; Genomic_DNA.
DR PIR; G72341; G72341.
DR RefSeq; NP_228530.1; NC_000853.1.
DR RefSeq; WP_004081012.1; NZ_CP011107.1.
DR PDB; 1O5O; X-ray; 2.30 A; A/B/C/D=1-209.
DR PDBsum; 1O5O; -.
DR AlphaFoldDB; Q9WZI0; -.
DR SMR; Q9WZI0; -.
DR STRING; 243274.THEMA_01055; -.
DR DrugBank; DB03685; Uridine monophosphate.
DR EnsemblBacteria; AAD35803; AAD35803; TM_0721.
DR KEGG; tma:TM0721; -.
DR eggNOG; COG0035; Bacteria.
DR InParanoid; Q9WZI0; -.
DR OMA; TYATRMP; -.
DR OrthoDB; 1581906at2; -.
DR UniPathway; UPA00574; UER00636.
DR EvolutionaryTrace; Q9WZI0; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; 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_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..209
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000120904"
FT BINDING 79
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 104
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 131..139
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 194
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 199..201
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 200
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 4..6
FT /evidence="ECO:0007829|PDB:1O5O"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:1O5O"
FT HELIX 26..44
FT /evidence="ECO:0007829|PDB:1O5O"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1O5O"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1O5O"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1O5O"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1O5O"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1O5O"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:1O5O"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1O5O"
SQ SEQUENCE 209 AA; 23320 MW; BD306120FF64D586 CRC64;
MKNLVVVDHP LIKHKLTIMR DKNTGPKEFR ELLREITLLL AYEATRHLKC EEVEVETPIT
KTIGYRINDK DIVVVPILRA GLVMADGILE LLPNASVGHI GIYRDPETLQ AVEYYAKLPP
LNDDKEVFLL DPMLATGVSS IKAIEILKEN GAKKITLVAL IAAPEGVEAV EKKYEDVKIY
VAALDERLND HGYIIPGLGD AGDRLFRTK
