UPP_KLEP7
ID UPP_KLEP7 Reviewed; 208 AA.
AC A6TCB0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
GN OrderedLocusNames=KPN78578_27700; ORFNames=KPN_02821;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR78231.1; -; Genomic_DNA.
DR RefSeq; WP_002913827.1; NC_009648.1.
DR PDB; 6WN8; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=1-208.
DR PDBsum; 6WN8; -.
DR AlphaFoldDB; A6TCB0; -.
DR SMR; A6TCB0; -.
DR STRING; 272620.KPN_02821; -.
DR jPOST; A6TCB0; -.
DR EnsemblBacteria; ABR78231; ABR78231; KPN_02821.
DR KEGG; kpn:KPN_02821; -.
DR HOGENOM; CLU_067096_2_2_6; -.
DR OMA; TYATRMP; -.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000000265; Chromosome.
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_1000053727"
FT BINDING 78
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 103
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 130..138
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 193
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 198..200
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 199
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..5
FT /evidence="ECO:0007829|PDB:6WN8"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:6WN8"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:6WN8"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6WN8"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:6WN8"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6WN8"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6WN8"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:6WN8"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:6WN8"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6WN8"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6WN8"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:6WN8"
SQ SEQUENCE 208 AA; 22565 MW; 7FB607C20B0298F6 CRC64;
MKIVEVKHPL VKHKLGLMRE HDISTKRFRE LASEVGSLLT YEATADLETE KVTIEGWNGP
VEVEQIKGKK ITVVPILRAG LGMMEGVLEH VPSARISVVG IYRNEETLEP VPYFQKLVSN
IDERMALVVD PMLATGGSMI ATIDLLKNAG CTSIKVLVLV AAPEGIAALE KAHPDVELYT
ASVDKGLNEH GYIIPGLGDA GDKIFGTK
