UPP_MYCTU
ID UPP_MYCTU Reviewed; 207 AA.
AC P9WFF3; L0TCE8; P0A658; P94928;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
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=Rv3309c;
GN ORFNames=MTV016.08c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP46128.1; -; Genomic_DNA.
DR PIR; D70842; D70842.
DR RefSeq; NP_217826.1; NC_000962.3.
DR RefSeq; WP_003417245.1; NZ_NVQJ01000003.1.
DR PDB; 5E38; X-ray; 3.00 A; A/B/C/D=2-207.
DR PDBsum; 5E38; -.
DR AlphaFoldDB; P9WFF3; -.
DR SMR; P9WFF3; -.
DR STRING; 83332.Rv3309c; -.
DR PaxDb; P9WFF3; -.
DR DNASU; 887944; -.
DR GeneID; 45427304; -.
DR GeneID; 887944; -.
DR KEGG; mtu:Rv3309c; -.
DR TubercuList; Rv3309c; -.
DR eggNOG; COG0035; Bacteria.
DR OMA; TYATRMP; -.
DR PhylomeDB; P9WFF3; -.
DR BRENDA; 2.4.2.9; 3445.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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..207
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000120858"
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 129..137
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 192
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 197..199
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 198
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 3..5
FT /evidence="ECO:0007829|PDB:5E38"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5E38"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:5E38"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5E38"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5E38"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:5E38"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5E38"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5E38"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:5E38"
FT TURN 199..203
FT /evidence="ECO:0007829|PDB:5E38"
SQ SEQUENCE 207 AA; 21898 MW; 63B2486AE7C42AF8 CRC64;
MQVHVVDHPL AAARLTTLRD ERTDNAGFRA ALRELTLLLI YEATRDAPCE PVPIRTPLAE
TVGSRLTKPP LLVPVLRAGL GMVDEAHAAL PEAHVGFVGV ARDEQTHQPV PYLDSLPDDL
TDVPVMVLDP MVATGGSMTH TLGLLISRGA ADITVLCVVA APEGIAALQK AAPNVRLFTA
AIDEGLNEVA YIVPGLGDAG DRQFGPR
