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Database: UniProt
Entry: A0A133ZM10_9CORY
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Original site: A0A133ZM10_9CORY 
ID   A0A133ZM10_9CORY        Unreviewed;       211 AA.
AC   A0A133ZM10;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Uracil phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011894, ECO:0000256|HAMAP-Rule:MF_01218};
DE            EC=2.4.2.9 {ECO:0000256|ARBA:ARBA00011894, ECO:0000256|HAMAP-Rule:MF_01218};
DE   AltName: Full=UMP pyrophosphorylase {ECO:0000256|ARBA:ARBA00031082, ECO:0000256|HAMAP-Rule:MF_01218};
DE   AltName: Full=UPRTase {ECO:0000256|HAMAP-Rule:MF_01218};
GN   Name=upp {ECO:0000256|HAMAP-Rule:MF_01218};
GN   ORFNames=HMPREF0307_00184 {ECO:0000313|EMBL:KXB56493.1};
OS   Corynebacterium sp. DNF00584.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1384076 {ECO:0000313|EMBL:KXB56493.1, ECO:0000313|Proteomes:UP000070591};
RN   [1] {ECO:0000313|EMBL:KXB56493.1, ECO:0000313|Proteomes:UP000070591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00584 {ECO:0000313|EMBL:KXB56493.1,
RC   ECO:0000313|Proteomes:UP000070591};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01218};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01218};
CC       Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC       {ECO:0000256|HAMAP-Rule:MF_01218};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP.
CC       {ECO:0000256|HAMAP-Rule:MF_01218}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uracil: step 1/1. {ECO:0000256|ARBA:ARBA00005180,
CC       ECO:0000256|HAMAP-Rule:MF_01218}.
CC   -!- SIMILARITY: Belongs to the UPRTase family.
CC       {ECO:0000256|ARBA:ARBA00009516, ECO:0000256|HAMAP-Rule:MF_01218}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXB56493.1}.
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DR   EMBL; LSCZ01000003; KXB56493.1; -; Genomic_DNA.
DR   RefSeq; WP_066485047.1; NZ_KQ959728.1.
DR   AlphaFoldDB; A0A133ZM10; -.
DR   GeneID; 79852503; -.
DR   PATRIC; fig|1384076.3.peg.179; -.
DR   OrthoDB; 9781675at2; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000070591; Unassembled WGS sequence.
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   NCBIfam; TIGR01091; upp; 1.
DR   PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR32315:SF4; URACIL PHOSPHORIBOSYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF14681; UPRTase; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW   Rule:MF_01218};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_01218};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01218};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01218};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01218}; Reference proteome {ECO:0000313|Proteomes:UP000070591};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01218}.
FT   BINDING         77
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01218"
FT   BINDING         192
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01218"
FT   BINDING         197..199
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01218"
SQ   SEQUENCE   211 AA;  22456 MW;  64E176DF8A782142 CRC64;
     MDIHVVDHPL AASRLTLMRD ARSDNAAFRA ALKDLGTMLV YEAARDLPVE HFDCVTPVDT
     AQGTRLQDPP IIVPIIRAGL GMIDPALSMI PDAQVGFIGM ARDEETHEPV PYLEALPEDL
     SGRTVFVVDP MLATGGSLLH ALRLLAARGA TNITAICMVS AQEGVDALAN SGLPVRLVTA
     VIDPSLDEDA YIVPGLGDAG DRLYGPRNID L
//
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