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Database: UniProt
Entry: A0A401I2H9_9BACL
LinkDB: A0A401I2H9_9BACL
Original site: A0A401I2H9_9BACL 
ID   A0A401I2H9_9BACL        Unreviewed;       187 AA.
AC   A0A401I2H9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Bifunctional protein PyrR {ECO:0000256|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Pyrimidine operon regulatory protein {ECO:0000256|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Uracil phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01219};
DE              Short=UPRTase {ECO:0000256|HAMAP-Rule:MF_01219};
DE              EC=2.4.2.9 {ECO:0000256|HAMAP-Rule:MF_01219};
GN   Name=pyrR {ECO:0000256|HAMAP-Rule:MF_01219};
GN   ORFNames=PA598K_03908 {ECO:0000313|EMBL:GBF75495.1};
OS   Paenibacillus sp. 598K.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1117987 {ECO:0000313|EMBL:GBF75495.1, ECO:0000313|Proteomes:UP000288287};
RN   [1] {ECO:0000313|EMBL:GBF75495.1, ECO:0000313|Proteomes:UP000288287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=598K {ECO:0000313|EMBL:GBF75495.1,
RC   ECO:0000313|Proteomes:UP000288287};
RA   Mizushima D., Miyazaki T., Shiwa Y., Kimura K., Fujita N., Yoshikawa H.,
RA   Kimura A., Kitamura S., Hara H., Funane K.;
RT   "A novel intracellular dextranase derived from Paenibacillus sp. 598K with
RT   an ability of degrading cycloisomaltooligosaccharides.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC       activity which is not physiologically significant. {ECO:0000256|HAMAP-
CC       Rule:MF_01219}.
CC   -!- FUNCTION: Regulates transcriptional attenuation of the pyrimidine
CC       nucleotide (pyr) operon by binding in a uridine-dependent manner to
CC       specific sites on pyr mRNA. This disrupts an antiterminator hairpin in
CC       the RNA and favors formation of a downstream transcription terminator,
CC       leading to a reduced expression of downstream genes.
CC       {ECO:0000256|HAMAP-Rule:MF_01219}.
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_01219};
CC   -!- SUBUNIT: Homodimer and homohexamer; in equilibrium. {ECO:0000256|HAMAP-
CC       Rule:MF_01219}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrR subfamily. {ECO:0000256|ARBA:ARBA00005565,
CC       ECO:0000256|HAMAP-Rule:MF_01219}.
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:GBF75495.1}.
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DR   EMBL; BFBX01000065; GBF75495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401I2H9; -.
DR   OrthoDB; 9802227at2; -.
DR   Proteomes; UP000288287; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-UniRule.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_01219; PyrR; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR023050; PyrR.
DR   PANTHER; PTHR11608; BIFUNCTIONAL PROTEIN PYRR; 1.
DR   PANTHER; PTHR11608:SF0; BIFUNCTIONAL PROTEIN PYRR; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_01219}; Reference proteome {ECO:0000313|Proteomes:UP000288287};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01219};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01219};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01219};
KW   Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW   ECO:0000256|HAMAP-Rule:MF_01219};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01219, ECO:0000313|EMBL:GBF75495.1}.
FT   DOMAIN          12..157
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   MOTIF           103..115
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01219"
SQ   SEQUENCE   187 AA;  20955 MW;  80271A6EAC16D12B CRC64;
     MSEERHDIMD ETSIRRALTR IAHEILEKNK GIDNCVLVGI RTRGIYLARR LAERIHEIEG
     KQVAVGELDI TSYRDDRSTR PVSSGAACVD EAGQSLALQD KRVILFDDVL YTGRTIRAAM
     DALMDHGRPQ LIQLAVLADR GHRELPIRAD YVGKNVPTSK LEKIEVSLSE LDGEDKVTII
     QQRGQQA
//
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