ID I3D7W5_9PAST Unreviewed; 179 AA.
AC I3D7W5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 ECO:0000313|EMBL:EIJ67808.1};
GN ORFNames=HMPREF1052_0597 {ECO:0000313|EMBL:EIJ67808.1};
OS Pasteurella bettyae CCUG 2042.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=1095749 {ECO:0000313|EMBL:EIJ67808.1, ECO:0000313|Proteomes:UP000006457};
RN [1] {ECO:0000313|EMBL:EIJ67808.1, ECO:0000313|Proteomes:UP000006457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 2042 {ECO:0000313|EMBL:EIJ67808.1,
RC ECO:0000313|Proteomes:UP000006457};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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 the transcription of the pyrimidine nucleotide
CC (pyr) operon in response to exogenous pyrimidines. {ECO:0000256|HAMAP-
CC 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 -!- 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:EIJ67808.1}.
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DR EMBL; AJSX01000041; EIJ67808.1; -; Genomic_DNA.
DR RefSeq; WP_005761559.1; NZ_AJSX01000041.1.
DR AlphaFoldDB; I3D7W5; -.
DR PATRIC; fig|1095749.3.peg.1896; -.
DR eggNOG; COG2065; Bacteria.
DR OrthoDB; 9802227at2; -.
DR Proteomes; UP000006457; Unassembled WGS sequence.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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|HAMAP-Rule:MF_01219,
KW ECO:0000313|EMBL:EIJ67808.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006457};
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 Transferase {ECO:0000256|HAMAP-Rule:MF_01219, ECO:0000313|EMBL:EIJ67808.1}.
FT DOMAIN 5..154
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT MOTIF 100..112
FT /note="PRPP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01219"
SQ SEQUENCE 179 AA; 20494 MW; 286C28FFC3AB417A CRC64;
MEKIIVDESQ FMRTISRISH EIIEKHQDLN NLVIIGIKRR GAEIAELIKR KINELTGQDL
PAMDLDITFY RDDLEYVEAE SQSPIYSGAS DYINIQNKNV ILIDDVLFTG RTIRAALDAL
VDFGRAAKIE LVIFVDRGHR ELPIRADYVG KNVPTSRAEK VQVRTMKYDN CYEVALLPK
//
