ID A0A1M6NGQ2_9FIRM Unreviewed; 182 AA.
AC A0A1M6NGQ2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN02745227_01116 {ECO:0000313|EMBL:SHJ94796.1};
OS Anaerobranca californiensis DSM 14826.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteinivoraceae;
OC Anaerobranca.
OX NCBI_TaxID=1120989 {ECO:0000313|EMBL:SHJ94796.1, ECO:0000313|Proteomes:UP000243547};
RN [1] {ECO:0000313|Proteomes:UP000243547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14826 {ECO:0000313|Proteomes:UP000243547};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRAI01000010; SHJ94796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6NGQ2; -.
DR STRING; 1120989.SAMN02745227_01116; -.
DR Proteomes; UP000243547; 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|HAMAP-Rule:MF_01219,
KW ECO:0000313|EMBL:SHJ94796.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243547};
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:SHJ94796.1}.
FT DOMAIN 9..165
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT MOTIF 102..114
FT /note="PRPP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01219"
SQ SEQUENCE 182 AA; 20426 MW; 51E10FE29152AF48 CRC64;
MKNSVEKAKI LDEKAMFRAI TRIAHEIIEK NKGVEDVVLV GIKRRGVPLA QKIAEKIMEI
EGHKVLVGTI DITLYRDDLS TKNHQAEVKG HQIDFSIEDK IVVLVDDVLY TGRTVRAALD
ALTDLGRARG IQLAVLVDRG HRELPIRADY VGKNVPTSKK ELVKVKLEQY DGINEVVIEE
LI
//
