ID F6B464_DESCC Unreviewed; 184 AA.
AC F6B464;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
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 OrderedLocusNames=Desca_1260 {ECO:0000313|EMBL:AEF94119.1};
OS Desulfotomaculum nigrificans (strain DSM 14880 / VKM B-2319 / CO-1-SRB)
OS (Desulfotomaculum carboxydivorans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=868595 {ECO:0000313|EMBL:AEF94119.1, ECO:0000313|Proteomes:UP000009226};
RN [1] {ECO:0000313|Proteomes:UP000009226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC {ECO:0000313|Proteomes:UP000009226};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL Submitted (MAY-2011) 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; CP002736; AEF94119.1; -; Genomic_DNA.
DR RefSeq; WP_013810089.1; NC_015565.1.
DR AlphaFoldDB; F6B464; -.
DR STRING; 868595.Desca_1260; -.
DR KEGG; dca:Desca_1260; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_2_1_9; -.
DR OMA; PIQPDFC; -.
DR Proteomes; UP000009226; Chromosome.
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:AEF94119.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009226};
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:AEF94119.1}.
FT DOMAIN 11..164
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT MOTIF 104..116
FT /note="PRPP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01219"
SQ SEQUENCE 184 AA; 20847 MW; F36814EF79E9F953 CRC64;
MQERDLKEKA QILDDKGMRR AMVRIAHEII ERNKGVENVA LIGIRRRGVP LAQRLAKYIS
DIEGTNVPVG ILDITLYRDD LTTLANQPQV HQTEVNFPVT GKKLVLVDDV LYTGRTVRAA
LDAIMDLGRP EVVQLAVLID RGHREIPIRA DYVGKNVPTS RKEVISVRLT EIDQEERVVI
LERI
//