PYRR_COREF
ID PYRR_COREF Reviewed; 192 AA.
AC Q8FT38;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Bifunctional protein PyrR {ECO:0000255|HAMAP-Rule:MF_01219};
DE Includes:
DE RecName: Full=Pyrimidine operon regulatory protein {ECO:0000255|HAMAP-Rule:MF_01219};
DE Includes:
DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01219};
DE Short=UPRTase {ECO:0000255|HAMAP-Rule:MF_01219};
DE EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01219};
GN Name=pyrR {ECO:0000255|HAMAP-Rule:MF_01219}; OrderedLocusNames=CE1733;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
CC -!- FUNCTION: Regulates the transcription of the pyrimidine nucleotide
CC (pyr) operon in response to exogenous pyrimidines. {ECO:0000255|HAMAP-
CC Rule:MF_01219}.
CC -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC activity which is not physiologically significant. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01219};
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrR subfamily. {ECO:0000255|HAMAP-Rule:MF_01219}.
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DR EMBL; BA000035; BAC18543.1; -; Genomic_DNA.
DR RefSeq; WP_006767733.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FT38; -.
DR SMR; Q8FT38; -.
DR STRING; 196164.23493573; -.
DR EnsemblBacteria; BAC18543; BAC18543; BAC18543.
DR KEGG; cef:CE1733; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_2_1_11; -.
DR OMA; PIQPDFC; -.
DR OrthoDB; 1725260at2; -.
DR Proteomes; UP000001409; Chromosome.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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 Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..192
FT /note="Bifunctional protein PyrR"
FT /id="PRO_1000053833"
FT MOTIF 107..119
FT /note="PRPP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ SEQUENCE 192 AA; 21002 MW; D3DA8E1187C344D0 CRC64;
MSERRNTVVE LLGENDVSRT VARIAHQIIE KTALDSEGAD RVMLLGIPSG GVPLAERLAA
KIEEFSGVRV DTGAIDITLY RDDLRNKPHR ALQPTSIPSG GIDKTTVVLV DDVLFSGRTV
RAALDALRDL GRPNYIQLAV LVDRGHRQLP IRADYVGKNL PTARAEDVTV MLREIDGRDA
VTLTREEGEG DN
