ID   PYRR_CORGL              Reviewed;         192 AA.
AC   P59011;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
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};
GN   OrderedLocusNames=Cgl1613, cg1817;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAF21622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000036; BAB99006.1; -; Genomic_DNA.
DR   EMBL; BX927152; CAF21622.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_600827.1; NC_003450.3.
DR   RefSeq; WP_003862208.1; NC_006958.1.
DR   AlphaFoldDB; P59011; -.
DR   SMR; P59011; -.
DR   STRING; 196627.cg1817; -.
DR   World-2DPAGE; 0001:P59011; -.
DR   KEGG; cgb:cg1817; -.
DR   KEGG; cgl:Cgl1613; -.
DR   PATRIC; fig|196627.13.peg.1575; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_2_1_11; -.
DR   OMA; PIQPDFC; -.
DR   Proteomes; UP000000582; 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_0000183033"
FT   MOTIF           107..119
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
FT   BINDING         49..50
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         111..119
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  20952 MW;  F709F51AA9294A95 CRC64;
     MSERNSAVLE LLNEDDVSRT IARIAHQIIE KTALDSKDAD RVMLLGIPSG GVPLARRLAE
     KIEEFSGVSV DTGAVDITLY RDDLRNKPHR ALQPTSIPAG GIDNTTVILV DDVLFSGRTI
     RAALDALRDV GRPNYIQLAV LVDRGHRQLP IRADYVGKNL PTARAEDVSV MLTEIDGRDA
     VTLTREDSEG DS