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Database: UniProt
Entry: K0K9T9_SACES
LinkDB: K0K9T9_SACES
Original site: K0K9T9_SACES 
ID   K0K9T9_SACES            Unreviewed;       190 AA.
AC   K0K9T9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
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:CCH33564.1};
GN   OrderedLocusNames=BN6_63200 {ECO:0000313|EMBL:CCH33564.1};
OS   Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS   15066 / NRRL 15764).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH33564.1, ECO:0000313|Proteomes:UP000006281};
RN   [1] {ECO:0000313|EMBL:CCH33564.1, ECO:0000313|Proteomes:UP000006281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC   {ECO:0000313|Proteomes:UP000006281};
RX   PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA   Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA   Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT   "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT   comparison to the other completely sequenced Pseudonocardiaceae.";
RL   BMC Genomics 13:465-465(2012).
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}.
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DR   EMBL; HE804045; CCH33564.1; -; Genomic_DNA.
DR   RefSeq; WP_015103675.1; NC_019673.1.
DR   AlphaFoldDB; K0K9T9; -.
DR   STRING; 1179773.BN6_63200; -.
DR   KEGG; sesp:BN6_63200; -.
DR   PATRIC; fig|1179773.3.peg.6368; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_2_1_11; -.
DR   OrthoDB; 9802227at2; -.
DR   BioCyc; SESP1179773:BN6_RS30430-MONOMER; -.
DR   Proteomes; UP000006281; Chromosome.
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:CCH33564.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006281};
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:CCH33564.1}.
FT   DOMAIN          17..164
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   MOTIF           113..125
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01219"
SQ   SEQUENCE   190 AA;  20674 MW;  64EFE254DA1F862B CRC64;
     MAPRQRGATD PAGERELLSA GDVARTVARM AHQIIEKTAL DAPSAPAVVL MGIPSRGAPL
     ARRLAVKIRE FSGVAVPTGT LDVTLHRDDL RRGPTRPLET TKLPDGGIDD RLVVLVDDVL
     FSGRTIRAAL DALRDHGRPR AVQLAVLVDR GHRELPIRAD YVGKNVPTAR SEEVHVLLEE
     FDQRDGVVLR
//
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