ID Q7VA79_PROMA Unreviewed; 181 AA.
AC Q7VA79;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 115.
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:AAQ00630.1};
GN OrderedLocusNames=Pro_1586 {ECO:0000313|EMBL:AAQ00630.1};
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167539 {ECO:0000313|EMBL:AAQ00630.1, ECO:0000313|Proteomes:UP000001420};
RN [1] {ECO:0000313|EMBL:AAQ00630.1, ECO:0000313|Proteomes:UP000001420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120 {ECO:0000313|Proteomes:UP000001420};
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAQ00630.1; -; Genomic_DNA.
DR RefSeq; NP_875977.1; NC_005042.1.
DR RefSeq; WP_011125736.1; NC_005042.1.
DR AlphaFoldDB; Q7VA79; -.
DR STRING; 167539.Pro_1586; -.
DR EnsemblBacteria; AAQ00630; AAQ00630; Pro_1586.
DR KEGG; pma:Pro_1586; -.
DR PATRIC; fig|167539.5.peg.1675; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_1_0_3; -.
DR OrthoDB; 9802227at2; -.
DR Proteomes; UP000001420; 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:AAQ00630.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001420};
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}; Transferase {ECO:0000256|HAMAP-Rule:MF_01219}.
FT DOMAIN 12..152
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT MOTIF 103..115
FT /note="PRPP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01219"
SQ SEQUENCE 181 AA; 20351 MW; 0739938DDB08F71A CRC64;
MTDQNTPERV EILSKEELDR TLTRLASQIL ENISDSNKLL LLGIPTRGIQ LAEVLASELQ
SKTGHKIEQG TIDPTFYRDD LARVGTRMSP ATEISSSLEG RQVVLVDDVI FTGRTVRAAL
ESLQAWGRPQ RVMLLVMVDR SGHRELPIQP DFCGRQVPTR RTESIELRLK EIDGEEGVFL
E
//
