PYRR_SYNFM
ID PYRR_SYNFM Reviewed; 186 AA.
AC A0LH56;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=Sfum_1064;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK16758.1; -; Genomic_DNA.
DR RefSeq; WP_011697929.1; NC_008554.1.
DR AlphaFoldDB; A0LH56; -.
DR SMR; A0LH56; -.
DR STRING; 335543.Sfum_1064; -.
DR PRIDE; A0LH56; -.
DR EnsemblBacteria; ABK16758; ABK16758; Sfum_1064.
DR KEGG; sfu:Sfum_1064; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_2_1_7; -.
DR OMA; PIQPDFC; -.
DR OrthoDB; 1725260at2; -.
DR Proteomes; UP000001784; 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..186
FT /note="Bifunctional protein PyrR"
FT /id="PRO_1000053880"
FT MOTIF 101..113
FT /note="PRPP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ SEQUENCE 186 AA; 20806 MW; 751A7DFA7414E838 CRC64;
MVENGSRVVM EARDIRSALE RLAREIVEQP VDPNGLALVG IHTGGVFLAK RLETLISKKL
KHSIPVGTLD ITLYRDDWTR LHTQPVVRAT NLPFPMDDRD VVLVDDVLYT GRTIRAALDA
LIDYGRPKRV QVAALVDRGH RELPICGQFI GIELKTRSDE QVNVLLKEKD GVDRVVIEQA
AQARKA
