PYRR_AKKM8
ID PYRR_AKKM8 Reviewed; 177 AA.
AC B2ULR4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Amuc_0113;
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC 107961 / Muc;
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
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; CP001071; ACD03958.1; -; Genomic_DNA.
DR RefSeq; WP_012419173.1; NC_010655.1.
DR AlphaFoldDB; B2ULR4; -.
DR SMR; B2ULR4; -.
DR STRING; 349741.Amuc_0113; -.
DR EnsemblBacteria; ACD03958; ACD03958; Amuc_0113.
DR GeneID; 60879539; -.
DR KEGG; amu:Amuc_0113; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_2_1_0; -.
DR OMA; PIQPDFC; -.
DR OrthoDB; 1725260at2; -.
DR BioCyc; AMUC349741:G1GBX-133-MON; -.
DR Proteomes; UP000001031; 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..177
FT /note="Bifunctional protein PyrR"
FT /id="PRO_1000139183"
FT MOTIF 99..111
FT /note="PRPP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ SEQUENCE 177 AA; 19303 MW; 61C0C2CD7F2D7F42 CRC64;
MTPPSQEIVL DGPGISRALE RMAHGIVARF PGEPLAIVGL LSQGDVIARR LVDKVKELGV
EAQYGSIDIS LYRDDIFKLE ARPSLRSSNL PFSTDDMRVV LVDDVLYTGR TIRAALNALF
DYGRPARIEL ACLIDRGGRE VPIQPDYTGH VLDHAGAKVI VSMKEADGED SVVIPSH
