PYRR_MYCTU
ID PYRR_MYCTU Reviewed; 193 AA.
AC P9WHK3; L0T9G5; P65941; P71807;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=Rv1379;
GN ORFNames=MTCY02B12.13;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(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; AL123456; CCP44138.1; -; Genomic_DNA.
DR PIR; H70958; H70958.
DR RefSeq; NP_215895.1; NC_000962.3.
DR RefSeq; WP_003407196.1; NZ_NVQJ01000050.1.
DR PDB; 1W30; X-ray; 1.90 A; A/B=1-193.
DR PDB; 5IAO; X-ray; 2.60 A; A/B/C/D/E/F=1-193.
DR PDBsum; 1W30; -.
DR PDBsum; 5IAO; -.
DR AlphaFoldDB; P9WHK3; -.
DR SMR; P9WHK3; -.
DR STRING; 83332.Rv1379; -.
DR PaxDb; P9WHK3; -.
DR GeneID; 886769; -.
DR KEGG; mtu:Rv1379; -.
DR TubercuList; Rv1379; -.
DR eggNOG; COG2065; Bacteria.
DR OMA; PIQPDFC; -.
DR PhylomeDB; P9WHK3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..193
FT /note="Bifunctional protein PyrR"
FT /id="PRO_0000183046"
FT MOTIF 115..127
FT /note="PRPP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
FT BINDING 57..58
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 119..127
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1W30"
FT HELIX 19..36
FT /evidence="ECO:0007829|PDB:1W30"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:1W30"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5IAO"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1W30"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:1W30"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1W30"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1W30"
FT STRAND 114..125
FT /evidence="ECO:0007829|PDB:1W30"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:1W30"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:1W30"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1W30"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1W30"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1W30"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:1W30"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1W30"
SQ SEQUENCE 193 AA; 20627 MW; 07A499B7D4E66159 CRC64;
MGAAGDAAIG RESRELMSAA DVGRTISRIA HQIIEKTALD DPVGPDAPRV VLLGIPTRGV
TLANRLAGNI TEYSGIHVGH GALDITLYRD DLMIKPPRPL ASTSIPAGGI DDALVILVDD
VLYSGRSVRS ALDALRDVGR PRAVQLAVLV DRGHRELPLR ADYVGKNVPT SRSESVHVRL
REHDGRDGVV ISR
