PYRE_MYCTU
ID PYRE_MYCTU Reviewed; 179 AA.
AC P9WHK9; L0T6H8; O53717; P0A5U0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208};
DE Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208};
DE Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208};
DE EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208};
GN Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208}; Synonyms=umpA;
GN OrderedLocusNames=Rv0382c; ORFNames=MTV036.17c;
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 AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
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: Catalyzes the transfer of a ribosyl phosphate group from 5-
CC phosphoribose 1-diphosphate to orotate, leading to the formation of
CC orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01208};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01208};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000255|HAMAP-Rule:MF_01208}.
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DR EMBL; AL123456; CCP43112.1; -; Genomic_DNA.
DR PIR; A70834; A70834.
DR RefSeq; WP_003401894.1; NZ_NVQJ01000002.1.
DR RefSeq; YP_177723.1; NC_000962.3.
DR PDB; 5HKF; X-ray; 2.25 A; A/B=1-179.
DR PDB; 5HKI; X-ray; 2.40 A; A/B/C/D=1-179.
DR PDB; 5HKL; X-ray; 1.90 A; A/B=1-179.
DR PDBsum; 5HKF; -.
DR PDBsum; 5HKI; -.
DR PDBsum; 5HKL; -.
DR AlphaFoldDB; P9WHK9; -.
DR SMR; P9WHK9; -.
DR STRING; 83332.Rv0382c; -.
DR PaxDb; P9WHK9; -.
DR DNASU; 886443; -.
DR GeneID; 45424348; -.
DR GeneID; 886443; -.
DR KEGG; mtu:Rv0382c; -.
DR TubercuList; Rv0382c; -.
DR eggNOG; COG0461; Bacteria.
DR OMA; YVNCKPV; -.
DR PhylomeDB; P9WHK9; -.
DR BRENDA; 2.4.2.10; 3445.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006222; P:UMP biosynthetic process; IBA:GO_Central.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01208; PyrE; 1.
DR InterPro; IPR023031; OPRT.
DR InterPro; IPR004467; Or_phspho_trans_dom.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00336; pyrE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Magnesium; Pyrimidine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..179
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110712"
FT BINDING 94
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 95
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 98
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 100
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 120..128
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 124
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 152
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5HKF"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:5HKL"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:5HKL"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:5HKL"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:5HKL"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:5HKL"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:5HKI"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 114..126
FT /evidence="ECO:0007829|PDB:5HKL"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5HKL"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:5HKL"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:5HKL"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:5HKL"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:5HKL"
SQ SEQUENCE 179 AA; 18892 MW; 92E6A3AEDB2ECAB0 CRC64;
MAGPDRAELA ELVRRLSVVH GRVTLSSGRE ADYYVDLRRA TLHHRASALI GRLMRELTAD
WDYSVVGGLT LGADPVATAI MHAPGRPIDA FVVRKSAKAH GMQRLIEGSE VTGQRVLVVE
DTSTTGNSAL TAVHAVQDVG GEVVGVATVV DRATGAAEAI EAEGLRYRSV LGLADLGLD
