PYRE_ECOLI
ID PYRE_ECOLI Reviewed; 213 AA.
AC P0A7E3; P00495; Q2M7V6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
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:0000303|PubMed:6349999}; OrderedLocusNames=b3642, JW3617;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=6349999; DOI=10.1111/j.1432-1033.1983.tb07641.x;
RA Poulsen P., Jensen K.F., Valentin-Hansen P., Carlsson P., Lundberg L.G.;
RT "Nucleotide sequence of the Escherichia coli pyrE gene and of the DNA in
RT front of the protein-coding region.";
RL Eur. J. Biochem. 135:223-229(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6207018; DOI=10.1002/j.1460-2075.1984.tb02046.x;
RA Poulsen P., Bonekamp F., Jensen K.F.;
RT "Structure of the Escherichia coli pyrE operon and control of pyrE
RT expression by a UTP modulated intercistronic attentuation.";
RL EMBO J. 3:1783-1790(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH DIPHOSPHATE ANALOG,
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8620002; DOI=10.1021/bi952226y;
RA Henriksen A., Aghajari N., Jensen K.F., Gajhede M.;
RT "A flexible loop at the dimer interface is a part of the active site of the
RT adjacent monomer of Escherichia coli orotate phosphoribosyltransferase.";
RL Biochemistry 35:3803-3809(1996).
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 ECO:0000269|PubMed:8620002}.
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 -!- ACTIVITY REGULATION: Inhibited by sulfate and phosphate ions.
CC {ECO:0000269|PubMed:8620002}.
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:0000269|PubMed:6349999,
CC ECO:0000269|PubMed:8620002}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000255|HAMAP-Rule:MF_01208}.
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DR EMBL; X00781; CAA25358.1; -; Genomic_DNA.
DR EMBL; V01578; CAA24899.1; -; Genomic_DNA.
DR EMBL; L10328; AAA61995.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76666.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77650.1; -; Genomic_DNA.
DR PIR; D65165; XJEC.
DR RefSeq; NP_418099.1; NC_000913.3.
DR RefSeq; WP_000806177.1; NZ_STEB01000024.1.
DR PDB; 1ORO; X-ray; 2.40 A; A/B=1-213.
DR PDB; 6TAI; X-ray; 1.55 A; AAA/BBB=1-213.
DR PDB; 6TAJ; X-ray; 1.60 A; AAA/BBB=1-213.
DR PDB; 6TAK; X-ray; 1.25 A; AAA/BBB=1-213.
DR PDBsum; 1ORO; -.
DR PDBsum; 6TAI; -.
DR PDBsum; 6TAJ; -.
DR PDBsum; 6TAK; -.
DR AlphaFoldDB; P0A7E3; -.
DR SMR; P0A7E3; -.
DR BioGRID; 4259572; 15.
DR IntAct; P0A7E3; 1.
DR STRING; 511145.b3642; -.
DR jPOST; P0A7E3; -.
DR PaxDb; P0A7E3; -.
DR PRIDE; P0A7E3; -.
DR EnsemblBacteria; AAC76666; AAC76666; b3642.
DR EnsemblBacteria; BAE77650; BAE77650; BAE77650.
DR GeneID; 60902666; -.
DR GeneID; 948157; -.
DR KEGG; ecj:JW3617; -.
DR KEGG; eco:b3642; -.
DR PATRIC; fig|1411691.4.peg.3064; -.
DR EchoBASE; EB0801; -.
DR eggNOG; COG0461; Bacteria.
DR HOGENOM; CLU_074878_0_1_6; -.
DR InParanoid; P0A7E3; -.
DR OMA; MKAYQRQ; -.
DR PhylomeDB; P0A7E3; -.
DR BioCyc; EcoCyc:OROPRIBTRANS-MON; -.
DR BioCyc; MetaCyc:OROPRIBTRANS-MON; -.
DR UniPathway; UPA00070; UER00119.
DR EvolutionaryTrace; P0A7E3; -.
DR PRO; PR:P0A7E3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP:EcoCyc.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0046132; P:pyrimidine ribonucleoside 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.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosyltransferase; Magnesium;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..213
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110694"
FT BINDING 26
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 34..35
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 72..73
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 ECO:0000305|PubMed:8620002"
FT BINDING 99
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 ECO:0000305|PubMed:8620002"
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 /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208,
FT ECO:0000305|PubMed:8620002"
FT BINDING 103
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 ECO:0000305|PubMed:8620002"
FT BINDING 105
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 124..132
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 128
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 156
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT CONFLICT 133
FT /note="Missing (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1ORO"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1ORO"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1ORO"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1ORO"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1ORO"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1ORO"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1ORO"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:1ORO"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:1ORO"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:1ORO"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1ORO"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:1ORO"
SQ SEQUENCE 213 AA; 23567 MW; F618A6D0A119B9D4 CRC64;
MKPYQRQFIE FALSKQVLKF GEFTLKSGRK SPYFFNAGLF NTGRDLALLG RFYAEALVDS
GIEFDLLFGP AYKGIPIATT TAVALAEHHD LDLPYCFNRK EAKDHGEGGN LVGSALQGRV
MLVDDVITAG TAIRESMEII QANGATLAGV LISLDRQERG RGEISAIQEV ERDYNCKVIS
IITLKDLIAY LEEKPEMAEH LAAVKAYREE FGV
