PYRE_BACAN
ID PYRE_BACAN Reviewed; 210 AA.
AC Q81WF6; Q6HUK4; Q6KNT9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
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:0000255|HAMAP-Rule:MF_01208};
GN OrderedLocusNames=BA_4021, GBAA_4021, BAS3733;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000255|HAMAP-Rule:MF_01208}.
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DR EMBL; AE016879; AAP27748.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33138.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56035.1; -; Genomic_DNA.
DR RefSeq; NP_846262.1; NC_003997.3.
DR RefSeq; WP_000711466.1; NZ_WXXJ01000026.1.
DR RefSeq; YP_029984.1; NC_005945.1.
DR PDB; 3M3H; X-ray; 1.75 A; A=1-210.
DR PDB; 4RV4; X-ray; 2.65 A; A/B/C=1-210.
DR PDBsum; 3M3H; -.
DR PDBsum; 4RV4; -.
DR AlphaFoldDB; Q81WF6; -.
DR SMR; Q81WF6; -.
DR STRING; 260799.BAS3733; -.
DR DNASU; 1086652; -.
DR EnsemblBacteria; AAP27748; AAP27748; BA_4021.
DR EnsemblBacteria; AAT33138; AAT33138; GBAA_4021.
DR GeneID; 45023711; -.
DR KEGG; ban:BA_4021; -.
DR KEGG; bar:GBAA_4021; -.
DR KEGG; bat:BAS3733; -.
DR PATRIC; fig|198094.11.peg.3992; -.
DR eggNOG; COG0461; Bacteria.
DR HOGENOM; CLU_074878_1_1_9; -.
DR OMA; ENPFTWA; -.
DR UniPathway; UPA00070; UER00119.
DR EvolutionaryTrace; Q81WF6; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
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; Glycosyltransferase; Magnesium; Pyrimidine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..210
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110665"
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 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 HELIX 1..11
FT /evidence="ECO:0007829|PDB:3M3H"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:3M3H"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3M3H"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:3M3H"
FT HELIX 44..61
FT /evidence="ECO:0007829|PDB:3M3H"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:3M3H"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:4RV4"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:3M3H"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:3M3H"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3M3H"
FT STRAND 115..126
FT /evidence="ECO:0007829|PDB:3M3H"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:3M3H"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:3M3H"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:3M3H"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3M3H"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:3M3H"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:3M3H"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4RV4"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:3M3H"
SQ SEQUENCE 210 AA; 22714 MW; 0FB8FABEBB5E54B6 CRC64;
MKKEIASHLL EIGAVFLQPN DPFTWSSGMK SPIYCDNRLT LSYPKVRQTI AAGLEELIKE
HFPTVEVIAG TATAGIAHAA WVSDRMDLPM CYVRSKAKGH GKGNQIEGKA EKGQKVVVVE
DLISTGGSAI TCVEALREAG CEVLGIVSIF TYELEAGKEK LEAANVASYS LSDYSALTEV
AAEKGIIGQA ETKKLQEWRK NPADEAWITA
