ID F8C482_THEGP Unreviewed; 322 AA.
AC F8C482;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208};
DE Short=OPRT {ECO:0000256|HAMAP-Rule:MF_01208};
DE Short=OPRTase {ECO:0000256|HAMAP-Rule:MF_01208};
DE EC=2.4.2.10 {ECO:0000256|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208};
GN Name=pyrE {ECO:0000256|HAMAP-Rule:MF_01208};
GN OrderedLocusNames=TOPB45_0524 {ECO:0000313|EMBL:AEH22626.1};
OS Thermodesulfobacterium geofontis (strain OPF15).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH22626.1, ECO:0000313|Proteomes:UP000006583};
RN [1] {ECO:0000313|EMBL:AEH22626.1, ECO:0000313|Proteomes:UP000006583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF15 {ECO:0000313|EMBL:AEH22626.1,
RC ECO:0000313|Proteomes:UP000006583};
RX PubMed=23580711; DOI=10.1128/genomea.00162-13;
RA Elkins J.G., Hamilton-Brehm S.D., Lucas S., Han J., Lapidus A., Cheng J.F.,
RA Goodwin L.A., Pitluck S., Peters L., Mikhailova N., Davenport K.W.,
RA Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L., Kyrpides N.C.,
RA Ivanova N.N., Pagani I., Bruce D., Woyke T., Cottingham R.W.;
RT "Complete genome sequence of the hyperthermophilic sulfate-reducing
RT bacterium Thermodesulfobacterium geofontis OPF15T.";
RL Genome Announc. 1:E0016213-E0016213(2013).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01208};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01208};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000256|ARBA:ARBA00004889,
CC ECO:0000256|HAMAP-Rule:MF_01208}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01208}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000256|HAMAP-Rule:MF_01208}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01208}.
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DR EMBL; CP002829; AEH22626.1; -; Genomic_DNA.
DR RefSeq; WP_013909326.1; NC_015682.1.
DR AlphaFoldDB; F8C482; -.
DR STRING; 795359.TOPB45_0524; -.
DR KEGG; top:TOPB45_0524; -.
DR PATRIC; fig|795359.3.peg.531; -.
DR eggNOG; COG0461; Bacteria.
DR HOGENOM; CLU_863140_0_0_0; -.
DR OrthoDB; 9785917at2; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000006583; Chromosome.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
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 Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR HAMAP; MF_01208; PyrE; 1.
DR InterPro; IPR023031; OPRT.
DR InterPro; IPR004467; Or_phspho_trans_dom.
DR InterPro; IPR009875; PilZ_domain.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR NCBIfam; TIGR00336; pyrE; 1.
DR PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR Pfam; PF07238; PilZ; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF141371; PilZ domain-like; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW ECO:0000313|EMBL:AEH22626.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01208}; Reference proteome {ECO:0000313|Proteomes:UP000006583};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:AEH22626.1}.
FT DOMAIN 2..97
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
FT DOMAIN 233..293
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT BINDING 228
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:0000256|HAMAP-Rule:MF_01208"
FT BINDING 229
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:0000256|HAMAP-Rule:MF_01208"
FT BINDING 232
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:0000256|HAMAP-Rule:MF_01208"
FT BINDING 254..262
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:0000256|HAMAP-Rule:MF_01208"
FT BINDING 258
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT BINDING 286
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ SEQUENCE 322 AA; 36675 MW; 4BA796E2E7F434A5 CRC64;
MKRKFSRIPI SNTVEFFWQN KSYEGVLKDL SYGGLYIESK IIPSIDEEIP IVLFLEGTHP
SIKLFFKGKV VRTNKEGFAV KYTYISPESF EHFKNFVNYN YPSLEIAEKE VYRFLGEAHP
LFKGFINLNI LALKNEILKF ILERAFLYSP DKPFILSSGK ESPYYLDCRK ITLYSLTFGL
VGALFWQKIK YLGVDGVAGM SIGADPIVCS ILAKANEEDI SLEGIFVRKE PKKYGTQKQI
EGNIRGGMDI VLVEDVVTTG SSVLKAAEIL EKEKLHIIKI FALVDREEGG KENIEAKGYE
FEAFFTLSEI LKRHQELSNK NA
//
