ID G6C4Q8_9FUSO Unreviewed; 162 AA.
AC G6C4Q8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
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 ORFNames=HMPREF9093_01553 {ECO:0000313|EMBL:EHI78199.1};
OS Fusobacterium sp. oral taxon 370 str. F0437.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=861452 {ECO:0000313|EMBL:EHI78199.1, ECO:0000313|Proteomes:UP000003908};
RN [1] {ECO:0000313|EMBL:EHI78199.1, ECO:0000313|Proteomes:UP000003908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0437 {ECO:0000313|EMBL:EHI78199.1,
RC ECO:0000313|Proteomes:UP000003908};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHI78199.1}.
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DR EMBL; AGAD01000189; EHI78199.1; -; Genomic_DNA.
DR AlphaFoldDB; G6C4Q8; -.
DR STRING; 861452.HMPREF9093_01553; -.
DR PATRIC; fig|861452.3.peg.1410; -.
DR eggNOG; COG0461; Bacteria.
DR HOGENOM; CLU_074878_1_1_0; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000003908; Unassembled WGS sequence.
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 NCBIfam; TIGR00336; pyrE; 1.
DR PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01208}; Transferase {ECO:0000256|HAMAP-Rule:MF_01208}.
FT DOMAIN 6..121
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT BINDING 54
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 58
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 60
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 80..88
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 84
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ SEQUENCE 162 AA; 17986 MW; 9CC18E5B6CC142E0 CRC64;
MSYPKIRKQI AEGFVEKIKE LYPNVDYIVG TATAGIPHAA WISDIMDLPM LYVRGSAKDH
GKTNQIEGKY EKGKKVVVIE DLISTGKSSV LAAQALQEEG LEVLGVIAIF SYNLNKAKEK
FDEAKIPFST LTNYDVLLEL AKETGLIGDK ENQILVAWRN NL
//