ID R5V6M7_9FIRM Unreviewed; 226 AA.
AC R5V6M7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=BN518_00412 {ECO:0000313|EMBL:CCZ79106.1};
OS Roseburia sp. CAG:18.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1262941 {ECO:0000313|EMBL:CCZ79106.1, ECO:0000313|Proteomes:UP000018230};
RN [1] {ECO:0000313|EMBL:CCZ79106.1, ECO:0000313|Proteomes:UP000018230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:18 {ECO:0000313|Proteomes:UP000018230};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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|ARBA:ARBA00003769,
CC 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|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01208}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000256|ARBA:ARBA00006340,
CC 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:CCZ79106.1}.
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DR EMBL; CBAP010000140; CCZ79106.1; -; Genomic_DNA.
DR AlphaFoldDB; R5V6M7; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000018230; 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; PTHR46683; OROTATE PHOSPHORIBOSYLTRANSFERASE 1-RELATED; 1.
DR PANTHER; PTHR46683:SF1; OROTATE PHOSPHORIBOSYLTRANSFERASE 1-RELATED; 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 ECO:0000313|EMBL:CCZ79106.1}; 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:UP000018230};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:CCZ79106.1}.
FT DOMAIN 43..163
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
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:0000256|HAMAP-Rule:MF_01208"
FT BINDING 73..74
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 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:0000256|HAMAP-Rule:MF_01208"
FT BINDING 101
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 104
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 106
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 128..136
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 132
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT BINDING 161
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ SEQUENCE 226 AA; 25047 MW; 4EAFC2A2C99C3D1F CRC64;
MESYKSEFIE FMVESDVLKF GDFTLKSGRK SPFFMNAGAY VTGSQLKKLG EYYAKAIHAS
YGDDFDVLFG PAYKGIPLAV VTAIAFSELY GKEIRYCSDR KEAKDHGADK GGFLGSSLKD
GDRVVMIEDV TTSGKSMEET VPKVRGAANV EIVGLMVSLN RMEVGQGGVK SALDEIHEKY
GFEGKAIVTM EEVVEHLYNR ECQGRIVIDD TIRKAIDAYY EQYGCK
//
