ID A0A1L8PCE2_9LACT Unreviewed; 208 AA.
AC A0A1L8PCE2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AX762_09240 {ECO:0000313|EMBL:OJF92931.1};
OS Alkalibacterium sp. 20.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1798803 {ECO:0000313|EMBL:OJF92931.1, ECO:0000313|Proteomes:UP000182750};
RN [1] {ECO:0000313|EMBL:OJF92931.1, ECO:0000313|Proteomes:UP000182750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20 {ECO:0000313|EMBL:OJF92931.1,
RC ECO:0000313|Proteomes:UP000182750};
RA Wang D., Kot W., Qin Y., Naqvi K., Hansen L., Rensing C.;
RT "Genome sequencing of a beta-galactosidase producing bacteria
RT Alkalibacterium sp. 20.";
RL Submitted (FEB-2016) 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:OJF92931.1}.
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DR EMBL; LSRN01000035; OJF92931.1; -; Genomic_DNA.
DR RefSeq; WP_071848437.1; NZ_LSRN01000035.1.
DR AlphaFoldDB; A0A1L8PCE2; -.
DR STRING; 1798803.AX762_09240; -.
DR OrthoDB; 9802134at2; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000182750; 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 ECO:0000313|EMBL:OJF92931.1}; 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:UP000182750};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:OJF92931.1}.
FT DOMAIN 57..156
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT BINDING 96
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 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 102
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 122..130
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 126
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ SEQUENCE 208 AA; 22872 MW; 668E8934BD02136F CRC64;
MISKETIPEE LLRIGAVNVR PKQPYTWTSG LKSPIYCDNR LTMSYPVVRE QIVTALVELI
MKYYPEVEVI AGTATAGIPH AAWVADRLTL PMVYIRGEAK KHGTGKQIEG TFKSGAKLVV
IEDLISTGQS VIDAVNVAKS QGAEVLGVAA IFTYELSLGK SAFDDLNIEN HSVTDYTSLV
QAAFRTGVIE QDDLEALEKW NKNPETWS
//