ID S2E5J6_9ARCH Unreviewed; 201 AA.
AC S2E5J6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ECO:0000313|EMBL:EPA04771.1};
GN ORFNames=BG20_I1735 {ECO:0000313|EMBL:EPA04771.1};
OS Candidatus Nitrosarchaeum limnium BG20.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosarchaeum.
OX NCBI_TaxID=859192 {ECO:0000313|EMBL:EPA04771.1, ECO:0000313|Proteomes:UP000014065};
RN [1] {ECO:0000313|EMBL:EPA04771.1, ECO:0000313|Proteomes:UP000014065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BG20 {ECO:0000313|EMBL:EPA04771.1,
RC ECO:0000313|Proteomes:UP000014065};
RX PubMed=22461554; DOI=10.1128/JB.00007-12;
RA Mosier A.C., Allen E.E., Kim M., Ferriera S., Francis C.A.;
RT "Genome Sequence of "Candidatus Nitrosoarchaeum limnia" BG20, a Low-
RT Salinity Ammonia-Oxidizing Archaeon from the San Francisco Bay Estuary.";
RL J. Bacteriol. 194:2119-2120(2012).
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:EPA04771.1}.
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DR EMBL; AHJG01000260; EPA04771.1; -; Genomic_DNA.
DR RefSeq; WP_007402299.1; NZ_AHJG01000260.1.
DR AlphaFoldDB; S2E5J6; -.
DR PATRIC; fig|859192.6.peg.1930; -.
DR OrthoDB; 9089at2157; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000014065; 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:EPA04771.1}; 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:UP000014065};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:EPA04771.1}.
FT DOMAIN 50..160
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT BINDING 95
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 99
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 121..129
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 125
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT BINDING 153
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ SEQUENCE 201 AA; 22465 MW; 4B2E2FEE4CC18E5E CRC64;
MEFVKEFSTF LYQKGVIKFG DFTLASGKKS SYYVDLRLVP SYPHQFRSMI KHLQNNIIDN
TGLDRFDSLV SVPTGGLIIA SALAIETVKP LIYVRSKPKD YGTSKSVEGQ ITKGMKVVMI
DDVATTGGSV VNAIKSLRES DIVIEDAYVI VNRMEGAEET LKELGVKMYS LVNIIQITQA
LHEQKLVSDD ILEKVRKQIE K
//
