ID A0A0D7VW55_9FLAO Unreviewed; 214 AA.
AC A0A0D7VW55;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=PK35_16710 {ECO:0000313|EMBL:KJD31029.1};
OS Tamlana nanhaiensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tamlana.
OX NCBI_TaxID=1382798 {ECO:0000313|EMBL:KJD31029.1, ECO:0000313|Proteomes:UP000032361};
RN [1] {ECO:0000313|EMBL:KJD31029.1, ECO:0000313|Proteomes:UP000032361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FHC16 {ECO:0000313|EMBL:KJD31029.1,
RC ECO:0000313|Proteomes:UP000032361};
RX PubMed=25735434; DOI=10.1007/s10482-015-0410-x;
RA Liu X., Lai Q., Du Y., Li G., Sun F., Shao Z.;
RT "Tamlana nanhaiensis sp. nov., isolated from surface seawater collected
RT from the South China Sea.";
RL Antonie Van Leeuwenhoek 107:1189-1196(2015).
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:KJD31029.1}.
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DR EMBL; JTDV01000020; KJD31029.1; -; Genomic_DNA.
DR RefSeq; WP_044627727.1; NZ_JTDV01000020.1.
DR AlphaFoldDB; A0A0D7VW55; -.
DR STRING; 1382798.PK35_16710; -.
DR PATRIC; fig|1382798.3.peg.2349; -.
DR OrthoDB; 9802134at2; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000032361; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:KJD31029.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01208}; Reference proteome {ECO:0000313|Proteomes:UP000032361};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:KJD31029.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..154
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
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 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 126..134
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 130
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ SEQUENCE 214 AA; 23764 MW; D5CD9018965FCABD CRC64;
MIFNKNTAKK TAEVLLQVKA IKLSPQEPFT WASGWKSPIY CDNRIILSFP TIRNYVRETM
AKHIEEQYGK PDAIAGVATG AIGIGMLVAE YLGLPFIYVR PDAKGHGRKN QIEGFIESGQ
NVVVVEDLIS TGKSSLNAVK ALRDAGVKVK GMVAIFTYGF KVATENFENE NVFLRTLGNY
DTLLEKALET NYITEKELQT LSAWNANPSE WNAI
//