UMPS_NAEGR
ID UMPS_NAEGR Reviewed; 494 AA.
AC Q25566;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Uridine 5'-monophosphate synthase;
DE Short=UMP synthase;
DE Includes:
DE RecName: Full=Orotate phosphoribosyltransferase;
DE Short=OPRTase;
DE EC=2.4.2.10 {ECO:0000250|UniProtKB:P11172};
DE Includes:
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23 {ECO:0000250|UniProtKB:P11172};
DE AltName: Full=OMPdecase;
GN Name=UMP;
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 30223 / NEG;
RA Remillard S.P., Lai E.Y., Fulton C.;
RT "A bifunctional UMP synthase gene from Naegleria gruberi expresses OMP
RT decarboxylase activity in bacteria and in yeast.";
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme catalyzing the last two steps of de novo
CC pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT),
CC which converts orotate to orotidine-5'-monophosphate (OMP), and
CC orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic
CC reaction that decarboxylates OMP to uridine monophosphate (UMP).
CC {ECO:0000250|UniProtKB:P11172}.
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;
CC Evidence={ECO:0000250|UniProtKB:P11172};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10382;
CC Evidence={ECO:0000250|UniProtKB:P11172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC Evidence={ECO:0000250|UniProtKB:P11172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11597;
CC Evidence={ECO:0000250|UniProtKB:P11172};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000250|UniProtKB:P11172}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000250|UniProtKB:P11172}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the OMP decarboxylase
CC family. {ECO:0000305}.
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DR EMBL; L08073; AAA29385.1; -; Genomic_DNA.
DR AlphaFoldDB; Q25566; -.
DR SMR; Q25566; -.
DR STRING; 5762.XP_002673182.1; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_82737; -.
DR eggNOG; KOG1377; Eukaryota.
DR UniPathway; UPA00070; UER00119.
DR UniPathway; UPA00070; UER00120.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006222; P:UMP biosynthetic process; ISS:UniProtKB.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01208; PyrE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR023031; OPRT.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Glycosyltransferase; Lyase; Multifunctional enzyme;
KW Pyrimidine biosynthesis; Transferase.
FT CHAIN 1..494
FT /note="Uridine 5'-monophosphate synthase"
FT /id="PRO_0000139655"
FT ACT_SITE 322
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 288..290
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 288
FT /ligand="orotidine 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:57538"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 322
FT /ligand="orotidine 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:57538"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 325
FT /ligand="orotidine 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:57538"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 325
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 385
FT /ligand="orotidine 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:57538"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 385
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 444..446
FT /ligand="orotidine 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:57538"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 444..446
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 464..465
FT /ligand="orotidine 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:57538"
FT /evidence="ECO:0000250|UniProtKB:P11172"
FT BINDING 464..465
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:P11172"
SQ SEQUENCE 494 AA; 55809 MW; ECE04004A92B0080 CRC64;
METTTIDIQA LKKELVLDLI QIGALKFGRF TLKSGIVSPF YVDLRIIGPK MLRQFSVLLY
HVMTVKGLTN MEKRVICGVP YSALTFSSCM SMTYDLPMVI CRKERKQYGT GNMVEGIYTK
NETNCILIED VITSGASIVE TAEKLENEGL LVTDALVFLT REQLPLTNGM HILKKGEKVY
NVHPCLTMTE VTQVLLDEGK MSQEQREDIL QFIGTNTFSE TKTTAVPQKK KELTFTERAE
LTNNEFSKKL FKLMEEKQTN LCVAADITSK DDLLKLADET GPEICMLKTH IDTLDDQPDE
QFTQQLKELA KKHNFLIFED RKLADIGQVV KQQYARGPFK IAQWSDLCNS HLVSGGSATV
KALKESLKEE NITEPRGLLL IAQMSTEGAT TGESTKQEAL KVALENPDFV SGFICQSKLR
DDLDQFLYCT PGVRLDVKGD SLGQQYNSPE YVVCEKKCDV IIVGRGIYHD KERQNAAKLY
RKLGWEAYQK RIQQ
