ID   UMPS_PONAB              Reviewed;         480 AA.
AC   Q5R514;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   13-SEP-2023, entry version 90.
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=UMPS;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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   -!- SUBUNIT: Homodimer; dimerization is required for enzymatic activity.
CC       {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; CR861071; CAH93152.1; -; mRNA.
DR   RefSeq; NP_001126858.1; NM_001133386.1.
DR   AlphaFoldDB; Q5R514; -.
DR   SMR; Q5R514; -.
DR   STRING; 9601.ENSPPYP00000015062; -.
DR   GeneID; 100173867; -.
DR   KEGG; pon:100173867; -.
DR   CTD; 7372; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   InParanoid; Q5R514; -.
DR   OrthoDB; 922at2759; -.
DR   UniPathway; UPA00070; UER00119.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001595; Unplaced.
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; cd04725; OMP_decarboxylase_like; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01208; PyrE; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00336; pyrE; 1.
DR   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Decarboxylase; Glycosyltransferase; Lyase;
KW   Multifunctional enzyme; Phosphoprotein; Pyrimidine biosynthesis;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   CHAIN           2..480
FT                   /note="Uridine 5'-monophosphate synthase"
FT                   /id="PRO_0000257814"
FT   REGION          2..214
FT                   /note="OPRTase"
FT   REGION          215..220
FT                   /note="Domain linker"
FT   REGION          221..480
FT                   /note="OMPdecase"
FT   ACT_SITE        314
FT                   /note="For OMPdecase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   ACT_SITE        317
FT                   /note="For OMPdecase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         257
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         257
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         259
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         281..283
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         281
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         314
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         317
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         317
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         321
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         321
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         372
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         372
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         430..432
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         430..432
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         450..451
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         450..451
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   MOD_RES         37
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
SQ   SEQUENCE   480 AA;  52128 MW;  18DBEA8FCF5DB6BC CRC64;
     MAAVGAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADTLFQT
     AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL
     IIEDVVTSGS SVLETAEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML
     EILEQQKKID AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFSAR AELPRIHPVA
     SKLLRLMQKK ETNLCLSADV SEARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT
     LAKRHEFLIF EDRKFADIGN TVKKQYEGGV FKIASWADLV NAHVVPGSGV VKGLQEVGLP
     LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ
     LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADCL EAAEMYRKAA WEAYLSRLGV
//