UMPS_BOVIN
ID UMPS_BOVIN Reviewed; 480 AA.
AC P31754; Q2KHV1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8444356; DOI=10.1016/0378-1119(93)90412-v;
RA Schoeber S., Detlef S., Schwenger B.;
RT "Sequence of the cDNA encoding bovine uridine monophosphate synthase.";
RL Gene 124:307-308(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8486364; DOI=10.1006/geno.1993.1165;
RA Schwenger B., Schoeber S., Simon D.;
RT "DUMPS cattle carry a point mutation in the uridine monophosphate synthase
RT gene.";
RL Genomics 16:241-244(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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; X65125; CAA46253.1; -; mRNA.
DR EMBL; BC112872; AAI12873.1; -; mRNA.
DR PIR; JN0558; JN0558.
DR RefSeq; NP_803474.1; NM_177508.1.
DR AlphaFoldDB; P31754; -.
DR SMR; P31754; -.
DR STRING; 9913.ENSBTAP00000018248; -.
DR PaxDb; P31754; -.
DR PRIDE; P31754; -.
DR GeneID; 281568; -.
DR KEGG; bta:281568; -.
DR CTD; 7372; -.
DR eggNOG; KOG1377; Eukaryota.
DR HOGENOM; CLU_049275_1_0_1; -.
DR InParanoid; P31754; -.
DR OrthoDB; 1303452at2759; -.
DR TreeFam; TF314694; -.
DR UniPathway; UPA00070; UER00119.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000009136; 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; 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; 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 Pfam; PF00215; OMPdecase; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00336; pyrE; 1.
DR TIGRFAMs; TIGR01740; pyrF; 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_0000139648"
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"
FT CONFLICT 181
FT /note="C -> R (in Ref. 3; AAI12873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 52229 MW; 7BDD5964C340940B CRC64;
MAAADALLGS LVTGLYDVQA FKFGNFVLKS GLSSPVYIDL RGIISRPSIL NQVAEMLFQT
AENAEINFDT VCGVPYTALP LATIVCSTHE IPMLIRRKEK KDYGTKRLIE GAVNPGDTCL
IIEDVVSSGS SVWETAEVLQ KEGLKVTDAV VLVDREQGGR DNLQARGIRL HSVCTLSTVL
CILEQQKKIN AETVERVKRF IQENAFVAAN PNDSLPSVKK EPKELSFGAR AELPGTHPVA
AKLLRLMQKK ETNLCLSADV SESRELLQLA DALGSRICLL KIHVDILNDF TLDVMKELTT
LAKRHEFLIF EDRKFADIGN TVKKQYEGGV FKIASWADLV NAHAVPGSGV VKGLEEVGLP
LHRACLLVAE MSSAGTLATG SYTEAAVQMA EEHSEFVIGF ISGSRVSMKP EFLHLTPGVQ
LEAGGDNLGQ QYHSPQEVIG KRGSDIIIVG RGIIASANQL EAAKMYRKAA WEAYLSRLAV
