ID   UMPS_DICDI              Reviewed;         478 AA.
AC   P09556; Q54VT6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   24-JAN-2024, entry version 144.
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:0000305|PubMed:2835631};
DE   Includes:
DE     RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE              EC=4.1.1.23 {ECO:0000305|PubMed:2835631};
DE     AltName: Full=OMPdecase;
GN   Name=pyr56; Synonyms=pyr5-6; ORFNames=DDB_G0280041;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=AX3;
RX   PubMed=2835631; DOI=10.1007/bf00425698;
RA   Jacquet M., Guilbaud R., Garreau H.;
RT   "Sequence analysis of the DdPYR5-6 gene coding for UMP synthase in
RT   Dictyostelium discoideum and comparison with orotate phosphoribosyl
RT   transferases and OMP decarboxylases.";
RL   Mol. Gen. Genet. 211:441-445(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
CC   -!- FUNCTION: Participates in the last two steps of the pyrimidine
CC       biosynthetic pathway leading to UMP synthesis.
CC       {ECO:0000303|PubMed:2835631}.
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:0000305|PubMed:2835631};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10382;
CC         Evidence={ECO:0000305|PubMed:2835631};
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:0000305|PubMed:2835631};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11597;
CC         Evidence={ECO:0000305|PubMed:2835631};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 1/2. {ECO:0000305|PubMed:2835631}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000305|PubMed:2835631}.
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; X07560; CAA30443.1; -; Genomic_DNA.
DR   EMBL; AAFI02000035; EAL67247.1; -; Genomic_DNA.
DR   PIR; S03826; S03826.
DR   RefSeq; XP_641269.1; XM_636177.1.
DR   AlphaFoldDB; P09556; -.
DR   SMR; P09556; -.
DR   STRING; 44689.P09556; -.
DR   PaxDb; 44689-DDB0214958; -.
DR   EnsemblProtists; EAL67247; EAL67247; DDB_G0280041.
DR   GeneID; 8622401; -.
DR   KEGG; ddi:DDB_G0280041; -.
DR   dictyBase; DDB_G0280041; pyr56.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_049275_1_0_1; -.
DR   InParanoid; P09556; -.
DR   OMA; SAKHVCG; -.
DR   PhylomeDB; P09556; -.
DR   Reactome; R-DDI-500753; Pyrimidine biosynthesis.
DR   UniPathway; UPA00070; UER00119.
DR   UniPathway; UPA00070; UER00120.
DR   PRO; PR:P09556; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IGI:dictyBase.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IMP:dictyBase.
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:0019856; P:pyrimidine nucleobase biosynthetic process; IGI:dictyBase.
DR   GO; GO:0006222; P:UMP biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Decarboxylase; Glycosyltransferase; Lyase; Multifunctional enzyme;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..478
FT                   /note="Uridine 5'-monophosphate synthase"
FT                   /id="PRO_0000139651"
FT   REGION          1..210
FT                   /note="OPRTase"
FT   REGION          211..229
FT                   /note="Domain linker"
FT                   /evidence="ECO:0000255"
FT   REGION          230..478
FT                   /note="OMPdecase"
FT   ACT_SITE        311
FT                   /note="For OMPdecase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   ACT_SITE        313
FT                   /note="For OMPdecase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   ACT_SITE        316
FT                   /note="For OMPdecase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         258
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         280..282
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         280
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         313
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         316
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         316
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         320
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         320
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         371
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         371
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   CONFLICT        11..14
FT                   /note="NEID -> MKLM (in Ref. 1; CAA30443)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="Q -> E (in Ref. 1; CAA30443)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337
FT                   /note="D -> V (in Ref. 1; CAA30443)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   478 AA;  52519 MW;  0A5F45A4B0738636 CRC64;
     MNIKELVLKL NEIDAIKLGE FKLKSGIISP IYIDLRVTVS SPPLLAAIAE MMYQKVYKSG
     NAQETPALVC GVPYTALPIA TGMSIANNIP MVVRRKEAKA YGTKQLIEGR FKEGDNVLVV
     EDLVTSGASV LETVRDLNSV GLKVTDVVVL LDRQQGARQA LEKQGYRLHS VFTMEELINT
     LIEAGKLTGR TLELVQSFLD ANRNVVVPLP PTLAPPAPAP IVINKPFEER AKLASNPMAS
     KLFTLMSSKK TNLAVAADLT DKQQLLDLAE SIGSEICVLK THVDIIDNYD EEFIKSLKCI
     AAKHNFLIFE DRKFADIGNT VKYQFENGVY KISKWADMVT VHGVAGSSIV DGFKSGLKEY
     GSGLLLLAQM SSKGSLCVGD YTTQMIEMAN NNKEEVMGLI CQERLPSMTD GLVLMTPGVQ
     FNSTGDAMGQ QYNTPEYIIK EKNTDVIIVG RGIYQSNDPK SVANKYRTAA WETYQSKF
//