UMPS_DICDI
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 03-AUG-2022, entry version 138.
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 (Slime mold).
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.DDB0214958; -.
DR PaxDb; P09556; -.
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; DHLGQQY; -.
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; 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 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
