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Database: UniProt
Entry: A0A0V0UMZ7_9BILA
LinkDB: A0A0V0UMZ7_9BILA
Original site: A0A0V0UMZ7_9BILA 
ID   A0A0V0UMZ7_9BILA        Unreviewed;       934 AA.
AC   A0A0V0UMZ7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Uridine 5'-monophosphate synthase {ECO:0000256|ARBA:ARBA00015047};
DE            EC=2.4.2.10 {ECO:0000256|ARBA:ARBA00011971};
DE            EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
GN   ORFNames=T09_11723 {ECO:0000313|EMBL:KRX52751.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52751.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX52751.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX52751.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 1/2. {ECO:0000256|ARBA:ARBA00004889}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the OMP decarboxylase
CC       family. {ECO:0000256|ARBA:ARBA00009769}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00006221}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX52751.1}.
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DR   EMBL; JYDN01000228; KRX52751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0UMZ7; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
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   CDD; cd06223; PRTases_typeI; 2.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
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; 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; 2.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF53271; PRTase-like; 2.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681}.
FT   DOMAIN          703..915
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
SQ   SEQUENCE   934 AA;  105008 MW;  3A79850009DC30CD CRC64;
     MGATGLGEHR ITVHLSSCHL LFTTTLLKMD PRYETFLTDL FHLGAIQFGE FMLKSKHTSP
     IYVDMRRLLS HPTLLNTVED LMYDYAKELE YDVICGVPYG AIPLTSALSV KRSIPMIMQR
     KDAKAYGTKK IVEGLYKPGD KCLIIEDVIT FGSSIAETAR VLRAQGLIVT DALVILDRCQ
     GASRNLENLG ITKWSLFCLP DVLLLYEGRG LISNADCQRI SSYLFNVTDK IAPSALGNGL
     QEGAKVDKTG VLSVKAASNT ASLSHNLAKH LWQIALDKKS NLCVACKSSD PKEIIAVAEL
     AQKIGKFICM LIIRSDLICK VPLVDFISEL KTCAKSKNFM IMDDRKFCDV SSIVEMQLTG
     GEWSIAKWVD FVTVLPFSGR GVFSAIRKVS AENKVACFSI LSLHAKDSLI PKEFSEQSMK
     TAEKDIDVIA GVVCSKPPVL DSRFLYMTSA DESDQALLRF EDFDEMQFLE VEYLEMNHGI
     QYADIYKVWA FIFIVLLGSI NITAIFKFET VVMRSLYETP IFVDFQLAVS YPEIMNEIEE
     LVHSCLLSNL KFHSICGVPE GGLPLASIIS VKRNIPLLLY HKTKETTVTG KVIDGVWKKS
     DNCLIVDDVL MFGHSLADAA DVLRQHELEV TDAIVLLDRC QGPENFLKSN DIRRHYDLAG
     KFVDQCTIDE RMEPLFFSPD RLSMILHPKA RKLWEIALSK HSNLCFACDL CSPREILRLV
     EAVAVNICSL KLHADLIAIK EMPDFFSRLK RLAQSKKFML INDGNYCDDS DVVVELMLNS
     ATKPASWADF VTVQCLNGSS VFEAIKRVNS DYSVACLPVV EMSTSGNFFT EEYKKRALSL
     AQQYRQIVAG FICQKRPIND PSFLYISPGV HYKRRLDDQN WRTPDKAVRF NRDDIVVVGR
     GITKEKYSRV WAYTYQQISW DAFIIMNNAA ANVE
//
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