ID A0A0V1M4M8_9BILA Unreviewed; 945 AA.
AC A0A0V1M4M8;
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};
DE Flags: Fragment;
GN Name=UMPS {ECO:0000313|EMBL:KRZ66771.1};
GN ORFNames=T10_13510 {ECO:0000313|EMBL:KRZ66771.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ66771.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ66771.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ66771.1};
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:KRZ66771.1}.
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DR EMBL; JYDO01000225; KRZ66771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1M4M8; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000054843; 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:UP000054843}.
FT DOMAIN 714..926
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ66771.1"
SQ SEQUENCE 945 AA; 106721 MW; 6BBD30D4CAD0F1A1 CRC64;
LSSCHLLLTT TSLMMDAKYE RFLTDLFHLG VIQFGEFLLK SNHTSPIYVD MRRLLSHPTL
LNTVEDFMYE YAKELEYDVI CGVPYGAIPL TSALSVKRCI PMIMQRKDAK SYGTKKIVEG
LYKPGDKCLI IEDVITFGSS IAETARVLRA QGLIVTDALV ILDRCQGASR NLENLGITKW
SLFLLPDVLL LYEDRGLISN ADCQRISSYL FNVTDKIAPS ELENGLQEGA KVDKAGVWSV
KAAKNSASLS HCLAKQLWEI AINKKSNLCV ACKLSDPKEI IALAQKIGQF ICMLIIRSDL
IFKHPLVDFI SELKACAKSN NFMIMDDRKF CDVSSIVEMQ LTGGEWSIAN WVDFITVLPF
SGRGVFSAIR QIKTENNFAC FSVLSLHAKD SLVPKEFSEQ DIDVVAGVVC SKPPILDSRF
LYMTAADESD QAVLRVEDFD EMQFLDVEYL EMNHGIQYAD IYKVWACVET SPQVVVKMID
ECKALLKKLF HIGIFKFETV VMRSVYETPI FVDFQLAISY PEIMNKIEEL MYSCLLPNLK
FHSICGVPEG GLPLASIISV KRNIPLLMYH KTKETTVTEK VIDGVWKKSD NCLIVDDVLM
FGHSLVDAAD VLRQHELEVT DAIVILDRCQ GPDNFLRSND VLSYLNEQAL LTDFECLKIS
NHLLAFSDLA GKFIDQYAIE EMMEPLFFSP DRLSVICHPS ARRLWEIALS KQSNLCLACD
LCSPSEILKL VEDVSVNICS LKLHADMITV SEMPDFFLKL KELSQAHKFM LINDGNYCDD
SDVVVDLMMN SPTKPASWAD FVTVQCLNGP SVFEAIQKVN KHYNVACLPV VEMSTSGNFF
TEEYKKRALS LAQEYRQIVG GFICQKRPIN DPSFLYISPG VHYKRGMEDQ NWRTPDKAVR
FNRDDIIVVG RGITKETYSR VWAYTYQQIS WDAFMIMNSA AANID
//
