ID A0A0N0RTR2_9HYPO Unreviewed; 394 AA.
AC A0A0N0RTR2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00021923};
DE EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
DE AltName: Full=OMP decarboxylase {ECO:0000256|ARBA:ARBA00033428};
DE AltName: Full=Uridine 5'-monophosphate synthase {ECO:0000256|ARBA:ARBA00031744};
GN ORFNames=ESCO_005451 {ECO:0000313|EMBL:KOS20572.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS20572.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS20572.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00011018}.
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:KOS20572.1}.
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DR EMBL; LGSR01000017; KOS20572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0RTR2; -.
DR STRING; 150374.A0A0N0RTR2; -.
DR OrthoDB; 922at2759; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000053831; Unassembled WGS sequence.
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; cd04725; OMP_decarboxylase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR32119:SF2; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT DOMAIN 36..381
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT REGION 160..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 42948 MW; DB808D81ADA35144 CRC64;
MPSHPTLKAT FAERAETSRH PLTSYLFRLM DLKASNLCLS ADVPTARELL SLADSIGPSI
VVLKTHYDMV TGWDFHPETG TGAKLASLAR KHGFLIFEDR KFGDIGHTVE LQYTSGAARI
IDWAHITNVN MVPGKASVTS LAKAAARWLE RYPCEVRTSV TVGTPNMDQF GDDDDNNDNK
DKDYKNNNND ADDHKMGDQT GTNGTAPAEG ASQSRQSREG RKGSIVSVTT VTQQYESVAS
SRLGKTISED EEAPFPGIEE APLTRGLLIL AQMSSQGNFM NKEYTQACVE AAREHPDFVM
GFVAQECLNT EPEDAFIHMT PGCQLPPEDH AGDANGIVGG DGQGQQYNTP HKIINVCGTD
IAIVGRGIIK ADDPIGEADR YRSAAWKAYT ERVR
//
