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Database: UniProt
Entry: A0A0F0I645_ASPPU
LinkDB: A0A0F0I645_ASPPU
Original site: A0A0F0I645_ASPPU 
ID   A0A0F0I645_ASPPU        Unreviewed;       277 AA.
AC   A0A0F0I645;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00021923, ECO:0000256|RuleBase:RU000512};
DE            EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321, ECO:0000256|RuleBase:RU000512};
GN   ORFNames=P875_00042298 {ECO:0000313|EMBL:KJK61423.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61423.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK61423.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU000512};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861,
CC       ECO:0000256|RuleBase:RU000512}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00011018, ECO:0000256|RuleBase:RU000512}.
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:KJK61423.1}.
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DR   EMBL; JZEE01000675; KJK61423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I645; -.
DR   STRING; 1403190.A0A0F0I645; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000033540; 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; 1.
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   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   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   ECO:0000256|RuleBase:RU000512};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000512};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975,
KW   ECO:0000256|RuleBase:RU000512};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   DOMAIN          34..262
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
SQ   SEQUENCE   277 AA;  30310 MW;  C49F7E037B112977 CRC64;
     MSSKSQLTYS ARASKHPNAL VKKLFEVAEA KKTNVTVSAD VTTTKELLDL ADRLGPYIAV
     IKTHIDILSD FSEETITGLK ALAEKHNFLI FEDRKFIDIG NTVQKQYHGG TLRISEWAHI
     INCSILPGEG IVEALAQTAS AEDFPYGSER GLLILAEMTS KGSLATGQYT TSSVDYARKY
     KKFVMGFVST RHLGEVQSEV SSPSEEEDFV VFTTGVNLSS KGDKLGQQYQ TPESAVGRGA
     DFIIAGRGIY AAPDPVEAAK RYQKEGWDAY LKRVGAQ
//
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