ID PYRF_ASPFU Reviewed; 278 AA. AC O13410; Q4X1Y3; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=Orotidine 5'-phosphate decarboxylase; DE EC=4.1.1.23; DE AltName: Full=OMP decarboxylase; DE Short=OMPDCase; DE Short=OMPdecase; DE AltName: Full=Uridine 5'-monophosphate synthase; DE Short=UMP synthase; GN Name=pyrG; ORFNames=AFUA_2G08360; OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NIH 5233 / ATCC 13073; RX PubMed=9618589; DOI=10.1007/s002940050350; RA Weidner G., D'Enfert C., Koch A., Mol P.C., Brakhage A.A.; RT "Development of a homologous transformation system for the human pathogenic RT fungus Aspergillus fumigatus based on the pyrG gene encoding orotidine 5'- RT monophosphate decarboxylase."; RL Curr. Genet. 33:378-385(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L., RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., RA Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). 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:0000255|PROSITE-ProRule:PRU10110}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC UMP from orotate: step 2/2. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y11303; CAA72161.1; -; Genomic_DNA. DR EMBL; AAHF01000001; EAL93132.1; -; Genomic_DNA. DR RefSeq; XP_755170.1; XM_750077.1. DR AlphaFoldDB; O13410; -. DR SMR; O13410; -. DR STRING; 330879.O13410; -. DR EnsemblFungi; EAL93132; EAL93132; AFUA_2G08360. DR GeneID; 3513211; -. DR KEGG; afm:AFUA_2G08360; -. DR VEuPathDB; FungiDB:Afu2g08360; -. DR eggNOG; KOG1377; Eukaryota. DR HOGENOM; CLU_030821_0_0_1; -. DR InParanoid; O13410; -. DR OMA; CLIKTHI; -. DR OrthoDB; 922at2759; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000002530; Chromosome 2. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IMP:AspGD. 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; Lyase; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1..278 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134641" FT ACT_SITE 95 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110" FT BINDING 40 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 62..64 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 93..102 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 229 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 247 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 278 AA; 30267 MW; F4CFF6703CFD0803 CRC64; MSSKSQLTYG ARASKHPNPL AKRLFEIAEA KKTNVTVSAD VTTTRELLDL ADRLGPYIAV IKTHIDILTD FSVDTINGLN VLAQKHNFLI FEDRKFIDIG NTVQKQYHGG ALRISEWAHI INCSVLPGEG IVEALAQTAS AQDFPYGPER GLLVLAEMTS KGSLATGEYT KASVDYARKY KNFVMGFVST RALTEVQSDV SSASEDEDFV VFTTGVNLSS KGDKLGQQYQ TPASAIGRGA DFIIAGRGIY AAPDPVEAAQ RYQKEGWEAY MARVCGKS //