ID PYRF_PICST Reviewed; 267 AA. AC P49434; A3M000; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 111. 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=URA3; ORFNames=PICST_50417; OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL OS Y-11545) (Yeast) (Pichia stipitis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces. OX NCBI_TaxID=322104; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545; RX PubMed=7811063; DOI=10.1128/aem.60.12.4245-4254.1994; RA Yang V.W., Marks J.A., Davis B.P., Jeffries T.W.; RT "High-efficiency transformation of Pichia stipitis based on its URA3 gene RT and a homologous autonomous replication sequence, ARS2."; RL Appl. Environ. Microbiol. 60:4245-4254(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545; RX PubMed=17334359; DOI=10.1038/nbt1290; RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., RA Passoth V., Richardson P.M.; RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting RT yeast Pichia stipitis."; RL Nat. Biotechnol. 25:319-326(2007). 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; U08629; AAA65978.1; -; Genomic_DNA. DR EMBL; CP000502; ABN68626.1; -; Genomic_DNA. DR RefSeq; XP_001386655.1; XM_001386618.1. DR AlphaFoldDB; P49434; -. DR SMR; P49434; -. DR STRING; 322104.P49434; -. DR GeneID; 4840866; -. DR KEGG; pic:PICST_50417; -. DR eggNOG; KOG1377; Eukaryota. DR HOGENOM; CLU_030821_0_0_1; -. DR InParanoid; P49434; -. DR OMA; CLIKTHI; -. DR OrthoDB; 922at2759; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000002258; Chromosome 8. 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; Lyase; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1..267 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134675" FT ACT_SITE 94 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110" FT BINDING 38 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 60..62 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 92..101 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 218 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 236 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 267 AA; 29529 MW; D98361C398F49E06 CRC64; MVNVQTYTQR AESHQSPVAQ RLFKLMDSKK TNLCASVDVK TTSEFLSLID KLGPYICLVK THIDIIDDFS YEGTIVPLLE LSKKHNFMIF EDRKFADIGN TVKSQYSGGV YKIAQWSDIT NAHGVTGSGI VQGLKEAARE TTDEPRGLLM LAELSSKGSI AHGKYTEETV EIAKTDKEFV IGFIAQRDMG GQDEGFDWIV MTPGVGLDDK GDSLGQQYRT VDEVVSTGTD IIIVGRGLFG KGRDPDVEGQ RYREAGWNAY LKKTSQV //