ID PYRF_CAMJE Reviewed; 279 AA. AC Q9PIC1; Q0PBC9; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200}; DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200}; GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; GN OrderedLocusNames=Cj0381c; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP- CC Rule:MF_01200}. 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|HAMAP-Rule:MF_01200}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01200}. 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; AL111168; CAL34531.1; -; Genomic_DNA. DR PIR; C81381; C81381. DR RefSeq; WP_002858700.1; NZ_SZUC01000004.1. DR RefSeq; YP_002343818.1; NC_002163.1. DR PDB; 3RU6; X-ray; 1.80 A; A/B/C/D=1-279. DR PDBsum; 3RU6; -. DR AlphaFoldDB; Q9PIC1; -. DR SMR; Q9PIC1; -. DR IntAct; Q9PIC1; 23. DR STRING; 192222.Cj0381c; -. DR PaxDb; 192222-Cj0381c; -. DR EnsemblBacteria; CAL34531; CAL34531; Cj0381c. DR GeneID; 904704; -. DR KEGG; cje:Cj0381c; -. DR PATRIC; fig|192222.6.peg.372; -. DR eggNOG; COG0284; Bacteria. DR HOGENOM; CLU_067069_1_1_7; -. DR OrthoDB; 9806203at2; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000799; Chromosome. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule. 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 HAMAP; MF_01200_B; OMPdecase_type1_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014732; OMPdecase. DR InterPro; IPR018089; OMPdecase_AS. DR InterPro; IPR047596; OMPdecase_bac. DR InterPro; IPR001754; OMPdeCOase_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; TIGR01740; pyrF; 1. 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 1: Evidence at protein level; KW 3D-structure; Decarboxylase; Lyase; Pyrimidine biosynthesis; KW Reference proteome. FT CHAIN 1..279 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134535" FT ACT_SITE 60 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 8 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 30 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 58..67 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 186 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 206 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 207 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 12..21 FT /evidence="ECO:0007829|PDB:3RU6" FT TURN 22..24 FT /evidence="ECO:0007829|PDB:3RU6" FT STRAND 28..31 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 33..39 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 41..50 FT /evidence="ECO:0007829|PDB:3RU6" FT STRAND 54..61 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 65..76 FT /evidence="ECO:0007829|PDB:3RU6" FT TURN 77..79 FT /evidence="ECO:0007829|PDB:3RU6" FT STRAND 81..86 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 91..101 FT /evidence="ECO:0007829|PDB:3RU6" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:3RU6" FT STRAND 109..113 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 121..128 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 132..145 FT /evidence="ECO:0007829|PDB:3RU6" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:3RU6" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 158..164 FT /evidence="ECO:0007829|PDB:3RU6" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 192..197 FT /evidence="ECO:0007829|PDB:3RU6" FT STRAND 201..205 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 207..210 FT /evidence="ECO:0007829|PDB:3RU6" FT HELIX 215..226 FT /evidence="ECO:0007829|PDB:3RU6" SQ SEQUENCE 279 AA; 32331 MW; C395A4569A7338A8 CRC64; MKLCVALDLS TKEECLQLAK ELKNLDIWLK VGLRAYLRDG FKFIEELKKV DDFKIFLDLK FHDIPNTMAD ACEEVSKLGV DMINIHASAG KIAIQEVMTR LSKFSKRPLV LAVSALTSFD EENFFSIYRQ KIEEAVINFS KISYENGLDG MVCSVFESKK IKEHTSSNFL TLTPGIRPFG ETNDDQKRVA NLAMARENLS DYIVVGRPIY KNENPRAVCE KILNKIHRKN ISENDIEQNY EVIQQKEWDM CNHFEEWIKT RPDKEHALKE FYAKCGIKY //