ID PYRF_METJA Reviewed; 213 AA. AC Q57700; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 122. 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}; OrderedLocusNames=MJ0252; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). 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 -!- SEQUENCE CAUTION: CC Sequence=AAB98239.1; Type=Erroneous initiation; Evidence={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; L77117; AAB98239.1; ALT_INIT; Genomic_DNA. DR PIR; E64331; E64331. DR RefSeq; WP_064496436.1; NC_000909.1. DR PDB; 4LUI; X-ray; 1.60 A; A/B=1-213. DR PDB; 4LUJ; X-ray; 1.60 A; A/B=1-213. DR PDBsum; 4LUI; -. DR PDBsum; 4LUJ; -. DR AlphaFoldDB; Q57700; -. DR SMR; Q57700; -. DR STRING; 243232.MJ_0252; -. DR PaxDb; 243232-MJ_0252; -. DR EnsemblBacteria; AAB98239; AAB98239; MJ_0252. DR GeneID; 1451106; -. DR KEGG; mja:MJ_0252; -. DR eggNOG; arCOG00081; Archaea. DR HOGENOM; CLU_067069_2_0_2; -. DR InParanoid; Q57700; -. DR OrthoDB; 94124at2157; -. DR PhylomeDB; Q57700; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000805; Chromosome. 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; IEA:UniProtKB-UniPathway. DR CDD; cd04725; OMP_decarboxylase_like; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01200_A; OMPdecase_type1_A; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014732; OMPdecase. DR InterPro; IPR047595; OMPdecase_arc. DR InterPro; IPR018089; OMPdecase_AS. 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..213 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134610" FT ACT_SITE 61 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 9 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 31 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 59..68 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 115 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 166..176 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 192 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT STRAND 3..7 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 13..23 FT /evidence="ECO:0007829|PDB:4LUI" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:4LUI" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 34..38 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 43..52 FT /evidence="ECO:0007829|PDB:4LUI" FT STRAND 54..62 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 66..76 FT /evidence="ECO:0007829|PDB:4LUI" FT TURN 77..79 FT /evidence="ECO:0007829|PDB:4LUI" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 91..103 FT /evidence="ECO:0007829|PDB:4LUI" FT STRAND 107..111 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 117..120 FT /evidence="ECO:0007829|PDB:4LUI" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 127..137 FT /evidence="ECO:0007829|PDB:4LUI" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 149..159 FT /evidence="ECO:0007829|PDB:4LUI" FT STRAND 163..166 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:4LUJ" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:4LUI" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 192..195 FT /evidence="ECO:0007829|PDB:4LUI" FT HELIX 200..209 FT /evidence="ECO:0007829|PDB:4LUI" SQ SEQUENCE 213 AA; 23592 MW; 0B073BE37D50C556 CRC64; MPKLMLALDV LDRDRALKIV EDVKDYVDAI KVGYPLVLST GTEIIKEIKK LCNKEVIADF KVADIPATNE KIAKITLKYA DGIIVHGFVG EDSVKAVQDV AKKLNKKVIM VTEMSHPGAV QFLQPIADKL SEMAKKLKVD AIVAPSTRPE RLKEIKEIAE LPVITPGVGA QGGKIEDILN ILDENDYVIV GRAIYQSQNP KEEAKKYKEM LNK //