ID PYRF_THEMA Reviewed; 201 AA. AC Q9WYG7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 142. DE RecName: Full=Orotidine 5'-phosphate decarboxylase; DE EC=4.1.1.23; DE AltName: Full=OMP decarboxylase; DE Short=OMPDCase; DE Short=OMPdecase; GN Name=pyrF; OrderedLocusNames=TM_0332; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT. RG Joint center for structural genomics (JCSG); RT "Crystal Structure of orotidine 5'-phosphate decarboxylase (TM0332) from RT Thermotoga maritima at 2.00 A resolution."; RL Submitted (JAN-2005) to the PDB data bank. CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000250}. 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 -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily. CC {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; AE000512; AAD35419.1; -; Genomic_DNA. DR PIR; F72390; F72390. DR RefSeq; NP_228143.1; NC_000853.1. DR RefSeq; WP_004083099.1; NZ_CP011107.1. DR PDB; 1VQT; X-ray; 2.00 A; A=1-201. DR PDBsum; 1VQT; -. DR AlphaFoldDB; Q9WYG7; -. DR SMR; Q9WYG7; -. DR STRING; 243274.TM_0332; -. DR PaxDb; 243274-THEMA_03060; -. DR EnsemblBacteria; AAD35419; AAD35419; TM_0332. DR KEGG; tma:TM0332; -. DR eggNOG; COG0284; Bacteria. DR InParanoid; Q9WYG7; -. DR OrthoDB; 9806203at2; -. DR UniPathway; UPA00070; UER00120. DR EvolutionaryTrace; Q9WYG7; -. DR Proteomes; UP000008183; 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 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; 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..201 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134595" FT ACT_SITE 54 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110" FT BINDING 8 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 26 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 52..61 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 106 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 153 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 161 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 181 FT /ligand="substrate" FT /evidence="ECO:0000250" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:1VQT" FT STRAND 9..11 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 12..19 FT /evidence="ECO:0007829|PDB:1VQT" FT STRAND 23..27 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 29..32 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 37..43 FT /evidence="ECO:0007829|PDB:1VQT" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:1VQT" FT STRAND 48..55 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 59..69 FT /evidence="ECO:0007829|PDB:1VQT" FT STRAND 74..80 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 85..94 FT /evidence="ECO:0007829|PDB:1VQT" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 112..124 FT /evidence="ECO:0007829|PDB:1VQT" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 133..139 FT /evidence="ECO:0007829|PDB:1VQT" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:1VQT" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:1VQT" FT TURN 171..173 FT /evidence="ECO:0007829|PDB:1VQT" FT STRAND 175..180 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 181..184 FT /evidence="ECO:0007829|PDB:1VQT" FT HELIX 189..196 FT /evidence="ECO:0007829|PDB:1VQT" SQ SEQUENCE 201 AA; 22809 MW; 4C2FAD77302F206D CRC64; MTPVLSLDME DPIRFIDENG SFEVVKVGHN LAIHGKKIFD ELAKRNLKII LDLKFCDIPS TVERSIKSWD HPAIIGFTVH SCAGYESVER ALSATDKHVF VVVKLTSMEG SLEDYMDRIE KLNKLGCDFV LPGPWAKALR EKIKGKILVP GIRMEVKADD QKDVVTLEEM KGIANFAVLG REIYLSENPR EKIKRIKEMR L //