ID A0AAQ4CNG3_9CREN Unreviewed; 219 AA. AC A0AAQ4CNG3; DT 02-OCT-2024, integrated into UniProtKB/TrEMBL. DT 02-OCT-2024, sequence version 1. DT 27-NOV-2024, entry version 2. DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200}; DE EC=4.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01200}; DE AltName: Full=OMP decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200}; DE Short=OMPDCase {ECO:0000256|HAMAP-Rule:MF_01200}; DE Short=OMPdecase {ECO:0000256|HAMAP-Rule:MF_01200}; GN Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01200}; GN ORFNames=SACC_03610 {ECO:0000313|EMBL:BDB97344.1}; OS Saccharolobus caldissimus. OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Saccharolobus. OX NCBI_TaxID=1702097 {ECO:0000313|EMBL:BDB97344.1, ECO:0000313|Proteomes:UP001319921}; RN [1] {ECO:0000313|EMBL:BDB97344.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCM32116 {ECO:0000313|EMBL:BDB97344.1}; RA Sakai H., Kurosawa N.; RL Submitted (OCT-2021) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BDB97344.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCM32116 {ECO:0000313|EMBL:BDB97344.1}; RX DOI=10.1128/mra.01078-21; RA Sakai H.D., Kurosawa N.; RT "Complete Genome Sequence of the Hyperthermophilic and Acidophilic Archaeon RT Saccharolobus caldissimus Strain HS-3T."; RL Microbiol. Resour. Announc. e01078-21:0-0(2022). CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP- CC Rule:MF_01200}. CC -!- CATALYTIC ACTIVITY: CC Reaction=orotidine 5'-phosphate + H(+) = UMP + CO2; 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:0000256|HAMAP-Rule:MF_01200}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861, CC ECO:0000256|HAMAP-Rule:MF_01200}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01200}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily. CC {ECO:0000256|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; AP025226; BDB97344.1; -; Genomic_DNA. DR Proteomes; UP001319921; Chromosome. 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; 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. PE 3: Inferred from homology; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP- KW Rule:MF_01200}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01200}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_01200}. FT DOMAIN 4..202 FT /note="Orotidine 5'-phosphate decarboxylase" FT /evidence="ECO:0000259|SMART:SM00934" FT ACT_SITE 60 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200" FT BINDING 10 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200" FT BINDING 29 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200" FT BINDING 58..67 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200" FT BINDING 114 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200" FT BINDING 163..173 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200" FT BINDING 186 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200" SQ SEQUENCE 219 AA; 24235 MW; 574FBB9D09835216 CRC64; MKNRVILAMD KYIPLEILSE IESEVYGLKI GLPLVLDLGL EKVRNLVKEV NIEEIIVDFK LADIGYVMKS VVEKMLFADS FIAHSFIGVK GSLDELKSYL DEKGKGLYLV ASMSHSGWNN SFLSYIKEVI KEINPKGIVI GATKTDLISS FKREFSSIKI ISPGVGVQGA NYGDAICAGA DFEIIGRSIY TAKDPVNQLK SINKIIEDRV MNCKGRVPK //