ID A0A550D551_9CREN Unreviewed; 209 AA. AC A0A550D551; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, 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=DJ522_01155 {ECO:0000313|EMBL:TRM85329.1}; OS Sulfolobus sp. F3. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus; unclassified Sulfolobus. OX NCBI_TaxID=2200886 {ECO:0000313|EMBL:TRM85329.1}; RN [1] {ECO:0000313|EMBL:TRM85329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F3 {ECO:0000313|EMBL:TRM85329.1}; RA Yun J., Xu P., Xu J., Dai X., Wang Y., Zheng X.Z., Cao C., Yi Q.Y., RA Zhu Y., Wang L., Dong Z., Huang Y., Huang L., Du W.; RT "Cross-interface Injection: A General Nanoliter Liquid Handling Method RT Applied to Single Cells Genome Amplification Automated Nanoliter RT Liquid Handling Applied to Single Cell Multiple Displacement RT Amplification."; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'- CC monophosphate (OMP) to uridine 5'-monophosphate (UMP). CC {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01200}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 2/2. {ECO:0000256|HAMAP- CC Rule:MF_01200}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01200}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01200}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:TRM85329.1}. 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; QFWC01000012; TRM85329.1; -; Genomic_DNA. DR UniPathway; UPA00070; UER00120. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01200_A; OMPdecase_type1_A; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014732; OMPdecase. DR InterPro; IPR001754; OMPdeCOase_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1. DR Pfam; PF00215; OMPdecase; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; SSF51366; 1. PE 3: Inferred from homology; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01200}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01200}. FT DOMAIN 1 198 OMPdecase. {ECO:0000259|SMART:SM00934}. FT REGION 54 63 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01200}. FT REGION 159 169 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01200}. FT ACT_SITE 56 56 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_01200}. FT BINDING 6 6 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01200}. FT BINDING 25 25 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01200}. FT BINDING 110 110 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01200}. FT BINDING 182 182 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01200}. FT BINDING 183 183 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01200}. SQ SEQUENCE 209 AA; 23544 MW; 2BD662BC5DFCB5A5 CRC64; MILALDKHIP REVLLEISNE IHGIKIGLPF VLDVGLIKLK EILNDIKLEE IIIDFKLADI GFVMKQIVER LSFADAFIAH SFVGIEGALD ELKTFLDSQR KNLYLVAAMS HRGWNNEFNN YIKQIIQKIE PKGIVVGATR LDTIREFRFM FPKITIISPG VGTQGANYGD AICAGGDYEI VGRSVYNSPD PINEIRKINE IIRNKVMSC //