ID A0A0G1P4C7_9BACT Unreviewed; 231 AA.
AC A0A0G1P4C7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|RuleBase:RU000512};
DE EC=4.1.1.23 {ECO:0000256|RuleBase:RU000512};
GN ORFNames=UW91_C0035G0006 {ECO:0000313|EMBL:KKT91264.1};
OS Parcubacteria group bacterium GW2011_GWF2_45_11.
OC Bacteria.
OX NCBI_TaxID=1618973 {ECO:0000313|EMBL:KKT91264.1, ECO:0000313|Proteomes:UP000034898};
RN [1] {ECO:0000313|EMBL:KKT91264.1, ECO:0000313|Proteomes:UP000034898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP).
CC {ECO:0000256|ARBA:ARBA00002356}.
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|ARBA:ARBA00001419,
CC ECO:0000256|RuleBase:RU000512};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861,
CC ECO:0000256|RuleBase:RU000512}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family.
CC {ECO:0000256|RuleBase:RU000512}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKT91264.1}.
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; LCKE01000035; KKT91264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1P4C7; -.
DR PATRIC; fig|1618973.3.peg.856; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000034898; Unassembled WGS sequence.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
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 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; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 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 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW ECO:0000256|RuleBase:RU000512};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000512};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975,
KW ECO:0000256|RuleBase:RU000512}.
FT DOMAIN 7..219
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
SQ SEQUENCE 231 AA; 25852 MW; C71743389351254A CRC64;
MEQKQTNLCL AADLADWNKL TELVKKVGHK ICVLKTHLDI INNLPADFID QLIKLKNLYD
FLIFEDRKFA DIGHTVQRQY AGGFYKIADW ADIINCHILP GPGIIEGLRE IGLPKGQGLL
LLAQMSSAGN LLTDDYAHQA VELAKKYDDF VIGFIGMRKM IDDDKFINLT PGIQLTEGGD
NLGQQYNTPE NVIKNGSDII IVGRGIYEAG DPLTEAEKYR TAAWQAYQNI Q
//