PYRF_GRAFK
ID PYRF_GRAFK Reviewed; 272 AA.
AC A0LYL6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215};
DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01215};
DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215};
DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01215};
DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01215};
GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01215}; OrderedLocusNames=GFO_0478;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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_01215};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01215}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01215}.
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DR EMBL; CU207366; CAL65461.1; -; Genomic_DNA.
DR RefSeq; WP_011708399.1; NC_008571.1.
DR AlphaFoldDB; A0LYL6; -.
DR SMR; A0LYL6; -.
DR STRING; 411154.GFO_0478; -.
DR EnsemblBacteria; CAL65461; CAL65461; GFO_0478.
DR KEGG; gfo:GFO_0478; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_060704_1_0_10; -.
DR OMA; QSAFFER; -.
DR OrthoDB; 1181405at2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000000755; Chromosome.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule.
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 Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01215; OMPdecase_type2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011995; OMPdecase_type-2.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR43375; PTHR43375; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR02127; pyrF_sub2; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1..272
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000138952"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ SEQUENCE 272 AA; 30364 MW; 8525FE5005148EEF CRC64;
MTSQELTEQI LKKQSFLCVG LDTDLDKIPT YLLSEKDPVF SFNKAIIDAT HQYCVAYKPN
IAFYEAIGVD GWKALKKTIE YLHAEYPDLY TIADAKRGDI GNTSRMYAKA FFEDLGFDSI
TVAPYMGKDS VEPFLEFTNK HTILLALTSN EGAFDFQTLK TGDKELYKKV IETSKNWQNS
ENLMYVVGAT KAEYLAEIRK IIPENFLLVP GVGAQGGSLE EVCKYGMTKN VGLLINSSRK
IIYASDSSNF AEIAGAKAEA MQNQMASELE KL