PYRF_STRP4
ID PYRF_STRP4 Reviewed; 233 AA.
AC B5E301; Q9ZHA7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200};
DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200};
GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; OrderedLocusNames=SPG_0631;
OS Streptococcus pneumoniae serotype 19F (strain G54).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=512566;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9846742; DOI=10.1099/00221287-144-11-3069;
RA Massidda O., Anderluzzi D., Friedli L., Feger G.;
RT "Unconventional organization of the division and cell wall gene cluster of
RT Streptococcus pneumoniae.";
RL Microbiology 144:3069-3078(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RX PubMed=11442348; DOI=10.1089/10766290152044995;
RA Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT clinical isolate.";
RL Microb. Drug Resist. 7:99-125(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RA Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA Tettelin H., Oggioni M.;
RT "Pneumococcal beta glucoside metabolism investigated by whole genome
RT comparison.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01200};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01200}.
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DR EMBL; AF068902; AAC95452.1; -; Genomic_DNA.
DR EMBL; CP001015; ACF56433.1; -; Genomic_DNA.
DR RefSeq; WP_001206717.1; NC_011072.1.
DR AlphaFoldDB; B5E301; -.
DR SMR; B5E301; -.
DR KEGG; spx:SPG_0631; -.
DR HOGENOM; CLU_067069_1_1_9; -.
DR OMA; NFKIFLD; -.
DR UniPathway; UPA00070; UER00120.
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_01200_B; OMPdecase_type1_B; 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 PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1..233
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000138562"
FT ACT_SITE 63
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 61..70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
SQ SEQUENCE 233 AA; 25409 MW; A23B2543FD2E7EA8 CRC64;
MREHRPIIAL DFPSFEAVKE FLALFPAEES LYLKVGMELY YAAGPEIVSY LKGLGHSVFL
DLKLHDIPNT VKSAMKVLSQ LGVDMTNVHA AGGVEMMKAA REGLGSQAKL IAVTQLTSTS
EAQMQEFQNI QTSLQESVIH YAKKTAEAGL DGVVCSAQEV QVIKQATNPD FICLTPGIRP
AGVAVGDQKR VMTPADAYQI GSDYIVVGRP ITQAEDPVAA YHAIKDEWTQ DWN
