PYRF_STRPN
ID PYRF_STRPN Reviewed; 233 AA.
AC P0CB75; Q9ZHA7;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=SP_0701;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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 -!- INTERACTION:
CC P0CB75; P63588: aroD; NbExp=2; IntAct=EBI-2207109, EBI-2207290;
CC P0CB75; Q97SE6: gatA; NbExp=2; IntAct=EBI-2207109, EBI-2207039;
CC P0CB75; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207109, EBI-2207053;
CC P0CB75; Q97NV3: groES; NbExp=2; IntAct=EBI-2207109, EBI-2206949;
CC P0CB75; P65887: purA; NbExp=2; IntAct=EBI-2207109, EBI-2206955;
CC P0CB75; P0CB75: pyrF; NbExp=2; IntAct=EBI-2207109, EBI-2207109;
CC P0CB75; Q97NX5: scpA; NbExp=3; IntAct=EBI-2207109, EBI-2207368;
CC P0CB75; Q97SR4: uppS; NbExp=2; IntAct=EBI-2207109, EBI-2206983;
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01200}.
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DR EMBL; AE005672; AAK74844.1; -; Genomic_DNA.
DR PIR; C95081; C95081.
DR RefSeq; WP_001206711.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0CB75; -.
DR SMR; P0CB75; -.
DR IntAct; P0CB75; 7.
DR STRING; 170187.SP_0701; -.
DR EnsemblBacteria; AAK74844; AAK74844; SP_0701.
DR KEGG; spn:SP_0701; -.
DR eggNOG; COG0284; Bacteria.
DR OMA; NFKIFLD; -.
DR PhylomeDB; P0CB75; -.
DR BioCyc; SPNE170187:G1FZB-719-MON; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1..233
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134587"
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; 25423 MW; 29AB36FBCBF7B4C9 CRC64;
MREHRPIIAL DFPSFEAVKE FLALFPAEES LYLKVGMELY YAAGPEIVSY LKGLGHSVFL
DLKLHDIPNT VKSAMKILSQ LGVDMTNVHA AGGVEMMKAA REGLGSQAKL IAVTQLTSTS
EAQMQEFQNI QTSLQESVIH YAKKTAEAGL DGVVCSAQEV QVIKQATNPD FICLTPGIRP
AGVAVGDQKR VMTPADAYQI GSDYIVVGRP ITQAEDPVAA YHAIKDEWTQ DWN
