PYRF_STRP1
ID PYRF_STRP1 Reviewed; 230 AA.
AC Q9A077; Q48Z97;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
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};
GN OrderedLocusNames=SPy_0900, M5005_Spy0703;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK33817.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51321.1; -; Genomic_DNA.
DR RefSeq; NP_269096.1; NC_002737.2.
DR AlphaFoldDB; Q9A077; -.
DR SMR; Q9A077; -.
DR STRING; 1314.HKU360_00713; -.
DR PaxDb; Q9A077; -.
DR EnsemblBacteria; AAK33817; AAK33817; SPy_0900.
DR KEGG; spy:SPy_0900; -.
DR KEGG; spz:M5005_Spy0703; -.
DR PATRIC; fig|160490.10.peg.773; -.
DR HOGENOM; CLU_067069_1_1_9; -.
DR OMA; NFKIFLD; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000000750; 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_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; Reference proteome.
FT CHAIN 1..230
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134589"
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"
FT CONFLICT 42
FT /note="A -> V (in Ref. 2; AAZ51321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 24976 MW; 8E2820164986B547 CRC64;
MKEERPIIAL DFSSFEETKA FLDLFPAEEK LYVKIGMELY YAQGPDIVRY IKSLGHNVFL
DLKLHDIPNT VRAAMAVLKE LDIDMATVHA AGGVEMLKAA REGLGQGPTL IAVTQLTSTS
EDQMRGDQNI QTSLLESVLH YSKGAAKAQL DGAVCSAQEV EAIKAVTPTG FTCLTPGIRP
KGSNIGDQKR VMTPNQARRI GSDYIVVGRP ITQAKDPVAA YQAIKAEWAG
