PYRE_STRP1
ID PYRE_STRP1 Reviewed; 209 AA.
AC Q9A076; Q48Z96;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208};
DE Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208};
DE Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208};
DE EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208};
GN Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208};
GN OrderedLocusNames=SPy_0901, M5005_Spy0704;
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 transfer of a ribosyl phosphate group from 5-
CC phosphoribose 1-diphosphate to orotate, leading to the formation of
CC orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01208};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01208};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000255|HAMAP-Rule:MF_01208}.
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DR EMBL; AE004092; AAK33818.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51322.1; -; Genomic_DNA.
DR RefSeq; NP_269097.1; NC_002737.2.
DR PDB; 2AEE; X-ray; 1.95 A; A/B=1-209.
DR PDBsum; 2AEE; -.
DR AlphaFoldDB; Q9A076; -.
DR SMR; Q9A076; -.
DR STRING; 1314.HKU360_00714; -.
DR PaxDb; Q9A076; -.
DR EnsemblBacteria; AAK33818; AAK33818; SPy_0901.
DR KEGG; spy:SPy_0901; -.
DR KEGG; spz:M5005_Spy0704; -.
DR PATRIC; fig|160490.10.peg.774; -.
DR HOGENOM; CLU_074878_1_1_9; -.
DR OMA; ENPFTWA; -.
DR UniPathway; UPA00070; UER00119.
DR EvolutionaryTrace; Q9A076; -.
DR Proteomes; UP000000750; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01208; PyrE; 1.
DR InterPro; IPR023031; OPRT.
DR InterPro; IPR004467; Or_phspho_trans_dom.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00336; pyrE; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Magnesium; Pyrimidine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..209
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110753"
FT BINDING 96
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 100
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 102
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 122..130
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 126
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:2AEE"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:2AEE"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2AEE"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2AEE"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:2AEE"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:2AEE"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2AEE"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:2AEE"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:2AEE"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2AEE"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2AEE"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:2AEE"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:2AEE"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:2AEE"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:2AEE"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:2AEE"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:2AEE"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:2AEE"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:2AEE"
SQ SEQUENCE 209 AA; 22743 MW; 6113019D78A877AC CRC64;
MTLASQIATQ LLDIKAVYLK PEDPFTWASG IKSPIYTDNR VTLSYPKTRD LIENGFVETI
KAHFPEVEVI AGTATAGIPH GAIIADKMTL PFAYIRSKPK DHGAGNQIEG RVLKGQKMVI
IEDLISTGGS VLDAAAAASR EGADVLGVVA IFTYELPKAS QNFKEAGIKL ITLSNYTELI
AVAKLQGYIT NDGLHLLKKF KEDQVNWQQ
