PYRE_STRMU
ID PYRE_STRMU Reviewed; 209 AA.
AC Q8DTV2;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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}; OrderedLocusNames=SMU_1221;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58906.1; -; Genomic_DNA.
DR RefSeq; NP_721600.1; NC_004350.2.
DR RefSeq; WP_002263221.1; NC_004350.2.
DR PDB; 3DEZ; X-ray; 2.40 A; A/B=1-209.
DR PDBsum; 3DEZ; -.
DR AlphaFoldDB; Q8DTV2; -.
DR SMR; Q8DTV2; -.
DR STRING; 210007.SMU_1221; -.
DR PRIDE; Q8DTV2; -.
DR EnsemblBacteria; AAN58906; AAN58906; SMU_1221.
DR GeneID; 66817392; -.
DR KEGG; smu:SMU_1221; -.
DR PATRIC; fig|210007.7.peg.1094; -.
DR eggNOG; COG0461; Bacteria.
DR HOGENOM; CLU_074878_1_1_9; -.
DR OMA; ENPFTWA; -.
DR PhylomeDB; Q8DTV2; -.
DR BRENDA; 2.4.2.10; 5941.
DR UniPathway; UPA00070; UER00119.
DR EvolutionaryTrace; Q8DTV2; -.
DR Proteomes; UP000002512; 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_0000110750"
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 1..13
FT /evidence="ECO:0007829|PDB:3DEZ"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3DEZ"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3DEZ"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:3DEZ"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:3DEZ"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3DEZ"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:3DEZ"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:3DEZ"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3DEZ"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3DEZ"
FT STRAND 117..128
FT /evidence="ECO:0007829|PDB:3DEZ"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:3DEZ"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:3DEZ"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:3DEZ"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:3DEZ"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:3DEZ"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:3DEZ"
FT TURN 204..208
FT /evidence="ECO:0007829|PDB:3DEZ"
SQ SEQUENCE 209 AA; 22816 MW; 531D7E3C536531FE CRC64;
MTLAKDIARD LLDIKAVYLK PEEPFTWASG IKSPIYTDNR ITLSYPETRT LIENGFVETI
KEAFPEVEVI AGTATAGIPH GAIIADKMNL PFAYIRSKPK DHGAGNQIEG RVTKGQKMVI
IEDLISTGGS VLDAVAAAQR EGADVLGVVA IFTYELPKAT ANFEKASVKL VTLSNYSELI
KVAKVQGYID ADGLTLLKKF KENQETWQD
