PYRE_HAEI8
ID PYRE_HAEI8 Reviewed; 213 AA.
AC Q4QNR7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=NTHI0380;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(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; CP000057; AAX87330.1; -; Genomic_DNA.
DR RefSeq; WP_005644452.1; NC_007146.2.
DR AlphaFoldDB; Q4QNR7; -.
DR SMR; Q4QNR7; -.
DR EnsemblBacteria; AAX87330; AAX87330; NTHI0380.
DR GeneID; 56956845; -.
DR KEGG; hit:NTHI0380; -.
DR HOGENOM; CLU_074878_0_1_6; -.
DR OMA; MKAYQRQ; -.
DR OrthoDB; 1280396at2; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000002525; 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 3: Inferred from homology;
KW Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; Transferase.
FT CHAIN 1..213
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_1000066233"
FT BINDING 26
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 34..35
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 72..73
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 99
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 /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 103
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 105
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 124..132
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 128
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 156
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
SQ SEQUENCE 213 AA; 23643 MW; B93E460CD485A19E CRC64;
MEQYKRDFIE FALSRNVLKF GEFTLKSGRK SPYFFNAGLF NTGADLARLG EFYAAAIQAS
AVDFDVVFGP AYKGIPIGTS VSVALFNRYG IDKPVCFNRK EVKDHGEGGN LIGSPLQGKI
LLVDDVITAG TAIRESMELI SANKAELAAV LIALNRKERG KGELSAIQEV ERDYQCQVLS
IIDLDDLMQF IEQDPRYSSH LPEMRAYRAE FGV
