PYRE_AERPE
ID PYRE_AERPE Reviewed; 186 AA.
AC Q9Y9D8;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
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=APE_2349.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA81362.2; -; Genomic_DNA.
DR PIR; B72463; B72463.
DR PDB; 2YZK; X-ray; 1.80 A; A/B/C/D=10-186.
DR PDBsum; 2YZK; -.
DR AlphaFoldDB; Q9Y9D8; -.
DR SMR; Q9Y9D8; -.
DR STRING; 272557.APE_2349.1; -.
DR EnsemblBacteria; BAA81362; BAA81362; APE_2349.1.
DR KEGG; ape:APE_2349.1; -.
DR eggNOG; arCOG00029; Archaea.
DR UniPathway; UPA00070; UER00119.
DR EvolutionaryTrace; Q9Y9D8; -.
DR Proteomes; UP000002518; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Magnesium; Pyrimidine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..186
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110776"
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 121..129
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 125
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 153
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:2YZK"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:2YZK"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2YZK"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:2YZK"
FT HELIX 46..66
FT /evidence="ECO:0007829|PDB:2YZK"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2YZK"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:2YZK"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:2YZK"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2YZK"
FT STRAND 114..127
FT /evidence="ECO:0007829|PDB:2YZK"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:2YZK"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:2YZK"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:2YZK"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2YZK"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:2YZK"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:2YZK"
SQ SEQUENCE 186 AA; 19638 MW; A05A8636B3A22B91 CRC64;
MSHEELAEVL AKVLKKRGAV LRGDFVLSSG RRSSVYIDMR RLLGDESSYS VALDLLLEVG
GQDLARSSAV IGVATGGLPW AAMLALRLSK PLGYVRPERK GHGTLSQVEG DPPKGRVVVV
DDVATTGTSI AKSIEVLRSN GYTVGTALVL VDRGEGAGEL LARMGVRLVS VATLKTILEK
LGWGGE
