ID H2J4G1_MARPK Unreviewed; 186 AA.
AC H2J4G1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208};
DE Short=OPRT {ECO:0000256|HAMAP-Rule:MF_01208};
DE Short=OPRTase {ECO:0000256|HAMAP-Rule:MF_01208};
DE EC=2.4.2.10 {ECO:0000256|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208};
GN Name=pyrE {ECO:0000256|HAMAP-Rule:MF_01208};
GN OrderedLocusNames=Marpi_0369 {ECO:0000313|EMBL:AEX84816.1};
OS Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Marinitoga.
OX NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX84816.1, ECO:0000313|Proteomes:UP000007161};
RN [1] {ECO:0000313|EMBL:AEX84816.1, ECO:0000313|Proteomes:UP000007161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14283 / JCM 11233 / KA3
RC {ECO:0000313|Proteomes:UP000007161};
RX PubMed=23045491; DOI=10.1128/JB.01430-12;
RA Lucas S., Han J., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N.C., Ivanova N., Pagani I., Vannier P.,
RA Oger P., Bartlett D.H., Noll K.M., Woyke T., Jebbar M.;
RT "Complete Genome Sequence of the Thermophilic, Piezophilic, Heterotrophic
RT Bacterium Marinitoga piezophila KA3.";
RL J. Bacteriol. 194:5974-5975(2012).
RN [2] {ECO:0000313|Proteomes:UP000007161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14283 / JCM 11233 / KA3
RC {ECO:0000313|Proteomes:UP000007161};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M.,
RA Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.;
RT "Complete sequence of chromosome of Marinitoga piezophila KA3.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01208};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01208};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000256|ARBA:ARBA00004889,
CC ECO:0000256|HAMAP-Rule:MF_01208}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01208}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000256|HAMAP-Rule:MF_01208}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01208}.
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DR EMBL; CP003257; AEX84816.1; -; Genomic_DNA.
DR RefSeq; WP_014295888.1; NC_016751.1.
DR AlphaFoldDB; H2J4G1; -.
DR STRING; 443254.Marpi_0369; -.
DR KEGG; mpz:Marpi_0369; -.
DR eggNOG; COG0461; Bacteria.
DR HOGENOM; CLU_074878_3_0_0; -.
DR OrthoDB; 9783570at2; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000007161; 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 GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
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; IPR006273; Orotate_PRibTrfase_bac.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR NCBIfam; TIGR01367; pyrE_Therm; 1.
DR PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW ECO:0000313|EMBL:AEX84816.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01208}; Reference proteome {ECO:0000313|Proteomes:UP000007161};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:AEX84816.1}.
FT DOMAIN 44..160
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT BINDING 87
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:0000256|HAMAP-Rule:MF_01208"
FT BINDING 111..119
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:0000256|HAMAP-Rule:MF_01208"
FT BINDING 115
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT BINDING 143
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ SEQUENCE 186 AA; 20876 MW; C3667C52C9DA10D4 CRC64;
MEIMEILKKT NAILNGHFLL SSGLHSDTYI QCAQALKYPE YAEMLGKALS EKFNEKPDYV
VSPALGGLII GYEVARGLKT PFLFTERNKE GVMELRRNFF IEENAKVIII EDVITTGKST
LEVVKALEKY KPQIIGIGCI VNRSKKKDLN NIKIQSLVEI DAKTYEPDNC PLCKENIPAV
KPGSRK
//
