GenomeNet

Database: UniProt
Entry: K9VF66_9CYAN
LinkDB: K9VF66_9CYAN
Original site: K9VF66_9CYAN 
ID   K9VF66_9CYAN            Unreviewed;       492 AA.
AC   K9VF66;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Orotate phosphoribosyltransferase {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|HAMAP-Rule:MF_01208};
GN   Name=pyrE {ECO:0000256|HAMAP-Rule:MF_01208};
GN   ORFNames=Osc7112_1655 {ECO:0000313|EMBL:AFZ06154.1};
OS   Oscillatoria nigro-viridis PCC 7112.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX   NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ06154.1, ECO:0000313|Proteomes:UP000010478};
RN   [1] {ECO:0000313|EMBL:AFZ06154.1, ECO:0000313|Proteomes:UP000010478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ06154.1,
RC   ECO:0000313|Proteomes:UP000010478};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL   Submitted (MAY-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=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC         Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001419};
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003614; AFZ06154.1; -; Genomic_DNA.
DR   RefSeq; WP_015175472.1; NC_019729.1.
DR   AlphaFoldDB; K9VF66; -.
DR   STRING; 179408.Osc7112_1655; -.
DR   KEGG; oni:Osc7112_1655; -.
DR   PATRIC; fig|179408.3.peg.2010; -.
DR   eggNOG; COG0284; Bacteria.
DR   eggNOG; COG0461; Bacteria.
DR   HOGENOM; CLU_027768_0_0_3; -.
DR   OrthoDB; 9802134at2; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000010478; 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:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04725; OMP_decarboxylase_like; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01208; PyrE; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011995; OMPdecase_type-2.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00336; pyrE; 1.
DR   NCBIfam; TIGR02127; pyrF_sub2; 1.
DR   PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000313|EMBL:AFZ06154.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AFZ06154.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01208}; Reference proteome {ECO:0000313|Proteomes:UP000010478};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:AFZ06154.1}.
FT   DOMAIN          22..167
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|Pfam:PF00215"
FT   DOMAIN          339..453
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   BINDING         388
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         389
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         392
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         414..422
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"
SQ   SEQUENCE   492 AA;  54510 MW;  118F0D9D284B11BB CRC64;
     MSDRTNFFDK LLAAVENNQS LLYLALDPDP ETWPPQVSMT GEETQTFVTD LLSKLKSAID
     QTADLICACK ITLGFYQSLG IPGWALLQEI LTIIPPHLPV ILDAKHCDLN TSTVFAKIVF
     QDWRVDAITL SPYAGFDQVA PFLLYAGKTV FVLCATANPS AEAVQEYPTP ENPLYLQLVR
     LSQLWGTPEK LGLEVGVMPD MLARIRKEAP ERLILVEGDI AEENDLTEEN DLAQLLAAGL
     SKNGEDLLLP VPPSLLAGKE PRREIEKLRD SINKQRLRAI EGSPTCELWL PDVCFLQPEP
     HRDLILQLYD IGCVVFGDHV QASGAVFPYY IDLRKIISIP QIFHQIVSAY ADILKELKFD
     RIAGIPYGSL PTATGLALRM ERPMIFPRKE VKTYGAGKLI EGHFQAGETI VVVDDILISG
     KSVMEGAAKL KSAGLNVEDI VVLIDHEQGV KDKMQANGYR AHSVLALSEI AEVLYQANRI
     DTEQFNLLTA EH
//
DBGET integrated database retrieval system