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PYRE_CAEEL
ID   PYRE_CAEEL              Reviewed;         227 AA.
AC   O61790;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Orotate phosphoribosyltransferase {ECO:0000303|PubMed:19645718};
DE            Short=OPRT {ECO:0000303|PubMed:19645718};
DE            Short=OPRTase {ECO:0000303|PubMed:19645718};
DE            EC=2.4.2.10 {ECO:0000269|PubMed:19645718};
DE   AltName: Full=Uracil phosphoribosyltransferase {ECO:0000305|PubMed:19645718};
DE            EC=2.4.2.9 {ECO:0000269|PubMed:19645718};
GN   ORFNames=R12E2.11 {ECO:0000312|WormBase:R12E2.11};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RX   PubMed=19645718; DOI=10.1111/j.1742-4658.2009.07168.x;
RA   Kim S., Park D.H., Kim T.H., Hwang M., Shim J.;
RT   "Functional analysis of pyrimidine biosynthesis enzymes using the
RT   anticancer drug 5-fluorouracil in Caenorhabditis elegans.";
RL   FEBS J. 276:4715-4726(2009).
CC   -!- FUNCTION: Phosphoribosyltransferase which catalyzes the formation of
CC       UMP from uracil in vitro and thus may be involved in UMP biosynthesis
CC       via the salvage pathway. May also participate in the first step of UMP
CC       synthesis by catalyzing the formation of orotidine 5'-phosphate, a UMP
CC       precursor, from orotate. {ECO:0000269|PubMed:19645718}.
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;
CC         Evidence={ECO:0000269|PubMed:19645718};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC         Evidence={ECO:0000269|PubMed:19645718};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 1/2. {ECO:0000269|PubMed:19645718}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uracil: step 1/1. {ECO:0000269|PubMed:19645718}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P08870}.
CC   -!- TISSUE SPECIFICITY: Expressed in body wall muscles, spermatheca and
CC       vulva muscles. {ECO:0000269|PubMed:19645718}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrE subfamily. {ECO:0000305}.
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DR   EMBL; BX284601; CCD65178.1; -; Genomic_DNA.
DR   PIR; T33094; T33094.
DR   RefSeq; NP_491317.1; NM_058916.4.
DR   AlphaFoldDB; O61790; -.
DR   SMR; O61790; -.
DR   IntAct; O61790; 1.
DR   STRING; 6239.R12E2.11; -.
DR   EPD; O61790; -.
DR   PaxDb; O61790; -.
DR   PeptideAtlas; O61790; -.
DR   EnsemblMetazoa; R12E2.11.1; R12E2.11.1; WBGene00020036.
DR   GeneID; 172008; -.
DR   KEGG; cel:CELE_R12E2.11; -.
DR   UCSC; R12E2.11; c. elegans.
DR   CTD; 172008; -.
DR   WormBase; R12E2.11; CE18143; WBGene00020036; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_074878_2_0_1; -.
DR   InParanoid; O61790; -.
DR   OMA; ENPFTWA; -.
DR   OrthoDB; 1303452at2759; -.
DR   PhylomeDB; O61790; -.
DR   UniPathway; UPA00070; UER00119.
DR   UniPathway; UPA00574; UER00636.
DR   PRO; PR:O61790; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00020036; Expressed in larva and 4 other tissues.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:WormBase.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006222; P:UMP biosynthetic process; IDA:WormBase.
DR   GO; GO:0044206; P:UMP salvage; 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   Glycosyltransferase; Pyrimidine biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..227
FT                   /note="Orotate phosphoribosyltransferase"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000439230"
FT   BINDING         51
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:0000250|UniProtKB:P08870"
FT   BINDING         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                   /evidence="ECO:0000250|UniProtKB:P08870"
FT   BINDING         120
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:0000250|UniProtKB:P08870"
FT   BINDING         123
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:0000250|UniProtKB:P08870"
FT   BINDING         149
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000250|UniProtKB:P08870"
FT   BINDING         177
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000250|UniProtKB:P08870"
SQ   SEQUENCE   227 AA;  25192 MW;  164C1B151B207482 CRC64;
     MTAATATANG NHSIEDPVVM KVQAASPIQE TDFFENLYQM ECFRTGEFYL KSGQMTPIYI
     DLRRIMSSPR VLRMAAQAMC EKIVASNLKF DYVVGVPYAA LPLATLVSDI LNVPMLMKRK
     EAKAYGTKQL IEGVYQPGGT VLLVEDVVTS GESIRETAEA IRNENLLVTD AIAVLDRQQG
     ATANLAEDNL NFLSFLTMEK ILDGLITKNE MTEERKHEII AHLAKPF
 
 
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