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    URA4 dihydroorotase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851139, updated on 9-Dec-2024

    Summary

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    Official Symbol
    URA4
    Official Full Name
    dihydroorotase
    Primary source
    SGD:S000004412
    Locus tag
    YLR420W
    See related
    AllianceGenome:SGD:S000004412; FungiDB:YLR420W; VEuPathDB:YLR420W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables dihydroorotase activity. Involved in 'de novo' pyrimidine nucleobase biosynthetic process and pyrimidine nucleotide biosynthetic process. Located in cytoplasm and nucleus. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See URA4 in Genome Data Viewer
    Location:
    chromosome: XII
    Exon count:
    1
    Sequence:
    Chromosome: XII; NC_001144.5 (963785..964879)

    Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene putative helicase Neighboring gene tRNA-Leu Neighboring gene proteasome regulatory particle lid subunit RPN13 Neighboring gene Dck1p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001144.5

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Structure of the Saccharomyces cerevisiae URA4 gene encoding dihydroorotase. Guyonvarch A, et al. Mol Gen Genet, 1988 Apr. PMID 2897615
    2. Cloning of the PYR3 gene of Ustilago maydis and its use in DNA transformation. Banks GR, et al. Mol Cell Biol, 1988 Dec. PMID 2907604, Free PMC Article
    3. Complexed Crystal Structure of Saccharomyces cerevisiae Dihydroorotase with Inhibitor 5-Fluoroorotate Reveals a New Binding Mode. Guan HH, et al. Bioinorg Chem Appl, 2021. PMID 34630544, Free PMC Article
    4. Creation of a putative third metal binding site in type II dihydroorotases significantly enhances enzyme activity. Huang YH, et al. Protein Pept Lett, 2015. PMID 26446564
    5. Centromere silencing and function in fission yeast is governed by the amino terminus of histone H3. Mellone BG, et al. Curr Biol, 2003 Oct 14. PMID 14561399

    See all (38) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables dihydroorotase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables dihydroorotase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dihydroorotase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in 'de novo' UMP biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in 'de novo' pyrimidine nucleobase biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in 'de novo' pyrimidine nucleobase biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in pyrimidine nucleobase biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in pyrimidine nucleotide biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in pyrimidine nucleotide biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in pyrimidine nucleotide biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus HDA PubMed 

    General protein information

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    Preferred Names
    dihydroorotase
    NP_013524.1
    • Dihydroorotase; catalyzes the third enzymatic step in the de novo biosynthesis of pyrimidines, converting carbamoyl-L-aspartate into dihydroorotate

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001144.5 Reference assembly

      Range
      963785..964879
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182308.1 → NP_013524.1  TPA: dihydroorotase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013524.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VZ56, P20051
      UniProtKB/TrEMBL
      A7A1U1, G2WJN2
      Conserved Domains (1) summary
      TIGR00856
      Location:4 → 360
      pyrC_dimer; dihydroorotase, homodimeric type
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P20051.2

    Gene LinkOut

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