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    OPLAH 5-oxoprolinase, ATP-hydrolysing [ Bos taurus (domestic cattle) ]

    Gene ID: 408006, updated on 10-Oct-2024

    Summary

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    Official Symbol
    OPLAHprovided by VGNC
    Official Full Name
    5-oxoprolinase, ATP-hydrolysingprovided by VGNC
    Primary source
    VGNC:VGNC:53869
    See related
    BGD:BT11542; Ensembl:ENSBTAG00000017281
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Bos taurus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
    Also known as
    5-OPase
    Orthologs
    human mouse all
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    Genomic context

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    See OPLAH in Genome Data Viewer
    Location:
    chromosome: 14
    Exon count:
    29
    Annotation release Status Assembly Chr Location
    RS_2023_09 current ARS-UCD2.0 (GCF_002263795.3) 14 NC_037341.1 (763523..774582)

    Chromosome 14 - NC_037341.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC107133095 Neighboring gene glycosylphosphatidylinositol anchor attachment 1 Neighboring gene exosome component 4 Neighboring gene sphingomyelin phosphodiesterase 5 Neighboring gene spermatogenesis and centriole associated 1 Neighboring gene transfer RNA glycine (anticodon UCC) Neighboring gene uncharacterized LOC112449562

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_037341.1 Chromosome 14 Reference ARS-UCD2.0 Primary Assembly

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Bovine 5-oxo-L-prolinase: simple assay method, purification, cDNA cloning, and detection of mRNA in the coronary artery. Watanabe T, et al. Biol Pharm Bull, 2004 Mar. PMID 14993790
    2. A whole-genome assembly of the domestic cow, Bos taurus. Zimin AV, et al. Genome Biol, 2009. PMID 19393038, Free PMC Article
    3. TreeGrafter: phylogenetic tree-based annotation of proteins with Gene Ontology terms and other annotations. Tang H, et al. Bioinformatics, 2019 Feb 1. PMID 30032202, Free PMC Article

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. amino acid sequence determined
      Title: Bovine 5-oxo-L-prolinase: simple assay method, purification, cDNA cloning, and detection of mRNA in the coronary artery.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    General gene information

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    Homology

    Gene Ontology Provided by RefSeq

    Function Evidence Code Pubs
    enables 5-oxoprolinase (ATP-hydrolyzing) activity IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in glutathione metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytosol IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    5-oxoprolinase
    Names
    5-oxo-L-prolinase
    pyroglutamase
    NP_001001173.2
    XP_010810124.1
    XP_015329816.1
    XP_024857210.1
    XP_059749122.1
    XP_059749123.1
    XP_059749124.1
    XP_059749125.1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001001173.2 → NP_001001173.2  5-oxoprolinase

      Status: VALIDATED

      Source sequence(s)
      AW461711, EV743436, NKLS02000014
      UniProtKB/Swiss-Prot
      F1ME97, Q75WB5
      UniProtKB/TrEMBL
      A0A3Q1LQE0
      Related
      ENSBTAP00000022981.6, ENSBTAT00000022981.6
      Conserved Domains (1) summary
      cl19816
      Location:1 → 1258
      Hydantoinase_B; Hydantoinase B/oxoprolinase

    RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2023_09

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

    Reference ARS-UCD2.0 Primary Assembly

    Genomic

    1. NC_037341.1 Reference ARS-UCD2.0 Primary Assembly

      Range
      763523..774582
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_025001442.2 → XP_024857210.1  5-oxoprolinase isoform X1

      UniProtKB/TrEMBL
      A0A3Q1LQE0
      Conserved Domains (2) summary
      pfam15058
      Location:1 → 138
      Speriolin_N; Speriolin N terminus
      cl19816
      Location:96 → 1354
      Hydantoinase_B; Hydantoinase B/oxoprolinase

    2. XM_059893140.1 → XP_059749123.1  5-oxoprolinase isoform X4

    3. XM_059893139.1 → XP_059749122.1  5-oxoprolinase isoform X2

    4. XM_059893142.1 → XP_059749125.1  5-oxoprolinase isoform X6

    5. XM_059893141.1 → XP_059749124.1  5-oxoprolinase isoform X5

      UniProtKB/Swiss-Prot
      F1ME97, Q75WB5

    6. XM_015474330.3 → XP_015329816.1  5-oxoprolinase isoform X3

      UniProtKB/TrEMBL
      A0A3Q1LQE0
      Conserved Domains (4) summary
      PLN02666
      Location:25 → 1283
      PLN02666; 5-oxoprolinase
      pfam01968
      Location:256 → 538
      Hydantoinase_A; Hydantoinase/oxoprolinase
      pfam02538
      Location:759 → 1281
      Hydantoinase_B; Hydantoinase B/oxoprolinase
      pfam05378
      Location:34 → 237
      Hydant_A_N; Hydantoinase/oxoprolinase N-terminal region

    7. XM_010811822.4 → XP_010810124.1  5-oxoprolinase isoform X7

      UniProtKB/TrEMBL
      A0A3Q1LQE0
      Conserved Domains (1) summary
      cl19816
      Location:2 → 1134
      Hydantoinase_B; Hydantoinase B/oxoprolinase
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q75WB5.2 GenPept UniProtKB/Swiss-Prot:Q75WB5

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Molecular Biology Databases
    Research Materials