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    FMS1 polyamine oxidase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855034, updated on 9-Dec-2024

    Summary

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    Official Symbol
    FMS1
    Official Full Name
    polyamine oxidase
    Primary source
    SGD:S000004622
    Locus tag
    YMR020W
    See related
    AllianceGenome:SGD:S000004622; FungiDB:YMR020W; VEuPathDB:YMR020W
    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 polyamine oxidase activity. Involved in pantothenate biosynthetic process and spermine catabolic process. Located in cytoplasm. Orthologous to several human genes including KDM1B (lysine demethylase 1B). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See FMS1 in Genome Data Viewer
    Location:
    chromosome: XIII
    Exon count:
    1
    Sequence:
    Chromosome: XIII; NC_001145.3 (315377..316903)

    Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene Pex9p Neighboring gene Stb4p Neighboring gene Mac1p Neighboring gene E2 ubiquitin-conjugating protein UBC7

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001145.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Characterization of the Saccharomyces cerevisiae FMS1 gene related to Candida albicans corticosteroid-binding protein 1. Joets J, et al. Curr Genet, 1996 Jul 31. PMID 8660467
    2. Crystal structures of Fms1 and its complex with spermine reveal substrate specificity. Huang Q, et al. J Mol Biol, 2005 May 13. PMID 15843025
    3. Mechanistic and structural analyses of the role of His67 in the yeast polyamine oxidase Fms1. Adachi MS, et al. Biochemistry, 2012 Jun 19. PMID 22642831, Free PMC Article
    4. Controlling the regioselectivity and stereospecificity of FAD-dependent polyamine oxidases with the use of amine-attached guide molecules as conformational modulators. Keinänen TA, et al. Biosci Rep, 2018 Aug 31. PMID 30006473, Free PMC Article
    5. Mechanistic studies of the yeast polyamine oxidase Fms1: kinetic mechanism, substrate specificity, and pH dependence. Adachi MS, et al. Biochemistry, 2010 Dec 14. PMID 21067138, Free PMC Article

    See all (40) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The results are consistent with the role of Asn195 and Asp94 being to properly position the polyamine substrate for oxidation.
      Title: Mechanistic and structural analyses of the roles of active site residues in yeast polyamine oxidase Fms1: characterization of the N195A and D94N enzymes.
    2. X ray structure; Fms1 consists of an FAD-binding domain, with Rossmann fold topology, and a substrate-binding domain
      Title: Crystal structures of Fms1 and its complex with spermine reveal substrate specificity.
    Submit: New GeneRIF Correction

    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 N(1)-acetylpolyamine oxidase (3-acetamidopropanal-forming) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables polyamine oxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables polyamine oxidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables spermine oxidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in pantothenate biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in spermine catabolic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in spermine catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 

    General protein information

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    Preferred Names
    polyamine oxidase
    NP_013733.1
    • Polyamine oxidase; converts spermine to spermidine, which is required for the essential hypusination modification of translation factor eIF-5A; also involved in pantothenic acid biosynthesis

    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_001145.3 Reference assembly

      Range
      315377..316903
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182516.1 → NP_013733.1  TPA: polyamine oxidase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013733.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VZJ4, P50264
      UniProtKB/TrEMBL
      A6ZM82, B3LLS1, G2WK71, N1P5C2
      Conserved Domains (1) summary
      pfam01593
      Location:18 → 503
      Amino_oxidase; Flavin containing amine oxidoreductase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P50264.1

    Gene LinkOut

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