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    mal maroon-like [ Drosophila melanogaster (fruit fly) ]

    Gene ID: 33045, updated on 9-Dec-2024

    Summary

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    Official Symbol
    malprovided by FlyBase
    Official Full Name
    maroon-likeprovided by FlyBase
    Primary source
    FLYBASE:FBgn0002641
    Locus tag
    Dmel_CG1692
    See related
    AllianceGenome:FB:FBgn0002641
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Drosophila melanogaster
    Lineage
    Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora
    Also known as
    5; bz; CG1692; Dmel\CG1692; ma-l; SRF
    Summary
    Enables molybdenum cofactor sulfurtransferase activity. Involved in molybdopterin cofactor biosynthetic process. Is expressed in organism. Human ortholog(s) of this gene implicated in xanthinuria type II. Orthologous to human MOCOS (molybdenum cofactor sulfurase). [provided by Alliance of Genome Resources, Dec 2024]
    Orthologs
    all
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    Genomic context

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    See mal in Genome Data Viewer
    Location:
    19D1-19D1; 1-64 cM
    Exon count:
    4
    Annotation release Status Assembly Chr Location
    Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) X NC_004354.4 (20429675..20433210)
    Release 5.57 previous assembly Release 5 (GCF_000001215.2) X NC_004354.3 (20300702..20304237)

    Chromosome X - NC_004354.4Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Gene expression in Drosophila: post-translational modification of aldehyde oxidase and xanthine dehydrogenase. Finnerty V, et al. Mol Gen Genet, 1979 Apr 17. PMID 286873
    2. [Further studies on complementarity and nonautonomy of eye color mutants ma-1 and ma-1/bz of Drosophila melanogaster]. URSPRUNG H. Z Vererbungsl, 1961. PMID 13923942
    3. Studies on genetic organization in higher organisms. II. Complementation and fine structure of the maroon-like locus of Drosophila melanogaster. Finnerty VG, et al. Proc Natl Acad Sci U S A, 1970 Apr. PMID 5266164, Free PMC Article
    4. Biochemical differences between the mutants Rosy-2 and maroon-like of Drosophila melanogaster. FORREST HS, et al. Genetics, 1961 Nov. PMID 13894114, Free PMC Article
    5. Post-Translational Modification as a Potential Explanation of High Levels of Enzyme Polymorphism: Xanthine Dehydrogenase and Aldehyde Oxidase in DROSOPHILA MELANOGASTER. Finnerty V, et al. Genetics, 1979 Apr. PMID 17248907, Free PMC Article

    See all (94) 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 FlyBase

    Function Evidence Code Pubs
    enables molybdenum cofactor sulfurtransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables molybdenum cofactor sulfurtransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables molybdenum cofactor sulfurtransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables molybdenum cofactor sulfurtransferase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    enables molybdenum ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables pyridoxal phosphate binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in Mo-molybdopterin cofactor biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in molybdopterin cofactor biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in molybdopterin cofactor metabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in molybdopterin cofactor metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in molybdopterin cofactor metabolic process ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  

    General protein information

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    Preferred Names
    maroon-like
    Names
    CG1692-PA
    CG1692-PB
    bronzy
    mal-PA
    mal-PB
    maroonlike
    section 5
    NP_001285493.1
    NP_523423.1

    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_004354.4 Reference assembly

      Range
      20429675..20433210
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001298564.1 → NP_001285493.1  maroon-like, isoform B [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_001285493.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      Q9U9P1, Q9VRA2
      UniProtKB/TrEMBL
      X2JFY7
      Conserved Domains (4) summary
      PLN02724
      Location:17 → 753
      PLN02724; Molybdenum cofactor sulfurase
      pfam03473
      Location:651 → 754
      MOSC; MOSC domain
      pfam03476
      Location:511 → 633
      MOSC_N; MOSC N-terminal beta barrel domain
      cl18945
      Location:29 → 475
      AAT_I; Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the ...

    2. NM_078699.3 → NP_523423.1  maroon-like, isoform A [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_523423.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      Q9U9P1, Q9VRA2
      UniProtKB/TrEMBL
      X2JFY7
      Related
      FBpp0076998
      Conserved Domains (4) summary
      PLN02724
      Location:17 → 753
      PLN02724; Molybdenum cofactor sulfurase
      pfam03473
      Location:651 → 754
      MOSC; MOSC domain
      pfam03476
      Location:511 → 633
      MOSC_N; MOSC N-terminal beta barrel domain
      cl18945
      Location:29 → 475
      AAT_I; Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q9VRA2.1 Q9VRA2
    X2JFY7 X2JFY7

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