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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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