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basl-1 Aromatic-L-amino-acid decarboxylase [ Caenorhabditis elegans ]

Gene ID: 175779, updated on 2-Nov-2024

Summary

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Official Symbol
basl-1
Official Full Name
Aromatic-L-amino-acid decarboxylase
Primary source
WormBase:WBGene00015467
Locus tag
CELE_C05D2.3
See related
AllianceGenome:WB:WBGene00015467
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Caenorhabditis elegans (strain: Bristol N2)
Lineage
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary
Predicted to enable aromatic-L-amino-acid decarboxylase activity. Predicted to be involved in catecholamine metabolic process and serotonin biosynthetic process. Predicted to be active in cytoplasm. Human ortholog(s) of this gene implicated in Parkinson's disease; aromatic L-amino acid decarboxylase deficiency; bipolar disorder; inherited metabolic disorder; and nicotine dependence. Orthologous to human DDC (dopa decarboxylase). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See basl-1 in Genome Data Viewer
Location:
chromosome: III
Exon count:
8
Sequence:
Chromosome: III; NC_003281.10 (5614948..5617261)

Chromosome III - NC_003281.10Genomic Context describing neighboring genes Neighboring gene X chromosome NonDisjunction factor Neighboring gene DUF3598 domain-containing protein Neighboring gene Aromatic-L-amino-acid decarboxylase Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene Cell surface receptor daf-4;Serine/threonine-protein kinase receptor;receptor protein serine/threonine kinase Neighboring gene ncRNA

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_003281.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Function and evolution of the serotonin-synthetic bas-1 gene and other aromatic amino acid decarboxylase genes in Caenorhabditis. Hare EE, et al. BMC Evol Biol, 2004 Aug 2. PMID 15287963, Free PMC Article
  2. OrthoList 2: A New Comparative Genomic Analysis of Human and Caenorhabditis elegans Genes. Kim W, et al. Genetics, 2018 Oct. PMID 30120140, Free PMC Article
  3. Genome sequence of the nematode C. elegans: a platform for investigating biology. C. elegans Sequencing Consortium. Science, 1998 Dec 11. PMID 9851916

GeneRIFs: Gene References Into Functions

General gene information

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Markers

Homology

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables aromatic-L-amino-acid decarboxylase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables carbon-carbon lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables carboxy-lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables pyridoxal phosphate binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in amino acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in carboxylic acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in catecholamine metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in serotonin biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  

General protein information

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Preferred Names
Aromatic-L-amino-acid decarboxylase
NP_498210.1
  • Confirmed by transcript evidence

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_003281.10 Reference assembly

    Range
    5614948..5617261
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_065809.5 → NP_498210.1  Aromatic-L-amino-acid decarboxylase [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_498210.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    O45138
    Conserved Domains (1) summary
    cl18945
    Location:1 → 508
    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
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