dbt-1 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: dbt-1
Official Full Name: Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Primary source: WormBase:WBGene00014054
Locus tag: CELE_ZK669.4
See related: AllianceGenome:WB:WBGene00014054
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 acetyltransferase activity and lipoic acid binding activity. Involved in several processes, including positive regulation of egg-laying behavior; positive regulation of fatty acid biosynthetic process; and positive regulation of nematode larval development. Located in cilium; cytosol; and neuron projection. Is expressed in several structures, including body wall musculature; hypodermis; and intestine. Human ortholog(s) of this gene implicated in maple syrup urine disease. Orthologous to human DBT (dihydrolipoamide branched chain transacylase E2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See dbt-1 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 10

Sequence:: Chromosome: II; NC_003280.10 (7942602..7945206, complement)

Chromosome II - NC_003280.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003280.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

This study implicates the branched-chain alpha-keto acid dehydrogenase complex and branched-chain amino acid metabolism in arsenic responses, demonstrating the power of Caenorhabditis elegans natural genetic diversity to identify novel mechanisms by which environmental toxins affect organismal physiology.
Title: Natural variation in C. elegans arsenic toxicity is explained by differences in branched chain amino acid metabolism.

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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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Markers

ZK669.4 (e-PCR)
- UniSTS:308298

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables acetyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables acyltransferase activity	IEA Inferred from Electronic Annotation more info
enables dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity	IEA Inferred from Electronic Annotation more info
enables lipoic acid binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in fatty acid biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of egg-laying behavior	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of embryonic development	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of fatty acid biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of nematode larval development	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cell projection	IEA Inferred from Electronic Annotation more info
located_in cilium	IDA Inferred from Direct Assay more info	PubMed
located_in cilium	IEA Inferred from Electronic Annotation more info
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in dendrite	IEA Inferred from Electronic Annotation more info
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
located_in neuron projection	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

NP_495670.1

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

NC_003280.10 Reference assembly

Range

7942602..7945206 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_063269.7 → NP_495670.1 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_495670.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q23571

Conserved Domains (4) summary

cd06849
Location:31 → 104

lipoyl_domain; Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid ...

PLN02528
Location:33 → 448

PLN02528; 2-oxoisovalerate dehydrogenase E2 component

pfam00198
Location:233 → 445

2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain)

pfam02817
Location:146 → 179

E3_binding; e3 binding domain