bioB biotin synthase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: bioB
Official Full Name: biotin synthase
Primary source: ECOCYC:EG10118
Locus tag: b0775
See related: ASAP:ABE-0002644
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK0764
Summary: Radical SAM superfamily. [More information is available at EcoGene: EG10118]. Biotin synthase catalyzes the final reaction of biotin biosynthesis by inserting a sulfur atom between C6 and C9 of dethiobiotin in a S-adenosylmethoinine (SAM)-dependent reaction. [More information is available at EcoCyc: EG10118].
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Genomic context

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Sequence:: NC_000913.3 (809344..810384)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

In biotin synthase, abstraction of a hydrogen atom from the C9 methyl group of dethiobiotin results in formation of a dethiobiotinyl methylene carbon radical, which is quenched by a sulfur atom to form a new carbon-sulfur bond in 9-mercaptodethiobiotin.
Title: Reduction of the [2Fe-2S] cluster accompanies formation of the intermediate 9-mercaptodethiobiotin in Escherichia coli biotin synthase.
Asparagine 153 and aspartate 155 of bioB are important for retaining intermediates during the catalytic cycle.
Title: Protein residues that control the reaction trajectory in S-adenosylmethionine radical enzymes: mutagenesis of asparagine 153 and aspartate 155 in Escherichia coli biotin synthase.
mutations in the conserved YNHNLD sequence of Escherichia coli BioB affect the formation and stability of the [4Fe-4S](1+) cluster on reduction with dithionite and report the observation of a new [2Fe-2S](1+) cluster.
Title: Iron-sulfur cluster dynamics in biotin synthase: a new [2Fe-2S](1+) cluster.
It is proposed that the [2Fe-2S]2+ cluster of biotin synthase is both the sulfur-donating substrate and the sulfur-oxidizing cofactor, but each round of catalysis generates an inactive enzyme in which this cluster has been destroyed.
Title: Loss of iron-sulfur clusters from biotin synthase as a result of catalysis promotes unfolding and degradation.
mutants of highly conserved residues from the Y(150)NHNLD motif are inactive & are also unable to cleave AdoMet and to produce the deoxyadenosyl radical (AdoCH(2)(*)).
Title: Biotin synthase mechanism: mutagenesis of the YNHNLD conserved motif.

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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

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables 2 iron, 2 sulfur cluster binding	IBA Inferred from Biological aspect of Ancestor more info
enables 2 iron, 2 sulfur cluster binding	IDA Inferred from Direct Assay more info	PubMed
enables 2 iron, 2 sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables 4 iron, 4 sulfur cluster binding	IDA Inferred from Direct Assay more info	PubMed
enables 4 iron, 4 sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables biotin synthase activity	IBA Inferred from Biological aspect of Ancestor more info
enables biotin synthase activity	IDA Inferred from Direct Assay more info	PubMed
enables biotin synthase activity	IEA Inferred from Electronic Annotation more info
enables iron ion binding	IEA Inferred from Electronic Annotation more info
enables iron-sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	IDA Inferred from Direct Assay more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in biotin biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in biotin biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in biotin biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in sulfur compound biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in water-soluble vitamin biosynthetic process	IEA Inferred from Electronic Annotation more info