BATS

Biotin and Thiamin Synthesis associated domain

• SMART accession number: SM00876
• Description: Biotin synthase (BioB), , catalyses the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer (PUBMED:12482614). Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this entry) and form a heterodimer(PUBMED:12650933). Both of these reactions are thought of involve the binding of co-factors, and both function as dimers (PUBMED:12482614), (PUBMED:12650933). This domain therefore may be involved in co-factor binding or dimerisation.
• Interpro abstract (IPR010722):

  This domain is found in biotin synthase and 2-iminoacetate synthase. The latter enzyme is involved in thiamine diphosphate biosynthesis. The reactions catalysed by these enzymes involve the binding of co-factors and both enzymes function as dimers [ (PUBMED:12482614) (PUBMED:12650933) ]. This domain may therefore be involved in co-factor binding or dimerisation. The domain is also found in proteins that are currently uncharacterised, such as Q58195 .

There are 20794 BATS domains in 20792 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Cellular role: interaction

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Leonardi R, Fairhurst SA, Kriek M, Lowe DJ, Roach PL
• Thiamine biosynthesis in Escherichia coli: isolation and initialcharacterisation of the ThiGH complex.
• FEBS Lett. 2003; 539: 95-9

In Escherichia coli, two of the proteins required for the biosynthesis ofthe thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH, encodedas part of the thiCEFSGH operon. In this study, a C-terminallyhexahistidine-tagged ThiH (ThiH-His) was expressed in E. coli as a solubleprotein from thiGH-His-tag and thiFSGH-His-tag-bearing plasmids. Whenisolated under anaerobic conditions, ThiG and ThiH-His co-purify as alarge multimeric non-covalent complex. Electron paramagnetic resonance andUV-visible spectroscopy together with iron and sulfide analyses revealedthe presence of an iron-sulfur cluster within this complex.

• Ollagnier-de-Choudens S, Mulliez E, Fontecave M
• The PLP-dependent biotin synthase from Escherichia coli: mechanisticstudies.
• FEBS Lett. 2002; 532: 465-8

Biotin synthase (BioB), an iron-sulfur enzyme, catalyzes the last step ofthe biotin biosynthesis pathway. The reaction consists in the introductionof a sulfur atom into two non-activated C-H bonds of dethiobiotin.Substrate radical activation is initiated by the reductive cleavage ofS-adenosylmethionine (AdoMet) into a 5'-deoxyadenosyl radical. Therecently described pyridoxal 5'-phosphate-bound enzyme was used to showthat only one molecule of AdoMet, and not two, is required for theformation of one molecule of biotin. Furthermore 5'-deoxyadenosine, aproduct of the reaction, strongly inhibited biotin formation, anobservation that may explain why BioB is not able to make more than oneturnover. However this enzyme inactivation is not irreversible.

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
79.15	map00780	Biotin metabolism
20.18	map00730	Thiamine metabolism
0.67	map00510	N-Glycan biosynthesis

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with BATS domain which could be assigned to a KEGG orthologous group, and not all proteins containing BATS domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of BATS domains in PDB

PDB code	Title
1r30	The Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme
3ciw	X-RAY structure of the [FeFe]-hydrogenase maturase HydE from thermotoga maritima
3cix	X-RAY structure of the [FeFe]-hydrogenase maturase HydE from thermotoga maritima in complex with thiocyanate
3iix	X-ray structure of the FeFe-hydrogenase maturase HydE from T. maritima in complex with methionine and 5'deoxyadenosine
3iiz	X-ray structure of the FeFe-hydrogenase maturase HydE from T. maritima in complex with S-adenosyl-L-methionine
4jxc	X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters
4jy8	X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters
4jy9	X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters
4jyd	X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters.
4jye	X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters.
4jyf	X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters.
4r33	4R33
4r34	4R34
4rtb	4RTB
4wcx	4WCX
5fep	5FEP
5fes	5FES
5few	5FEW
5fex	5FEX
5fez	5FEZ
5ff0	5FF0
5ff2	5FF2
5ff3	5FF3
5ff4	5FF4

Links (links to other resources describing this domain)

• PFAM: BATS
• INTERPRO: IPR010722