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Links from Protein

Items: 3

1.

Biotin and Thiamin Synthesis associated domain

Biotin synthase (BioB), EC:2.8.1.6 , 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 [1]. 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 family) and form a heterodimer[2]. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers [1,2]. This domain therefore may be involved in co-factor binding or dimerisation (Finn, RD personal observation). [1]. 12482614. The PLP-dependent biotin synthase from Escherichia coli:. mechanistic studies.. Ollagnier-de-Choudens S, Mulliez E, Fontecave M;. FEBS Lett 2002;532:465-468.. [2]. 12650933. Thiamine biosynthesis in Escherichia coli: isolation and initial. characterisation of the ThiGH complex.. Leonardi R, Fairhurst SA, Kriek M, Lowe DJ, Roach PL;. FEBS Lett 2003;539:95-99. (from Pfam)

Date:
2024-08-14
Family Accession:
NF018651.5
Method:
HMM
2.
new record, indexing in progress
Family Accession:
3.

2-iminoacetate synthase ThiH

ThiH, a radical SAM enzyme involved in thiamine biosynthesis, acts on L-tyrosine and produces 2-iminoacetate. An alternate pathway for biosynthesis of the intermediate hydroxyethylthiazole relies instead on ThiO starting with glycine. Other proteins involved in hydroxyethylthiazole biosynthesis include ThiF, ThiS, and ThiG.

Gene:
thiH
GO Terms:
Molecular Function:
iron ion binding (GO:0005506)
Biological Process:
thiamine biosynthetic process (GO:0009228)
Molecular Function:
lyase activity (GO:0016829)
Molecular Function:
4 iron, 4 sulfur cluster binding (GO:0051539)
Molecular Function:
S-adenosyl-L-methionine binding (GO:1904047)
Date:
2024-05-30
Family Accession:
TIGR02351.2
Method:
HMM
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