Putative antilisterial bacteriocin (subtilosin) production enzyme; Catalyzes the formation of 3 thioether bonds during production of the sactipeptide subtilosin from SboA. In vitro the thioether bonds cannot be made in the absence of the SboA propeptide, suggesting this is the first reaction in subtilosin maturation. In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5'-dA.

uroporphyrin-III C-methyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the precorrin methyltransferase family.

Putative antilisterial bacteriocin (subtilosin) production enzyme; Catalyzes the formation of 3 thioether bonds during production of the sactipeptide subtilosin from SboA. In vitro the thioether bonds cannot be made in the absence of the SboA propeptide, suggesting this is the first reaction in subtilosin maturation. In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5'-dA.

Synthesis of sporulation killing factor A; Catalyzes the formation of the thioether bond required for production of the sporulation killing factor (SKF) from SkfA. Forms the cysteine-methionine thioether bond found in SKF; the acceptor amino acid can be hydrophobic, aromatic or a small hydrophilic amino acid but not a larger hydrophilic amino acid, i.e. Met=Ala, Phe, Leu, Tyr>Asn, Ser>>Gln, Glu, Lys. The relative position of Cys and Met in the substrate cannot be inverted, in vitro the thioether bond cannot be made in the absence of the SkfA propeptide, suggesting this is the first rea [...]

Putative antilisterial bacteriocin (subtilosin) production enzyme; Catalyzes the formation of 3 thioether bonds during production of the sactipeptide subtilosin from SboA. In vitro the thioether bonds cannot be made in the absence of the SboA propeptide, suggesting this is the first reaction in subtilosin maturation. In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5'-dA.

Putative AdoMet radical enzyme; Required for production of the modified peptide YydF (Probable). May activate a metalloenzyme (Potential).

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

Lysine-8-amino-7-oxononanoate aminotransferase; Catalyzes the transfer of the alpha-amino group from L-lysine to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). B.subtilis is the only bacterium known to utilize L-lysine as an amino donor in the biosynthesis of DAPA. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

Lysine 2,3-aminomutase; Catalyzes the interconversion of L-alpha-lysine and L-beta- lysine; Belongs to the radical SAM superfamily. KamA family.

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

Lipoyl synthase (lipoic acid synthetase); Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives; Belongs to the radical SAM superfamily. Lipoyl synthase family.

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

Enzyme for ms(2)i(6)A formation for tRNA modification; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

Molybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate (By similarity). Required for both nitrate assimilation and respiration.

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

tRNA N(6)-threonylcarbamoyladenosine (t(6)A) methylthiotransferase; Catalyzes the methylthiolation of N6- threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine. Belongs to the methylthiotransferase family. MtaB subfamily.

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

7-carboxy-7-deazaguanine synthase; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

Synthesis of sporulation killing factor A; Catalyzes the formation of the thioether bond required for production of the sporulation killing factor (SKF) from SkfA. Forms the cysteine-methionine thioether bond found in SKF; the acceptor amino acid can be hydrophobic, aromatic or a small hydrophilic amino acid but not a larger hydrophilic amino acid, i.e. Met=Ala, Phe, Leu, Tyr>Asn, Ser>>Gln, Glu, Lys. The relative position of Cys and Met in the substrate cannot be inverted, in vitro the thioether bond cannot be made in the absence of the SkfA propeptide, suggesting this is the first rea [...]

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

Spore photoproduct (thymine dimer) lyase; Involved in repair of UV radiation-induced DNA damage during spore germination. Can repair thymine dimer 5-thyminyl-5,6- dihydrothymine (known as spore photoproduct (SP)) by in situ monomerization of SP to two thymines.

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

Biosynthesis of the pyrimidine moiety from 5-aminoimidazole ribotide (AIR) (thiamin biosynthesis); Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family.

Lysine-8-amino-7-oxononanoate aminotransferase; Catalyzes the transfer of the alpha-amino group from L-lysine to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). B.subtilis is the only bacterium known to utilize L-lysine as an amino donor in the biosynthesis of DAPA. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.

Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.

Lysine-8-amino-7-oxononanoate aminotransferase; Catalyzes the transfer of the alpha-amino group from L-lysine to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). B.subtilis is the only bacterium known to utilize L-lysine as an amino donor in the biosynthesis of DAPA. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.

Biosynthesis of the pyrimidine moiety from 5-aminoimidazole ribotide (AIR) (thiamin biosynthesis); Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family.

Conserved hypothetical protein; This methylase may recognize the double-stranded sequence CTCGAG, causing specific methylation on C-? on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

DNA-methyltransferase (cytosine-specific); This methylase may recognize the double-stranded sequence CTCGAG, causing specific methylation on C-? on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Conserved hypothetical protein; This methylase may recognize the double-stranded sequence CTCGAG, causing specific methylation on C-? on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

DNA (cytosine-5-)-methyltransferase; This enzyme methylates the first cytosine within the sequences GGCC and GCNGC; Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Conserved hypothetical protein; This methylase may recognize the double-stranded sequence CTCGAG, causing specific methylation on C-? on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

S-adenosylmethionine decarboxylase; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.

Conserved hypothetical protein; This methylase may recognize the double-stranded sequence CTCGAG, causing specific methylation on C-? on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Putative AdoMet-dependent methyltransferase; Could be a S-adenosyl-L-methionine-dependent methyltransferase; Belongs to the methyltransferase superfamily. YrrT family.

DNA-methyltransferase (cytosine-specific); This methylase may recognize the double-stranded sequence CTCGAG, causing specific methylation on C-? on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Conserved hypothetical protein; This methylase may recognize the double-stranded sequence CTCGAG, causing specific methylation on C-? on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.