Literature summary extracted from

Popovic, B.; Tang, X.; Chirgadze, D.Y.; Huang, F.; Blundell, T.L.; Spencer, J.B.
Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis (2006), Proteins, 65, 220-230.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.6.1.100	gene btrR, expression in Escherichia coli strain BL21 (DE3) as His-tagged enzyme	Niallia circulans
2.6.1.101	gene btrR, expression in Escherichia coli strain BL21 (DE3) as His-tagged enzyme	Niallia circulans

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.6.1.100	purified recombinant enzyme compplexed with pyridoxamine 5'-phosphate or pyridoxal 5'-phosphate, 7-14 days, X-ray diffraction structure determination and analysis at 1.7 A and 2.1 A resolution, respectively	Niallia circulans
2.6.1.101	purified recombinant enzyme complexed with pyridoxamine 5'-phosphate or pyridoxal 5'-phosphate, 7-14 days, X-ray diffraction structure determination and analysis at 1.7 A and 2.1 A resolution, respectively	Niallia circulans

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.6.1.100	additional information	no inhibition by gabaculine, i.e. 3-amino-2,3-dihydrobenzoic acid, and (amino-oxy) acetic acid	Niallia circulans
2.6.1.101	additional information	no inhibition by gabaculine, i.e. 3-amino-2,3-dihydrobenzoic acid, and (amino-oxy) acetic acid	Niallia circulans

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2.6.1.100	L-glutamine + 2-deoxy-scyllo-inosose	Niallia circulans	-	2-oxoglutaramate + 2-deoxy-scyllo-inosamine	-	r
2.6.1.101	L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose	Niallia circulans	-	2-oxoglutaramate + 2-deoxystreptamine	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.6.1.100	Niallia circulans	Q8G8Y2	gene btrR	-
2.6.1.101	Niallia circulans	Q8G8Y2	gene btrR	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
2.6.1.100	recombinant His-tagged BtrR from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration	Niallia circulans
2.6.1.101	recombinant His-tagged BtrR from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration	Niallia circulans

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.6.1.100	L-glutamine + 2-deoxy-scyllo-inosose	-	Niallia circulans	2-oxoglutaramate + 2-deoxy-scyllo-inosamine	-	r
2.6.1.100	additional information	BtrR accepts four different carbocyclic substrates, 2-deoxy-scyllo-inosose, 2-deoxy-scyllo-inosamine, a ino-dideoxyscyllo-inosose, and 2-deoxysteptamine, requiring the binding site in the enzyme to have some flexibility. NeoB also shows L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-streptamine, EC 2.6.1.101. The existence of the closed conformation contributes to reaction type specificity within the aspartate aminotransferase family	Niallia circulans	?	-	?
2.6.1.101	L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose	-	Niallia circulans	2-oxoglutaramate + 2-deoxystreptamine	-	?
2.6.1.101	additional information	BtrR accepts four different carbocyclic substrates, 2-deoxy-scyllo-inosose, 2-deoxy-scyllo-inosamine, amino-dideoxyscyllo-inosose, and 2-deoxysteptamine, requiring the binding site in the enzyme to have some flexibility. NeoB also shows L-glutamine:2-deoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-scyllo-inosamine, EC 2.6.1.100	Niallia circulans	?	-	?

Subunits

EC Number	Subunits	Comment	Organism
2.6.1.100	homodimer	the active site of the BtrR protomer is located in a cleft between an alpha-helical N-terminus, a central alphabetaalpha-sandwich domain and an alphabeta-C-terminal domain, three-dimensional structure, overview	Niallia circulans
2.6.1.101	homodimer	the active site of the BtrR protomer is located in a cleft between an alpha-helical N-terminus, a central alphabetaalpha-sandwich domain and an alphabeta-C-terminal domain, three-dimensional structure, overview	Niallia circulans

Synonyms

EC Number	Synonyms	Comment	Organism
2.6.1.100	btrR	-	Niallia circulans
2.6.1.101	btrR	-	Niallia circulans

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
2.6.1.100	pyridoxal 5'-phosphate	dependent on, binding structure and structural changes upon pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate conversion, overview	Niallia circulans
2.6.1.101	pyridoxal 5'-phosphate	dependent on, binding structure and structural changes upon pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate conversion, overview	Niallia circulans

General Information

EC Number	General Information	Comment	Organism
2.6.1.100	evolution	BtrR has a fold characteristic of the aspartate aminotransferase family and is a member of the class of aminotransferases that function primarily in the biosynthesis of secondary metabolites, SMAT, i.e. the secondary metabolite aminotransferases subfamily	Niallia circulans
2.6.1.100	metabolism	the aminotransferase BtrR is involved in the biosynthesis of butirosin	Niallia circulans
2.6.1.100	additional information	active site structure of BtrR, homodimer with two active sites per dimer, BtrR with bound pyridoxamine 5'-phosphate lacks the covalent bond to Lys192. The active site of the BtrR protomer is located in a cleft between an alpha-helical N-terminus, a central alphabetaalpha-sandwich domain and an alphabeta-C-terminal domain	Niallia circulans
2.6.1.100	physiological function	the aminotransferase BtrR is involved in the biosynthesis of butirosin, a 2-deoxystreptamine-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyzing the pyridoxal 5'-phosphate-dependent transamination reaction both of 2-deoxy-scylloinosose to 2-deoxy-scyllo-inosamine and of amino-dideoxy-scyllo-inosose to 2-deoxystreptamine, cf. EC 2.6.1.101	Niallia circulans
2.6.1.101	evolution	BtrR has a fold characteristic of the aspartate aminotransferase family and is a member of the class of aminotransferases that function primarily in the biosynthesis of secondary metabolites, SMAT, i.e. the secondary metabolite aminotransferases subfamily	Niallia circulans
2.6.1.101	metabolism	the aminotransferase BtrR is involved in the biosynthesis of butirosin	Niallia circulans
2.6.1.101	additional information	active site structure of BtrR, homodimer with two active sites per dimer, BtrR with bound pyridoxamine 5'-phosphate lacks the covalent bond to Lys192. The active site of the BtrR protomer is located in a cleft between an alpha-helical N-terminus, a central alphabetaalpha-sandwich domain and an alphabeta-C-terminal domain	Niallia circulans
2.6.1.101	physiological function	the aminotransferase BtrR is involved in the biosynthesis of butirosin, a 2-deoxystreptamine-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyzing the pyridoxal 5'-phosphate-dependent transamination reaction both of 2-deoxy-scylloinosose to 2-deoxy-scyllo-inosamine, cf. EC 2.6.1.100, and of amino-dideoxy-scyllo-inosose to 2-deoxystreptamine	Niallia circulans

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Release 2023.1 (January 2023)