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Information on EC 6.2.1.39 - [butirosin acyl-carrier protein]-L-glutamate ligase and Organism(s) Niallia circulans and UniProt Accession Q4H4E7

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EC Tree
IUBMB Comments
Catalyses two steps in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. The enzyme adds one molecule of L-glutamate to a dedicated acyl-carrier protein, and following decarboxylation of the product by EC 4.1.1.95, L-glutamyl-[BtrI acyl-carrier protein] decarboxylase, adds a second L-glutamate molecule. Requires Mg2+ or Mn2+, and activity is enhanced in the presence of Mn2+.
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Niallia circulans
UNIPROT: Q4H4E7
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The taxonomic range for the selected organisms is: Niallia circulans
The enzyme appears in selected viruses and cellular organisms
Synonyms
BtrJ, [BtrI acyl-carrier protein]L-glutamate ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BtrJ
-
-
-
-
[BtrI acyl-carrier protein]L-glutamate ligase
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-
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-
SYSTEMATIC NAME
IUBMB Comments
[BtrI acyl-carrier protein]:L-glutamate ligase (ADP-forming)
Catalyses two steps in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. The enzyme adds one molecule of L-glutamate to a dedicated acyl-carrier protein, and following decarboxylation of the product by EC 4.1.1.95, L-glutamyl-[BtrI acyl-carrier protein] decarboxylase, adds a second L-glutamate molecule. Requires Mg2+ or Mn2+, and activity is enhanced in the presence of Mn2+.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 4-aminobutanoate + BtrI acyl-carrier protein
ADP + phosphate + 4-aminobutanoyl-S-[BtrI acyl-carrier protein]
show the reaction diagram
-
GABA-S-BtrI is closely related to holo-BtrI
-
?
ATP + L-glutamate + 4-aminobutanoyl-[BtrI acyl-carrier protein]
ADP + phosphate + 4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein]
show the reaction diagram
-
-
-
?
ATP + L-glutamate + 4-aminobutanoyl-[BtrI acyl-carrier protein]
ADP + phosphate + L-Glu-4-aminobutanoyl-S-[BtrI acyl-carrier protein]
show the reaction diagram
BtrJ is able to catalyze ligation of a second L-glutamate molecule to GABA-S-BtrI, forming an amide bond
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-
?
ATP + L-glutamate + BtrI acyl-carrier protein
ADP + phosphate + L-glutamyl-[BtrI acyl-carrier protein]
show the reaction diagram
-
-
-
?
additional information
?
-
the reaction mechanism is proposed to involve the generation of an acylphosphate intermediate via hydrolysis of ATP to ADP. No activity with (2S)-4-amino-2-hydroxybutyrate, AHBA. No gamma-L-Glu-gamma-L-Glu-S-BtrI produced in the BtrJ assay
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + 4-aminobutanoyl-[BtrI acyl-carrier protein]
ADP + phosphate + 4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein]
show the reaction diagram
-
-
-
?
ATP + L-glutamate + BtrI acyl-carrier protein
ADP + phosphate + L-glutamyl-[BtrI acyl-carrier protein]
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
essentially required
Mn2+
essentially required, activates
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene btrJ
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
BtrJ belongs to the ATP-grasp superfamily
metabolism
butirosin biosynthetic cluster, proceeds via intermediates tethered to a specific acyl carrier protein and gamma-glutamylation of an ACP-derived gamma-aminobutyrate intermediate. The pathway involves the acyl carrier protein BtrI, an ATP-dependent ligase BtrJ, a pyridoxal phosphate-dependent decarboxylase BtrK, and a two-component flavin-dependent monooxygenase system BtrO and BtrV, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BTRJ_NIACI
419
0
48648
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48600
1 * 48600, about, SDS-PAGE, 1 * 50962, His6-tagged BtrJ, mass spectrometry, 1 * 50969, His6-tagged BtrJ, sequence calculation
50962
1 * 48600, about, SDS-PAGE, 1 * 50962, His6-tagged BtrJ, mass spectrometry, 1 * 50969, His6-tagged BtrJ, sequence calculation
50969
1 * 48600, about, SDS-PAGE, 1 * 50962, His6-tagged BtrJ, mass spectrometry, 1 * 50969, His6-tagged BtrJ, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 48600, about, SDS-PAGE, 1 * 50962, His6-tagged BtrJ, mass spectrometry, 1 * 50969, His6-tagged BtrJ, sequence calculation
additional information
purified BtrJ shows aggregation in solution, preventable by DTT
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene btrJ, butirosin genetic cluster organization, overview. Expression of N-terminal His6-tagged BtrJ
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, Y.; Llewellyn, N.M.; Giri, R.; Huang, F.; Spencer, J.B.
Biosynthesis of the unique amino acid side chain of butirosin: possible protective-group chemistry in an acyl carrier protein-mediated pathway
Chem. Biol.
12
665-675
2005
Niallia circulans (Q4H4E7), Niallia circulans NR3312 (Q4H4E7)
Manually annotated by BRENDA team