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Information on EC 1.14.14.13 - 4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase and Organism(s) Niallia circulans and UniProt Accession Q4H4E5

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IUBMB Comments
Catalyses a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. FMNH2 is used as a free cofactor. Forms a complex with a dedicated NAD(P)H:FMN oxidoreductase. The enzyme is not able to hydroxylate free substrates, activation by the acyl-carrier protein is mandatory. Octanoyl-S-[BtrI acyl-carrier protein] is also accepted.
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This record set is specific for:
Niallia circulans
UNIPROT: Q4H4E5
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The taxonomic range for the selected organisms is: Niallia circulans
The enzyme appears in selected viruses and cellular organisms
Synonyms
btrO, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
btrO
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein],FMN:oxygen oxidoreductase (2-hydroxylating)
Catalyses a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. FMNH2 is used as a free cofactor. Forms a complex with a dedicated NAD(P)H:FMN oxidoreductase. The enzyme is not able to hydroxylate free substrates, activation by the acyl-carrier protein is mandatory. Octanoyl-S-[BtrI acyl-carrier protein] is also accepted.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-(L-gamma-glutamylamino)butanoyl-[BtrI acyl-carrier protein] + FMNH2 + O2
4-(L-gamma-glutamylamino)-(2S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] + FMN + H2O
show the reaction diagram
presence of FMN and O2 are required
-
-
?
butanoyl-[BtrI acyl-carrier protein] + FMNH2 + O2
(2S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] + FMN + H2O
show the reaction diagram
-
-
-
?
octanoyl-[BtrI acyl-carrier protein] + FMNH2 + O2
(2S)-2-hydroxyoctanoyl-[BtrI acyl-carrier protein] + FMN + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
no substrates: butanoate, butanoyl-CoA, L-glutamate, L-aspartate, gamma-aminobutanoate, and L-ornithine
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
no cofactor: FAD
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
putative
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
involved in biosynthesis of the aminoglycoside antibiotic butirosin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BTRO_NIACI
341
0
38740
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38700
x * 38700, calculated, x * 40000, SDS-PAGE of recombinant His-tagged protein
40000
x * 38700, calculated, x * 40000, SDS-PAGE of recombinant His-tagged protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 38700, calculated, x * 40000, SDS-PAGE of recombinant His-tagged protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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 (Q4H4E5)
Manually annotated by BRENDA team