Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup SPASM/twitch domain containing

  BtrN-like SPASM domain containing

     ⌊ Family 2-deoxy-scyllo-inosamine dehydrogenase (BtrN-like)

Total 100% <100%
Functional domains 10 9 1
UniProtKB 9 8 1
GI 22 19 3
Structures 2
Reactions 1
Functional domains of this family were last updated on June 10, 2017
New functional domains were last added to this family on June 22, 2014

BtrN catalyzes an unusual radical mediated dehydrogenation during aminoglycoside biosynthesis. Contains two [4Fe-4S] clusters, the first is the canonical radical SAM cluster, the second is implicated in substrate-radical oxidation (oxidises a secondary alcohol to a ketone). This family of proteins has a non-canonical structural architecture with a beta 5/alpha 4 motif.

Ruszczycky MW, Ogasawara Y, Liu HW

Radical SAM enzymes in the biosynthesis of sugar-containing natural products

▸ Abstract

Biochim Biophys Acta 2012;1824(11):1231-1244 | PubMed ID: 22172915

Yokoyama K, Numakura M, Kudo F, Ohmori D, Eguchi T

Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin

▸ Abstract

J Am Chem Soc 2007;129(49):15147-15155 | PubMed ID: 18001019

Goldman PJ, Grove TL, Booker SJ, Drennan CL

X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry

▸ Abstract

Proc Natl Acad Sci U S A 2013;110(40):15949-15954 | PubMed ID: 24048029

Maiocco SJ, Grove TL, Booker SJ, Elliott SJ

Electrochemical Resolution of the [4Fe-4S] Centers of the AdoMet Radical Enzyme BtrN: Evidence of Proton Coupling and an Unusual, Low-Potential Auxiliary Cluster

▸ Abstract

J Am Chem Soc 2015;137(27):8664-8667 | PubMed ID: 26088836

Grove, Ahlum, Sharma, Krebs & Booker

A consensus mechanism for Radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters.

▸ Abstract

Biochemistry 2010;49(18):3783-3785 | PubMed ID: 20377206

Yokoyama, Ohmori, Kudo & Eguchi

Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy

▸ Abstract

Bichemistry 2008;47(34):8950-8960 | PubMed ID: 18672902

family alignment: from EFDIDs 419736 419740 and 434491 -- the only sequences with the E and R conserved They share a high structural homology in the auxiliary cluster binding region between BtrN, fellow AdoMet radical dehydrogenase anSME, and molybdenum cofactor biosynthetic enzyme MoaA provides support for the establishment of an AdoMet radical structural motif that is likely common to ca 6,400 uncharacterized AdoMet radical enzymes.

Static File Downloads

File Name Description Parameters Stats
network.fam424.bs60.mek250K.xgmml One node per sequence network min bit score = 60
max edge count = 250K
size = 40K
num_edges = 45
num_nodes = 10
sfld_alignment_fam424.msa Annotated Sequence Alignment, Stockholm format 3 sequences
size: 2.3K

Total number of functional domains in this group.
Number of Functional Domains that have been manually or automatically been assigned to a family.
Number of Functional Domains that have not been assigned to a family.
Number of structures available from the PDB for members of this group.
Number of Functional Domains with 100% of Conserved Residues
Number of Functional Domains with less than 100% Conserved Residues

Active Site

Catalyzed Reaction(s)

2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent)

+ + + +
2-deoxy-scyllo-inosamine(1+)
65003
S-adenosyl-L-methionine zwitterion
59789
3-ammonio-2,3-dideoxy-scyllo-inosose(1+)
65002
5'-deoxyadenosine
17319
L-methionine zwitterion
57844
hydron
15378

EC: 1.1.99.38 | IntEnz: 1.1.99.38 | Kegg: 1.1.99.38 | BioCyc: 1.1.99.38 | BRENDA: 1.1.99.38