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)

  ⌊ FunctionalDomain Chain A, Crystal Structure Of Btrn In Complex With Adomet And 2-doia (ID 2058265)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code ISS
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus circulans Taxon ID: 1397 550544986 URP

Uniprot

Protein NameAccessionEC Number Identifier
S-adenosyl-L-methionine-dependent 2-deoxy-scyllo-inosamine dehydrogenase Q8G907 1.1.99.38 BTRN_BACCI (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 270 | Length of Functional Domain: 250

1       10        20        30        40        50        60

MGSSHHHHHHSSGLVPRGSHMDKLFSMIEVEVNSQCNRTCWYCPNSVSKRKETGEMDPAL
YKTLMEQLSSLDFAGRISFHFYGEPLLCKNLDLFVGMTTEYIPRARPIIYTNGDFLTEKR
LQTLTELGIQKFIVTQHAGAKHKFRGVYDQLAGADKEKVVYLDHSDLVLSNRGGILDNIP
QASKANMSCMVPSNLAVVTVLGNVLPCFEDFNQKMVMGNIGEQHISDIWHNDKFTSFRKM
LKEGHRGKSDLCKNCNNVSVQTEEQYDYVL
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
36 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
40 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
43 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 7/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
36 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
40 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
43 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
189 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IEA
207 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IEA
252 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IEA
255 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IEA
Family CAR This EFD conserves 9/9 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
36 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ICS PubMed:24048029
40 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ICS PubMed:24048029
43 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ICS PubMed:24048029
172 Arg (R) side chain General acid/base proton relay -- reactant ICS PubMed:24048029
189 Cys (C) side chain SPASM Domain [Fe4S4] cluster binding metal ligand -- binding ICS PubMed:24048029
207 Cys (C) side chain SPASM Domain [Fe4S4] cluster binding metal ligand -- binding ICS PubMed:24048029
209 Glu (E) side chain Activates R152
Notes: CFM numbering 		activation -- spectator ICS PubMed:24048029
252 Cys (C) side chain SPASM Domain [Fe4S4] cluster binding metal ligand -- binding ICS PubMed:24048029
255 Cys (C) side chain SPASM Domain [Fe4S4] cluster binding metal ligand -- binding ICS PubMed:24048029

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
4M7T Crystal Structure Of Btrn In Complex With Adomet And 2-Doia Btrn 3 1.56 Iron/Sulfur Cluster
(3 more ⇓) 		CSA • PDB • PDBSum
4M7S Crystal Structure Of Semet Btrn In An Open Conformation Btrn 3 2.02 Selenomethionine
(3 more ⇓) 		CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Oct. 16, 2014, 4:58 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
Oct. 15, 2016, 4:54 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update family assignment evidence code IEA ISS
update name 2-deoxy-scyllo-inosamine dehydrogenase (BtrN) Chain A, Crystal Structure Of Btrn In Complex With Adomet And 2-doia
update domain start position 20 21
update subgroup SPASM/twitch domain containing BtrN-like SPASM domain containing
update superfamily assignment evidence code IEA ISS
EC number assigned by UniProtKB accession ID.