Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup BATS domain containing

  ⌊ biotin synthase like

  ⌊ FunctionalDomain uncharacterized biotin synthase-like sequence (ID 2185632)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onJan. 14, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli Taxon ID: 562 487392364 WP_001663529.1 (RefSeq) URP
Escherichia coli p0305293.12 Taxon ID: 1116100 477378239 ENG46161.1 (Genbank) URP

Sequence

Length of Enzyme (full-length): 346 | Length of Functional Domain: 323

1       10        20        30        40        50        60

MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQGQVSTLLSIKTGACPEDCKYF
PQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGV
KAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKV
RDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDA
FDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDK
DLQLFRKLGLNPQQTAVLAGDNEQQQRLEQALMTPDTDEYYNAAAL
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 2/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
53 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
57 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
60 Phe (F) side chain MISMATCH: This residue does not match the specified amino acid type of C, and thus may not function in the same manner as other sequences in the superfamily
Subgroup CAR This EFD conserves 2/3 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
53 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
57 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
60 Phe (F) side chain MISMATCH: This residue does not match the specified amino acid type of C, and thus may not function in the same manner as other sequences in the subgroup

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1R30 The Crystal Structure Of Biotin Synthase, An S-Adenosylmethionine-Dependent Radical Enzyme Biotin Synthase 137 3.4 S-Adenosylmethionine
(4 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
July 5, 2014, 5:22 p.m. remove classification public -
remove curation agent updateSuperfamily.py -
remove domain end position 323 -
remove name uncharacterized Radical SAM superfamily sequence -
remove domain start position 1 -
remove superfamily assignment evidence code IEA -
create classification - public
create curation agent - holliday
create domain end position - 323
create name - uncharacterized Radical SAM superfamily sequence
create domain start position - 1
create superfamily assignment evidence code - IEA
Dec. 17, 2015, 4:34 a.m. update name uncharacterized Radical SAM superfamily sequence uncharacterized biotin synthase-like sequence
EC number assigned by UniProtKB accession ID.