Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup BATS domain containing

  ⌊ biotin synthase like

  ⌊ FunctionalDomain uncharacterized biotin synthase-like sequence (ID 2116273)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Shigella flexneri 1235-66 Taxon ID: 766154 391319919 EIQ76856.1 (Genbank)

Uniprot

Protein NameAccessionEC Number Identifier
n/a I6H7W4 I6H7W4_SHIFL (TrEMBL)

Sequence

Length of Enzyme (full-length): 244 | Length of Functional Domain: 244

1       10        20        30        40        50        60

MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFEPRQVQVSTLLSIKTGACPEDCKYC
PQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGV
KAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKV
RDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDA
FDFI
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
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 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 3/3 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 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

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
Oct. 16, 2014, 7:17 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
Dec. 17, 2015, 6:23 a.m. update curation agent setDomainBoundaries.py holliday
update name uncharacterized Biotin Synthase subgroup sequence uncharacterized biotin synthase-like sequence
update subgroup BATS domain containing biotin synthase like
Oct. 15, 2016, 7:16 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.