Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup BATS domain containing

  ⌊ biotin synthase like

     ⌊ Family biotin synthase

  ⌊ FunctionalDomain biotin synthase-like protein (ID 378889)

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
Escherichia fergusonii Taxon ID: 564 446852819 WP_000930075.1 (RefSeq) URP
Escherichia fergusonii ECD227 Taxon ID: 981367 325498054 EGC95913.1 (Genbank) URP
Escherichia fergusonii ATCC 35469 Taxon ID: 585054 254810685 URP
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Uniprot

Protein NameAccessionEC Number Identifier
Biotin synthase {ECO:0000255|HAMAP-Rule:MF_01694} B7LJY8 BIOB_ESCF3 (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

MAHHPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYC
PQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGV
KAMGLEACMTLGTLSESQAQRLADAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKV
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 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
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
53 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Relates to Cys53 in the PDB file 1R30 		cofactor binding -- binding IDA PubMed:21370834
57 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Relates to Cys57 in the PDB file 1R30 		cofactor binding -- binding IDA PubMed:21370834
60 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Relates to Cys60 in the PDB file 1R30 		cofactor binding -- binding IDA PubMed:21370834
97 Cys (C) side chain Binds [2Fe-2S] cluster
Notes: Relates to Cys97 in the PDB file 1R30 		substrate binding -- binding IDA PubMed:21370834
128 Cys (C) side chain Binds [2Fe-2S] cluster
Notes: Relates to Cys128 in the PDB file 1R30 		substrate binding -- binding IDA PubMed:21370834
188 Cys (C) side chain Binds [2Fe-2S] cluster
Notes: Relates to Cys188 in the PDB file 1R30 		substrate binding -- binding IDA PubMed:21370834
260 Arg (R) side chain Binds [2Fe-2S] cluster, Modifies RedOx potential
Notes: Relates to Arg260 in the PDB file 1R30 		activation -- spectator IDA PubMed:21370834

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
May 14, 2014, 3:28 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 320 323
May 11, 2015, 11:26 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update name Biotin Synthase biotin synthase-like protein
Dec. 17, 2015, 4:58 a.m. update curation agent setDomainBoundaries.py holliday
update subgroup BATS domain containing biotin synthase like
Jan. 18, 2016, 4:49 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.