Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup BATS domain containing

  ⌊ biotin synthase like

     ⌊ Family biotin synthase

  ⌊ FunctionalDomain biotin synthase-like protein (ID 407288)

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
Citrobacter freundii Taxon ID: 546 838589155 KLV73556.1 (Genbank) URP
Citrobacter freundii Taxon ID: 546 838587223 KLV71631.1 (Genbank) URP
Citrobacter freundii UCI 32 Taxon ID: 1400137 575564364 ETX64036.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A0J1M9R6 A0A0J1M9R6_9ENTR (TrEMBL)
n/a A0A155X234 A0A155X234_ENTCL (TrEMBL)

Sequence

Length of Enzyme (full-length): 338 | Length of Functional Domain: 315

1       10        20        30        40        50        60

MSQVTELFEKPLLDLLFEAQQVHRQHFDPQQVQVSTLLSIKTGACPEDCKYCPQSSRYKT
GLETERLMEVEQVLDSARKAKQAGSTRFCMGAAWKNPHERDMPYLEQMVQGVKELGLEAC
MTLGTLDESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRSYQERLDTLDKVREAGIKVC
SGGIVGLGETVTDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDAFDFIRTIA
VARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPNEDKDLLLFRKL
GLNPQQTAVLAGDNEQQQRLEQALRTPDTDDYYNAATV
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
45 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
49 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
52 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
45 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
49 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
52 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
45 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Relates to Cys53 in the PDB file 1R30 		cofactor binding -- binding IDA PubMed:21370834
49 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Relates to Cys57 in the PDB file 1R30 		cofactor binding -- binding IDA PubMed:21370834
52 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Relates to Cys60 in the PDB file 1R30 		cofactor binding -- binding IDA PubMed:21370834
89 Cys (C) side chain Binds [2Fe-2S] cluster
Notes: Relates to Cys97 in the PDB file 1R30 		substrate binding -- binding IDA PubMed:21370834
120 Cys (C) side chain Binds [2Fe-2S] cluster
Notes: Relates to Cys128 in the PDB file 1R30 		substrate binding -- binding IDA PubMed:21370834
180 Cys (C) side chain Binds [2Fe-2S] cluster
Notes: Relates to Cys188 in the PDB file 1R30 		substrate binding -- binding IDA PubMed:21370834
252 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
Oct. 16, 2014, 6:12 a.m. update curation agent holliday setDomainBoundaries.py
May 11, 2015, 12:52 p.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update family assignment evidence code IEA ISS
update name Biotin Synthase biotin synthase-like protein
Dec. 17, 2015, 5:32 a.m. update curation agent setDomainBoundaries.py holliday
update subgroup BATS domain containing biotin synthase like
Jan. 18, 2016, 5:25 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.