Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup SPASM/twitch domain containing

  ⌊ main SPASM domain-containing

  ⌊ thioether bond formation requiring one auxiliary iron-sulfur cluster

     ⌊ Family antilisterial bacteriocin subtilosin biosynthesis protein (AlbA-like)

  ⌊ FunctionalDomain Antilisterial bacteriocin subtilosin biosynthesis protein AlbA (ID 280039)

Superfamily Assignment Evidence Code(s) ISS PubMed:22366720
Family Assignment Evidence Code CFM PubMed:22366720
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus subtilis subsp. subtilis str. 168 Taxon ID: 224308 16080789 NP_391617.1 (RefSeq) PRP URP
Bacillus subtilis Taxon ID: 1423 489335371 WP_003242599.1 (RefSeq) URP
Bacillus subtilis KCTC 1028 Taxon ID: 1136873 807076099 AKC49305.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Antilisterial bacteriocin subtilosin biosynthesis protein AlbA P71011 ALBA_BACSU (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 448 | Length of Functional Domain: 448

1       10        20        30        40        50        60

MFIEQMFPFINESVRVHQLPEGGVLEIDYLRDNVSISDFEYLDLNKTAYELCMRMDGQKT
AEQILAEQCAVYDESPEDHKDWYYDMLNMLQNKQVIQLGNRASRHTITTSGSNEFPMPLH
ATFELTHRCNLKCAHCYLESSPEALGTVSIEQFKKTADMLFDNGVLTCEITGGEIFVHPN
ANEILDYVCKKFKKVAVLTNGTLMRKESLELLKTYKQKIIVGISLDSVNSEVHDSFRGRK
GSFAQTCKTIKLLSDHGIFVRVAMSVFEKNMWEIHDMAQKVRDLGAKAFSYNWVDDFGRG
RDIVHPTKDAEQHRKFMEYEQHVIDEFKDLIPIIPYERKRAANCGAGWKSIVISPFGEVR
PCALFPKEFSLGNIFHDSYESIFNSPLVHKLWQAQAPRFSEHCMKDKCPFSGYCGGCYLK
GLNSNKYHRKNICSWAKNEQLEDVVQLI
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
129 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
133 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
136 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
129 Cys (C) side chain [4Fe-4S]-AdoMet binding residue cofactor binding -- binding ISS
133 Cys (C) side chain [4Fe-4S]-AdoMet binding residue cofactor binding -- binding ISS
136 Cys (C) side chain [4Fe-4S]-AdoMet binding residue cofactor binding -- binding ISS
403 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
408 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
414 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 3/3 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
129 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
133 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
136 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

Catalyzed Reactions

thioether cross-link between Cys and Thr

+ + + +
cysteine residue
32460		 L-threonine residue
30013		 S-adenosyl-L-methionine zwitterion
59789		 Cys-Thr thioether
132254		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

thioether cross-link between Cys and Phe

+ + + +
cysteine residue
32460		 phenylalanine residue
32503		 S-adenosyl-L-methionine zwitterion
59789		 Cys-Phe thioether
132409		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

Curation History
Time Change Annotation Old Value New Value
Oct. 16, 2014, 3:53 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.