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 thurincin H (ThnB-like)

  ⌊ FunctionalDomain thurincin H (ThnB) (ID 412081)

Superfamily Assignment Evidence Code(s) ISS PubMed:21786372
Family Assignment Evidence Code CFM PubMed:21786372
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus thuringiensis Taxon ID: 1428 262358192 ACY56718.1 (Genbank) URP
Bacillus cereus AH1134 Taxon ID: 405533 206731956 EDZ49156.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a D0QZJ5 D0QZJ5_BACTU (TrEMBL)
n/a B5UXQ7 B5UXQ7_BACCE (TrEMBL)

Sequence

Length of Enzyme (full-length): 459 | Length of Functional Domain: 459

1       10        20        30        40        50        60

MNGYLFWKEKLEIRKFTSNYESMLVVHKNPNESAPTLKNENTFTINKTATEIIELIDGTK
TYGQVVSFLSLKYSEDPISIEKKLNAFLNNVSKVYNMNIGTQEEPINVPVNLIEEQTIYP
KVASIEITNRCNVRCRHCYGDFGAVKPKVMSLDQIKSLLDDLNNIGVKLIELTGGDITVH
PNLKEILLYALNLDFSQITLLTNGIALSDKVMDIIIKNKSKTFVQIDMHSLDDNYLTWFF
KVPNTLHKIKNNIMKLAENDVRLRIATIVTHLNVHEVEDIAEWVHNLGIDSIGVSPVIPM
GRALGCSDLYLNEEDVKTYGEALLKINKKYPKFVSLYEGARAEIRNCGAITSHIVIAPDG
EIKMCTMHSLDDLKNSIGNVFEQNIKDIYDEKFKYINAFFNLQAPQMDSEECKECENKRF
CSTCFLRSFIKAQEIGDKCKWFKNHVPEIIKEPLMVGQN
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
131 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
135 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
138 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
131 Cys (C) side chain [4Fe-4S]-AdoMet binding residue cofactor binding -- binding ISS
135 Cys (C) side chain [4Fe-4S]-AdoMet binding residue cofactor binding -- binding ISS
138 Cys (C) side chain [4Fe-4S]-AdoMet binding residue cofactor binding -- binding ISS
412 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
415 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
421 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
131 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
135 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
138 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
412 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
415 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
421 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
424 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS

Catalyzed Reactions

thioether cross-link between Cys and Ser

+ + + +
cysteine residue
32460		 L-serine residue
29999		 S-adenosyl-L-methionine zwitterion
59789		 Cys-Ser thioether
132411		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844

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

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 Asn

+ + + +
cysteine residue
32460		 L-asparagine residue
50347		 S-adenosyl-L-methionine zwitterion
59789		 Cys-Asn thioether
132414		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844

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

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:01 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 344 459
update domain start position 124 1
July 15, 2014, 6:04 a.m. update curation agent setDomainBoundaries.py holliday
Oct. 16, 2014, 6:24 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.