Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup organic radical-activating enzymes

  ⌊ activating enzymes, group 2

     ⌊ Family benzylsuccinate synthase activase

  ⌊ FunctionalDomain Benzylsuccinate synthase activating enzyme (ID 409316)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:9632263
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Thauera aromatica Taxon ID: 59405 75499376
Thauera aromatica Taxon ID: 59405 17221315

Uniprot

Protein NameAccessionEC Number Identifier
Benzylsuccinate synthase activating enzyme O87941 1.97.1.- BSSD_THAAR (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 331 | Length of Functional Domain: 331

1       10        20        30        40        50        60

MKIPLITEIQRFSLQDGPGIRTTIFLKGCPLRCPWCHNPETQDARQEFYFYPDRCVGCGR
CVAVCPAETSRLVRNSDGRTIVQIDRTNCQRCMRCVAACLTEARAIVGQHMSVDEILREA
LSDSAFYRNSGGGVTISGGDPLYFPDFTRQLASELHARGVHVAIETSCFPKQGKVVESMI
GIVDLFIVDLKTLDAHKHLDVIGWPLAPILANLETLFAAGAKVRIHIPVIPGFNDSHADI
DAYAEYLGKHAAAISGIDLLNFHCYGEGKYTFLGRAGSYQYSGVDETPAEKIVPLAQALK
ARGLAVTIGGIVGIANGKNELTGDIALEVHH
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
29 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
33 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
36 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
29 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
33 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
36 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
Family CAR This EFD conserves 3/3 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
29 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
33 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
36 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

Catalyzed Reaction

[benzylsuccinate synthase]-activating enzyme

+ + + + +
benzylsuccinate synthase (inactive)
4pkf		 S-adenosyl-L-methioninate
67040		 1,5-dihydroflavin
62787		 benzylsuccinate synthase (active)
4pkf		 L-methionine zwitterion
57844		 5'-deoxyadenosine
17319		 semiquinone
15817

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

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 2:55 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 310 331
July 15, 2014, 5:59 a.m. update curation agent setDomainBoundaries.py holliday
Oct. 16, 2014, 6:16 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.