Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup organic radical-activating enzymes

  ⌊ activating enzymes, group 2

     ⌊ Family glycerol dehydratase activase

  ⌊ FunctionalDomain Glycerol dehydratase activator (ID 386005)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:12704244
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Clostridium butyricum Taxon ID: 1492 696618667 WP_033127376.1 (RefSeq) URP
n/a 756817882 AJN03386.1 (Genbank)
n/a 430158359 AGA39521.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
n/a Q8GEZ7 Q8GEZ7_CLOBU (TrEMBL)

Sequence

Length of Enzyme (full-length): 304 | Length of Functional Domain: 304

1       10        20        30        40        50        60

MSKEIKGVLFNIQKFSLHDGPGIRTIVFFKGCSMSCLWCSNPESQDIKPQVMFNKNLCTK
CGRCKSQCKSAAIDMNSEYRIDKSKCTECTKCVDNCLSGALVIEGRNYSVEDVIKELKKD
SVQYRRSNGGITLSGGEVLLQPDFAVELLKECKSYGWHTAIETAMYVNSESVKKVIPYID
LAMIDIKSMNDEIHRKFTGVSNEIILQNIKLSDELAKEIIIRIPVIEGFNADLQSIGAIA
QFSKSLTNLKRIDLLPYHNYGENKYQAIGREYSLKELKSPSKDKMERLKALVEIMGIPCT
IGAE
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
32 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
39 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
32 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
39 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
32 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
39 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

Catalyzed Reaction

[glycerol dehydratase]-activating enzyme

+ + + + +
glycerol dehydratase (inactive)
1r8w		 S-adenosyl-L-methioninate
67040		 1,5-dihydroflavin
62787		 glycerol dehydratase (active)
1r8w		 L-methionine zwitterion
57844		 5'-deoxyadenosine
17319		 semiquinone
15817

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

Curation History
Time Change Annotation Old Value New Value
July 15, 2014, 5:22 a.m. update family assignment evidence code CFM,ISS CFM
Oct. 16, 2014, 5:23 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.