Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup organic radical-activating enzymes

  ⌊ FunctionalDomain uncharacterized Organic radical-activating enzymes subgroup sequence (ID 440867)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Taxon ID: 543 490998335 WP_004860059.1 (RefSeq)
Raoultella ornithinolytica Taxon ID: 54291 763450901 KIZ43645.1 (Genbank) URP
Escherichia coli 2-156-04_S1_C2 Taxon ID: 1444067 651841052 KDX15229.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A181XTA3 A0A181XTA3_KLEOX (TrEMBL)

Sequence

Length of Enzyme (full-length): 246 | Length of Functional Domain: 245

1       10        20        30        40        50        60

MSTIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGTEVTVESLMKEV
VTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACRKEGIHTCLDTNGFVRRYDPVIDEL
LEVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFARYLSNKNIKVWIRYVVVPGWSDDDDS
AHRLGEFTRDMGNVEKIELLPYHELGKHKWVAMGEEYKLDGVHPPKKETMDRVKGILEQY
GHKVMY
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
30 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
34 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
37 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
30 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
34 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
37 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3C8F 4Fe-4S-Pyruvate Formate-Lyase Activating Enzyme With Partially Disordered Adomet Pyruvate Formate-Lyase 1-Activating Enzyme 148 2.25 Iron/Sulfur Cluster
(2 more ⇓) 		CSA • PDB • PDBSum
3CB8 4Fe-4S-Pyruvate Formate-Lyase Activating Enzyme In Complex With Adomet And A Peptide Substrate Pyruvate Formate-Lyase 1-Activating Enzyme • Peptide Substrate Vsgyav 148 2.77 Sodium Ion
(3 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, 7:21 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.