Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup organic radical-activating enzymes

  ⌊ FunctionalDomain uncharacterized Organic radical-activating enzymes subgroup sequence (ID 440866)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Klebsiella oxytoca Taxon ID: 571 838860099 KLY41994.1 (Genbank) URP
Klebsiella oxytoca MGH 27 Taxon ID: 1328428 583722643 EWF84604.1 (Genbank) URP
Klebsiella oxytoca MGH 41 Taxon ID: 1328430 583709331 EWF71438.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A181X4D2 A0A181X4D2_KLEOX (TrEMBL)
n/a H3N9P3 H3N9P3_9ENTR (TrEMBL)

Sequence

Length of Enzyme (full-length): 276 | Length of Functional Domain: 245

1       10        20        30        40        50        60

MDNSQNRLDIAFELCIYIGPGWAKFGDITAMSTIGRIHSFESCGTVDGPGIRFITFFQGC
LMRCLYCHNRDTWDTHGGKEITVEELMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRD
WFRACKKEGIHTCLDTNGFVRRYDPVIDELLEVTDLVMLDLKQMNDEIHQNLVGVSNHRT
LEFARYLSNKNINVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELGKHKW
VAMGEEYKLDGVHPPKKETMERVKGILEQYGHKVMY
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
60 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
64 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
67 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
60 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
64 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
67 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.