Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup organic radical-activating enzymes

  ⌊ activating enzymes, group 2

     ⌊ Family pyruvate formate-lyase activase

  ⌊ FunctionalDomain Pyruvate formate-lyase-activating enzyme (ID 2048858)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli HVH 146 (4-3189767) Taxon ID: 1281079 535096531 EQS42856.1 (Genbank) URP
Escherichia coli HVH 141 (4-5995973) Taxon ID: 1281074 535062335 EQS09122.1 (Genbank) URP
Escherichia coli HVH 17 (4-7473087) Taxon ID: 1280968 534598083 EQN55938.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a I2S5H1 I2S5H1_ECOLX (TrEMBL)

Sequence

Length of Enzyme (full-length): 265 | Length of Functional Domain: 245

1       10        20        30        40        50        60

MSNLTNCNTTENTATAGAAKSVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRD
TWDTHGGKEVTVEDLMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACKKEGIH
TCLDTNGFVRRYDPVIDELLEVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAKYLANKN
VKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELGKHKWVAMGEEYKLDG
VKPPKKETMERVKGILEQYGHKVMF
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
49 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
53 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
56 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
49 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
53 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
56 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
49 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
53 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
56 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
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
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
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, 7:37 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.