A0A0H3BZ80 · A0A0H3BZ80_STRPZ

Function

function

Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Function[formate-C-acetyltransferase]-activating enzyme activity
Molecular Functionlyase activity
Molecular Functionmetal ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyruvate formate-lyase-activating enzyme
  • EC number

Gene names

    • Name
      pflC
    • Ordered locus names
      Spy49_0312

Organism names

Accessions

  • Primary accession
    A0A0H3BZ80

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain46-275Radical SAM core

Sequence similarities

Belongs to the organic radical-activating enzymes family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    287
  • Mass (Da)
    33,125
  • Last updated
    2015-09-16 v1
  • Checksum
    E6425425E0603EE6
MPSLFDEKCYNENVKTFTSNEGDAMTEKDYGQVTGMVHSTESFGSVDGPGIRFIIFLQGCKLRCQYCHNPDTWEMETNNSKIRTVNDVLKEALQYKHFWGKKGGITVSGGEAMLQIDFITALFIEAKKLGIHTTLDTCGFTYRPTPEYHQVLDNLLAVTDLILLDLKEIDEKQHKIVTRQPNKNILQFARYLSDKQIPVWIRHVLVPGLTDIDDHLTRLGEFVKTLKNVDKFEVLPYHTMGEFKWRELGIPYQLEGVKPPTKERVQNAKNLMQTESYTEYMNRIHQS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000829
EMBL· GenBank· DDBJ
ACI60650.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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