Identification
Name:Pyruvate formate-lyase 1-activating enzyme
Synonyms:
  • Formate-C-acetyltransferase-activating enzyme 1
  • PFL-activating enzyme 1
Gene Name:pflA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB000052-Ketobutyric acidMetaboCard
ECMDB211745'-DeoxyadenosineMetaboCard
ECMDB01206Acetyl-CoAMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB00142Formic acidMetaboCard
ECMDB00696L-MethionineMetaboCard
ECMDB01275Propionyl-CoAMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB01185S-AdenosylmethionineMetaboCard
GO Classification:
Function
4 iron, 4 sulfur cluster binding
binding
catalytic activity
iron-sulfur cluster binding
metal cluster binding
oxidoreductase activity
[formate-C-acetyltransferase]-activating enzyme activity
Process
cellular metabolic process
metabolic process
oxidation reduction
oxygen and reactive oxygen species metabolic process
Gene Properties
Blattner:b0902
Gene OrientationCounterclockwise
Centisome Percentage:20.47
Left Sequence End949563
Right Sequence End950303
Gene Sequence:
>741 bp
ATGTCAGTTATTGGTCGCATTCACTCCTTTGAATCCTGTGGAACCGTAGACGGCCCAGGT
ATTCGCTTTATCACCTTTTTCCAGGGCTGCCTGATGCGCTGCCTGTATTGTCATAACCGC
GACACCTGGGACACGCATGGCGGTAAAGAAGTTACCGTTGAAGATTTGATGAAGGAAGTG
GTGACCTATCGCCACTTTATGAACGCTTCCGGCGGCGGCGTTACCGCATCCGGCGGTGAA
GCAATCCTGCAAGCTGAGTTTGTTCGTGACTGGTTCCGCGCCTGCAAAAAAGAAGGCATT
CATACCTGTCTGGACACCAACGGTTTTGTTCGTCGTTACGATCCGGTGATTGATGAACTG
CTGGAAGTAACCGACCTGGTAATGCTCGATCTCAAACAGATGAACGACGAGATCCACCAA
AATCTGGTTGGAGTTTCCAACCACCGCACGCTGGAGTTCGCTAAATATCTGGCGAACAAA
AATGTGAAGGTGTGGATCCGCTACGTTGTTGTCCCAGGCTGGTCTGACGATGACGATTCA
GCGCATCGCCTCGGTGAATTTACCCGTGATATGGGCAACGTTGAGAAAATCGAGCTTCTC
CCCTACCACGAGCTGGGCAAACACAAATGGGTGGCAATGGGTGAAGAGTACAAACTCGAC
GGTGTTAAACCACCGAAGAAAGAGACCATGGAACGCGTGAAAGGCATTCTTGAGCAGTAC
GGTCATAAGGTAATGTTCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:246
Protein Molecular Weight:28204
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Pyruvate formate-lyase 1-activating enzyme
MSVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTVEDLMKEV
VTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDEL
LEVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAKYLANKNVKVWIRYVVVPGWSDDDDS
AHRLGEFTRDMGNVEKIELLPYHELGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQY
GHKVMF
References
External Links:
ResourceLink
Uniprot ID:P0A9N4
Uniprot Name:PFLA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062478
Ecogene ID:EG10028
Ecocyc:EG10028
ColiBase:b0902
Kegg Gene:b0902
EchoBASE ID:EB0027
CCDB:PFLA_ECOLI
BacMap:16128869
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Rodel, W., Plaga, W., Frank, R., Knappe, J. (1988). "Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences." Eur J Biochem 177:153-158. Pubmed: 3053170