Identification
Name:Formate acetyltransferase 1
Synonyms:
  • Pyruvate formate-lyase 1
Gene Name:pflB
Enzyme Class:
Biological Properties
General Function:Involved in formate C-acetyltransferase activity
Specific Function:Acetyl-CoA + formate = CoA + pyruvate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
SMPDB Reactions:
Thumb+ThumbThumb+Propionyl-CoA+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB000052-Ketobutyric acidMetaboCard
ECMDB01206Acetyl-CoAMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB00142Formic acidMetaboCard
ECMDB01275Propionyl-CoAMetaboCard
ECMDB00243Pyruvic acidMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
acetyltransferase activity
acyltransferase activity
C-acetyltransferase activity
catalytic activity
formate C-acetyltransferase activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
Process
alcohol metabolic process
carbohydrate metabolic process
glucose metabolic process
hexose metabolic process
metabolic process
monosaccharide metabolic process
primary metabolic process
small molecule metabolic process
Gene Properties
Blattner:b0903
Gene OrientationCounterclockwise
Centisome Percentage:20.49
Left Sequence End950495
Right Sequence End952777
Gene Sequence:
>2283 bp
ATGTCCGAGCTTAATGAAAAGTTAGCCACAGCCTGGGAAGGTTTTACCAAAGGTGACTGG
CAGAATGAAGTAAACGTCCGTGACTTCATTCAGAAAAACTACACTCCGTACGAGGGTGAC
GAGTCCTTCCTGGCTGGCGCTACTGAAGCGACCACCACCCTGTGGGACAAAGTAATGGAA
GGCGTTAAACTGGAAAACCGCACTCACGCGCCAGTTGACTTTGACACCGCTGTTGCTTCC
ACCATCACCTCTCACGACGCTGGCTACATCAACAAGCAGCTTGAGAAAATCGTTGGTCTG
CAGACTGAAGCTCCGCTGAAACGTGCTCTTATCCCGTTCGGTGGTATCAAAATGATCGAA
GGTTCCTGCAAAGCGTACAACCGCGAACTGGATCCGATGATCAAAAAAATCTTCACTGAA
TACCGTAAAACTCACAACCAGGGCGTGTTCGACGTTTACACTCCGGACATCCTGCGTTGC
CGTAAATCTGGTGTTCTGACCGGTCTGCCAGATGCATATGGCCGTGGCCGTATCATCGGT
GACTACCGTCGCGTTGCGCTGTACGGTATCGACTACCTGATGAAAGACAAACTGGCACAG
TTCACTTCTCTGCAGGCTGATCTGGAAAACGGCGTAAACCTGGAACAGACTATCCGTCTG
CGCGAAGAAATCGCTGAACAGCACCGCGCTCTGGGTCAGATGAAAGAAATGGCTGCGAAA
TACGGCTACGACATCTCTGGTCCGGCTACCAACGCTCAGGAAGCTATCCAGTGGACTTAC
TTCGGCTACCTGGCTGCTGTTAAGTCTCAGAACGGTGCTGCAATGTCCTTCGGTCGTACC
TCCACCTTCCTGGATGTGTACATCGAACGTGACCTGAAAGCTGGCAAGATCACCGAACAA
GAAGCGCAGGAAATGGTTGACCACCTGGTCATGAAACTGCGTATGGTTCGCTTCCTGCGT
ACTCCGGAATACGATGAACTGTTCTCTGGCGACCCGATCTGGGCAACCGAATCTATCGGT
GGTATGGGCCTCGACGGTCGTACCCTGGTTACCAAAAACAGCTTCCGTTTCCTGAACACC
CTGTACACCATGGGTCCGTCTCCGGAACCGAACATGACCATTCTGTGGTCTGAAAAACTG
CCGCTGAACTTCAAGAAATTCGCCGCTAAAGTGTCCATCGACACCTCTTCTCTGCAGTAT
GAGAACGATGACCTGATGCGTCCGGACTTCAACAACGATGACTACGCTATTGCTTGCTGC
GTAAGCCCGATGATCGTTGGTAAACAAATGCAGTTCTTCGGTGCGCGTGCAAACCTGGCG
AAAACCATGCTGTACGCAATCAACGGCGGCGTTGACGAAAAACTGAAAATGCAGGTTGGT
CCGAAGTCTGAACCGATCAAAGGCGATGTCCTGAACTATGATGAAGTGATGGAGCGCATG
GATCACTTCATGGACTGGCTGGCTAAACAGTACATCACTGCACTGAACATCATCCACTAC
ATGCACGACAAGTACAGCTACGAAGCCTCTCTGATGGCGCTGCACGACCGTGACGTTATC
CGCACCATGGCGTGTGGTATCGCTGGTCTGTCCGTTGCTGCTGACTCCCTGTCTGCAATC
AAATATGCGAAAGTTAAACCGATTCGTGACGAAGACGGTCTGGCTATCGACTTCGAAATC
GAAGGCGAATACCCGCAGTTTGGTAACAATGATCCGCGTGTAGATGACCTGGCTGTTGAC
CTGGTAGAACGTTTCATGAAGAAAATTCAGAAACTGCACACCTACCGTGACGCTATCCCG
ACTCAGTCTGTTCTGACCATCACTTCTAACGTTGTGTATGGTAAGAAAACGGGTAACACC
CCAGACGGTCGTCGTGCTGGCGCGCCGTTCGGACCGGGTGCTAACCCGATGCACGGTCGT
GACCAGAAAGGTGCAGTAGCCTCTCTGACTTCCGTTGCTAAACTGCCGTTTGCTTACGCT
AAAGATGGTATCTCCTACACCTTCTCTATCGTTCCGAACGCACTGGGTAAAGACGACGAA
GTTCGTAAGACCAACCTGGCTGGTCTGATGGATGGTTACTTCCACCACGAAGCATCCATC
GAAGGTGGTCAGCACCTGAACGTTAACGTGATGAACCGTGAAATGCTGCTCGACGCGATG
GAAAACCCGGAAAAATATCCGCAGCTGACCATCCGTGTATCTGGCTACGCAGTACGTTTC
AACTCGCTGACTAAAGAACAGCAGCAGGACGTTATTACTCGTACCTTCACTCAATCTATG
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:760
Protein Molecular Weight:85357
Protein Theoretical pI:6
PDB File:1MZO
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Formate acetyltransferase 1
MSELNEKLATAWEGFTKGDWQNEVNVRDFIQKNYTPYEGDESFLAGATEATTTLWDKVME
GVKLENRTHAPVDFDTAVASTITSHDAGYINKQLEKIVGLQTEAPLKRALIPFGGIKMIE
GSCKAYNRELDPMIKKIFTEYRKTHNQGVFDVYTPDILRCRKSGVLTGLPDAYGRGRIIG
DYRRVALYGIDYLMKDKLAQFTSLQADLENGVNLEQTIRLREEIAEQHRALGQMKEMAAK
YGYDISGPATNAQEAIQWTYFGYLAAVKSQNGAAMSFGRTSTFLDVYIERDLKAGKITEQ
EAQEMVDHLVMKLRMVRFLRTPEYDELFSGDPIWATESIGGMGLDGRTLVTKNSFRFLNT
LYTMGPSPEPNMTILWSEKLPLNFKKFAAKVSIDTSSLQYENDDLMRPDFNNDDYAIACC
VSPMIVGKQMQFFGARANLAKTMLYAINGGVDEKLKMQVGPKSEPIKGDVLNYDEVMERM
DHFMDWLAKQYITALNIIHYMHDKYSYEASLMALHDRDVIRTMACGIAGLSVAADSLSAI
KYAKVKPIRDEDGLAIDFEIEGEYPQFGNNDPRVDDLAVDLVERFMKKIQKLHTYRDAIP
TQSVLTITSNVVYGKKTGNTPDGRRAGAPFGPGANPMHGRDQKGAVASLTSVAKLPFAYA
KDGISYTFSIVPNALGKDDEVRKTNLAGLMDGYFHHEASIEGGQHLNVNVMNREMLLDAM
ENPEKYPQLTIRVSGYAVRFNSLTKEQQQDVITRTFTQSM
References
External Links:
ResourceLink
Uniprot ID:P09373
Uniprot Name:PFLB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651427
PDB ID:1MZO
Ecogene ID:EG10701
Ecocyc:EG10701
ColiBase:b0903
Kegg Gene:b0903
EchoBASE ID:EB0695
CCDB:PFLB_ECOLI
BacMap:16128870
General Reference:
  • Becker, A., Fritz-Wolf, K., Kabsch, W., Knappe, J., Schultz, S., Volker Wagner, A. F. (1999). "Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase." Nat Struct Biol 6:969-975. Pubmed: 10504733
  • 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
  • Molloy, M. P., Herbert, B. R., Walsh, B. J., Tyler, M. I., Traini, M., Sanchez, J. C., Hochstrasser, D. F., Williams, K. L., Gooley, A. A. (1998). "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis." Electrophoresis 19:837-844. Pubmed: 9629924
  • 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
  • Sawers, G., Bock, A. (1989). "Novel transcriptional control of the pyruvate formate-lyase gene: upstream regulatory sequences and multiple promoters regulate anaerobic expression." J Bacteriol 171:2485-2498. Pubmed: 2651404
  • Wagner, A. F., Frey, M., Neugebauer, F. A., Schafer, W., Knappe, J. (1992). "The free radical in pyruvate formate-lyase is located on glycine-734." Proc Natl Acad Sci U S A 89:996-1000. Pubmed: 1310545
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842