Formate acetyltransferase 1

Details

Name
Formate acetyltransferase 1
Synonyms
  • 2.3.1.54
  • pfl
  • Pyruvate formate-lyase 1
Gene Name
pflB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011242|Formate acetyltransferase 1
MSELNEKLATAWEGFTKGDWQNEVNVRDFIQKNYTPYEGDESFLAGATEATTTLWDKVME
GVKLENRTHAPVDFDTAVASTITSHDAGYINKQLEKIVGLQTEAPLKRALIPFGGIKMIE
GSCKAYNRELDPMIKKIFTEYRKTHNQGVFDVYTPDILRCRKSGVLTGLPDAYGRGRIIG
DYRRVALYGIDYLMKDKLAQFTSLQADLENGVNLEQTIRLREEIAEQHRALGQMKEMAAK
YGYDISGPATNAQEAIQWTYFGYLAAVKSQNGAAMSFGRTSTFLDVYIERDLKAGKITEQ
EAQEMVDHLVMKLRMVRFLRTPEYDELFSGDPIWATESIGGMGLDGRTLVTKNSFRFLNT
LYTMGPSPEPNMTILWSEKLPLNFKKFAAKVSIDTSSLQYENDDLMRPDFNNDDYAIACC
VSPMIVGKQMQFFGARANLAKTMLYAINGGVDEKLKMQVGPKSEPIKGDVLNYDEVMERM
DHFMDWLAKQYITALNIIHYMHDKYSYEASLMALHDRDVIRTMACGIAGLSVAADSLSAI
KYAKVKPIRDEDGLAIDFEIEGEYPQFGNNDPRVDDLAVDLVERFMKKIQKLHTYRDAIP
TQSVLTITSNVVYGKKTGNTPDGRRAGAPFGPGANPMHGRDQKGAVASLTSVAKLPFAYA
KDGISYTFSIVPNALGKDDEVRKTNLAGLMDGYFHHEASIEGGQHLNVNVMNREMLLDAM
ENPEKYPQLTIRVSGYAVRFNSLTKEQQQDVITRTFTQSM
Number of residues
760
Molecular Weight
85356.555
Theoretical pI
5.83
GO Classification
Functions
formate C-acetyltransferase activity
Processes
glucose metabolic process / threonine catabolic process
Components
cytosol / membrane
General Function
Formate c-acetyltransferase activity
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011243|Formate acetyltransferase 1 (pflB)
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP09373
UniProtKB Entry NamePFLB_ECOLI
GenBank Protein ID42370
GenBank Gene IDX08035
General References
  1. Rodel W, Plaga W, Frank R, Knappe J: Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences. Eur J Biochem. 1988 Oct 15;177(1):153-8. [Article]
  2. 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 al.: 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. 1996 Jun 30;3(3):137-55. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Sawers G, Bock A: Novel transcriptional control of the pyruvate formate-lyase gene: upstream regulatory sequences and multiple promoters regulate anaerobic expression. J Bacteriol. 1989 May;171(5):2485-98. [Article]
  6. Wagner AF, Frey M, Neugebauer FA, Schafer W, Knappe J: The free radical in pyruvate formate-lyase is located on glycine-734. Proc Natl Acad Sci U S A. 1992 Feb 1;89(3):996-1000. [Article]
  7. Molloy MP, Herbert BR, Walsh BJ, Tyler MI, Traini M, Sanchez JC, Hochstrasser DF, Williams KL, Gooley AA: Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis. Electrophoresis. 1998 May;19(5):837-44. [Article]
  8. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  9. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
  10. Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y: Identification of lysine succinylation as a new post-translational modification. Nat Chem Biol. 2011 Jan;7(1):58-63. doi: 10.1038/nchembio.495. Epub 2010 Dec 12. [Article]
  11. Becker A, Fritz-Wolf K, Kabsch W, Knappe J, Schultz S, Volker Wagner AF: Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase. Nat Struct Biol. 1999 Oct;6(10):969-75. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01992Coenzyme Ainvestigational, nutraceuticalunknownDetails
DB03278D-TreitolexperimentalunknownDetails
DB03940Oxamic AcidexperimentalunknownDetails