Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Formate acetyltransferase 1  

UniProtKB / Swiss-Prot ID :  PFLB_ECOLI

Gene Name (Synonyms) : 
pflB, pfl b0903, JW0886  

Species :  Escherichia coli (strain K12). 

Subcellular Localization :  Cytoplasm. 

Protein Function :   

Protein Sequence MSELNEKLATAWEGFTKGDWQNEVNVRDFIQKNYTPYEGDESFLAGATEATTTLWDKVMEGVKLENRTHA...
Predicted Secondary Structure CCCHHHHHHHHHHHHCCCCCCCCCCHHHHHHHCCCCCCCCHHHHCCCCHHHHHHHHHHHHHHHHHHHHCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
63N6-acetyllysine; alternate.MEGVKLENR
HHHHHHHHH
62.02UniProtKB
Link
63N6-succinyllysine; alternate.MEGVKLENR
HHHHHHHHH
62.02UniProtKB
Link
107N6-succinyllysine.EAPLKRALI
CHHHHHHCC
34.27UniProtKB
Link
117N6-acetyllysine; alternate.FGGIKMIEG
CCHHHHHHH
36.78UniProtKB
Link
117N6-succinyllysine; alternate.FGGIKMIEG
CCHHHHHHH
36.78UniProtKB
Link
123S-nitrosocysteineIEGSCKAYN
HHHHHHHCC
4.26dbSNO
Link
124N6-acetyllysine; alternate.EGSCKAYNR
HHHHHHCCC
56.45UniProtKB
Link
124N6-succinyllysine; alternate.EGSCKAYNR
HHHHHHCCC
56.45UniProtKB
Link
195N6-acetyllysine; alternate.DYLMKDKLA
HHHHHHHHH
49.46UniProtKB
Link
195N6-succinyllysine; alternate.DYLMKDKLA
HHHHHHHHH
49.46UniProtKB
Link
454N6-acetyllysine; alternate.GVDEKLKMQ
CCCHHCCCE
49.28UniProtKB
Link
454N6-succinyllysine; alternate.GVDEKLKMQ
CCCHHCCCE
49.28UniProtKB
Link
467N6-succinyllysine.SEPIKGDVL
CCCCCCCCC
60.83UniProtKB
Link
541N6-acetyllysine.LSAIKYAKV
HHHHHHHHH
38.58UniProtKB
Link
591N6-acetyllysine.KKIQKLHTY
HHHHHCCCC
45.79UniProtKB
Link
654N6-succinyllysine.TSVAKLPFA
HHHHCCCHH
55.31UniProtKB
Link
735Glycine radical.IRVSGYAVR
EEEEEEEEE
16.15UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation is a highly abundant and evolutionarily conservedmodification in Escherichia coli.";
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,Grishin N.V., Zhao Y.;
Mol. Cell. Proteomics 8:215-225(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-117; LYS-195;LYS-454; LYS-541 AND LYS-591, AND MASS SPECTROMETRY.
N6-succinyllysine
ReferencePubMed
"Identification of lysine succinylation as a new post-translationalmodification.";
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
Nat. Chem. Biol. 7:58-63(2011).
Cited for: SUCCINYLATION AT LYS-63; LYS-107; LYS-117; LYS-124; LYS-195; LYS-454;LYS-467 AND LYS-654.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures