Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serine hydroxymethyltransferase  

UniProtKB / Swiss-Prot ID :  GLYA_ECOLI

Gene Name (Synonyms) : 
glyA b2551, JW2535  

Species :  Escherichia coli (strain K12). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF- independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of allothreonine and 3- phenylserine. Also catalyzes the irreversible conversion of 5,10- methenyltetrahydrofolate to 5-formyltetrahydrofolate. 

Protein Sequence MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEY...
Predicted Secondary Structure CCCCCCCHHHCCHHHHHHHHHHHHHHHCCEEEEEECCCCCHHHHHHHHHHHHHHHCCCCCCCCCCCCCCH...
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
54N6-acetyllysine.QLTNKYAEG
HHHHHHCCC
40.37UniProtKB
Link
62N6-succinyllysine.GYPGKRYYG
CCCCCCCCC
32.49UniProtKB
Link
229N6-(pyridoxal phosphate)lysine.TTTHKTLAG
CCCCCHHHC
43.04UniProtKB
Link
242N6-succinyllysine.LILAKGGSE
EEECCCCHH
61.43UniProtKB
Link
250N6-acetyllysine; alternate.EELYKKLNS
HHHHHHHHH
64.51UniProtKB
Link
250N6-succinyllysine; alternate.EELYKKLNS
HHHHHHHHH
64.51UniProtKB
Link
277N6-succinyllysine.AVALKEAME
HHHHHHHHC
33.42UniProtKB
Link
285N6-acetyllysine.EPEFKTYQQ
CHHHHHHHH
44.66UniProtKB
Link
293N6-succinyllysine.QQVAKNAKA
HHHHHHHHH
59.59UniProtKB
Link
331N6-succinyllysine.NLTGKEADA
CCCHHHHHH
44.48UniProtKB
Link
346N6-succinyllysine.ITVNKNSVP
EEEECCCCC
46.38UniProtKB
Link
354N6-acetyllysine; alternate.PNDPKSPFV
CCCCCCCCC
73.88UniProtKB
Link
354N6-succinyllysine; alternate.PNDPKSPFV
CCCCCCCCC
73.88UniProtKB
Link
375N6-acetyllysine.RRGFKEAEA
CCCCCHHHH
59.86UniProtKB
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-54; LYS-250; LYS-285;LYS-354 AND LYS-375, 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-62; LYS-242; LYS-250; LYS-277; LYS-293; LYS-331;LYS-346 AND LYS-354.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures