CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006265
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 S-formylglutathione hydrolase YeiG 
Protein Synonyms/Alias
 FGH 
Gene Name
 yeiG 
Gene Synonyms/Alias
 b2154; JW2141 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
87DTSPRGEKVANDDGYacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids. 
Sequence Annotation
 ACT_SITE 145 145 Charge relay system (Probable).
 ACT_SITE 223 223 Charge relay system (Probable).
 ACT_SITE 256 256 Charge relay system (Probable).  
Keyword
 Complete proteome; Hydrolase; Reference proteome; Serine esterase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 278 AA 
Protein Sequence
MEMLEEHRCF EGWQQRWRHD SSTLNCPMTF SIFLPPPRDH TPPPVLYWLS GLTCNDENFT 60
TKAGAQRVAA ELGIVLVMPD TSPRGEKVAN DDGYDLGQGA GFYLNATQPP WATHYRMYDY 120
LRDELPALVQ SQFNVSDRCA ISGHSMGGHG ALIMALKNPG KYTSVSAFAP IVNPCSVPWG 180
IKAFSSYLGE DKNAWLEWDS CALMYASNAQ DAIPTLIDQG DNDQFLADQL QPAVLAEAAR 240
QKAWPMTLRI QPGYDHSYYF IASFIEDHLR FHAQYLLK 278 
Gene Ontology
 GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
 GO:0004416; F:hydroxyacylglutathione hydrolase activity; IDA:EcoCyc.
 GO:0018738; F:S-formylglutathione hydrolase activity; IDA:EcoCyc.
 GO:0046294; P:formaldehyde catabolic process; IMP:EcoCyc. 
Interpro
 IPR000801; Esterase_put.
 IPR014186; S-formylglutathione_hydrol. 
Pfam
 PF00756; Esterase 
SMART
  
PROSITE
  
PRINTS