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Protein

S-formylglutathione hydrolase YeiG

Gene

yeiG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

S-formylglutathione + H2O = glutathione + formate.1 Publication

Enzyme regulationi

Inhibited by the sulfhydryl inhibitors (N-ethylmaleimide, iodoacetate, ZnCl2 and CuCl2).1 Publication

Kineticsi

  1. KM=0.43 mM for S-formylglutathione1 Publication
  2. KM=1.03 mM for alpha-naphthyl acetate1 Publication
  3. KM=0.45 mM for pNP-acetate1 Publication
  4. KM=0.70 mM for pNP-butyrate1 Publication
  5. KM=0.95 mM for pNP-caproate1 Publication
  6. KM=0.48 mM for pNP-propionate1 Publication
  7. KM=0.58 mM for S-lactoylglutathione1 Publication
  1. Vmax=12.6 µmol/min/mg enzyme with S-formylglutathione as substrate1 Publication
  2. Vmax=9.79 µmol/min/mg enzyme with alpha-naphthyl acetate as substrate1 Publication
  3. Vmax=0.50 µmol/min/mg enzyme with pNP-acetate as substrate1 Publication
  4. Vmax=0.70 µmol/min/mg enzyme with pNP-butyrate as substrate1 Publication
  5. Vmax=0.64 µmol/min/mg enzyme with pNP-caproate as substrate1 Publication
  6. Vmax=0.71 µmol/min/mg enzyme with pNP-propionate as substrate1 Publication
  7. Vmax=1.97 µmol/min/mg enzyme with S-lactoylglutathione as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei145Charge relay systemCurated1
Active sitei223Charge relay systemCurated1
Active sitei256Charge relay systemCurated1

GO - Molecular functioni

  • carboxylic ester hydrolase activity Source: UniProtKB-KW
  • hydroxyacylglutathione hydrolase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • S-formylglutathione hydrolase activity Source: EcoCyc

GO - Biological processi

  • formaldehyde catabolic process Source: EcoCyc
  • protein homotetramerization Source: EcoCyc

Keywordsi

Molecular functionHydrolase, Serine esterase

Enzyme and pathway databases

BioCyciEcoCyc:EG12026-MONOMER
MetaCyc:EG12026-MONOMER
BRENDAi3.1.2.2 2026
SABIO-RKP33018

Protein family/group databases

ESTHERiecoli-yeiG A85-EsteraseD-FGH

Names & Taxonomyi

Protein namesi
Recommended name:
S-formylglutathione hydrolase YeiG (EC:3.1.2.12)
Short name:
FGH
Gene namesi
Name:yeiG
Ordered Locus Names:b2154, JW2141
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12026 yeiG

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26C → A: Reduces catalytic efficiency, but has no effect on affinity for substrate. 1 Publication1
Mutagenesisi54C → A: Reduces affinity for substrate and catalytic efficiency. 1 Publication1
Mutagenesisi80D → A: Increases affinity for substrate, but reduces catalytic efficiency. 1 Publication1
Mutagenesisi145S → A: Loss of activity. 1 Publication1
Mutagenesisi199D → A: Reduces catalytic efficiency, but has no effect on affinity for substrate. 1 Publication1
Mutagenesisi218D → A: Reduces affinity for substrate and catalytic efficiency. 1 Publication1
Mutagenesisi223D → A: Loss of activity. 1 Publication1
Mutagenesisi255D → A: Increases affinity for substrate, but reduces catalytic efficiency. 1 Publication1
Mutagenesisi256H → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002103451 – 278S-formylglutathione hydrolase YeiGAdd BLAST278

Proteomic databases

PaxDbiP33018
PRIDEiP33018

Expressioni

Inductioni

Constitutively expressed.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260472, 13 interactors
DIPiDIP-11919N
IntActiP33018, 5 interactors
STRINGi316385.ECDH10B_2311

Structurei

3D structure databases

ProteinModelPortaliP33018
SMRiP33018
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the esterase D family.Curated

Phylogenomic databases

eggNOGiENOG4105C4W Bacteria
COG0627 LUCA
HOGENOMiHOG000263929
InParanoidiP33018
KOiK01070
OMAiEDHLRHH
PhylomeDBiP33018

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000801 Esterase_put
IPR014186 S-formylglutathione_hydrol
PANTHERiPTHR10061 PTHR10061, 1 hit
PfamiView protein in Pfam
PF00756 Esterase, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
TIGRFAMsiTIGR02821 fghA_ester_D, 1 hit

Sequencei

Sequence statusi: Complete.

P33018-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMLEEHRCF EGWQQRWRHD SSTLNCPMTF SIFLPPPRDH TPPPVLYWLS
60 70 80 90 100
GLTCNDENFT TKAGAQRVAA ELGIVLVMPD TSPRGEKVAN DDGYDLGQGA
110 120 130 140 150
GFYLNATQPP WATHYRMYDY LRDELPALVQ SQFNVSDRCA ISGHSMGGHG
160 170 180 190 200
ALIMALKNPG KYTSVSAFAP IVNPCSVPWG IKAFSSYLGE DKNAWLEWDS
210 220 230 240 250
CALMYASNAQ DAIPTLIDQG DNDQFLADQL QPAVLAEAAR QKAWPMTLRI
260 270
QPGYDHSYYF IASFIEDHLR FHAQYLLK
Length:278
Mass (Da):31,259
Last modified:February 1, 1994 - v1
Checksum:i69292AD902EF3E72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00007 Genomic DNA Translation: AAA60510.1
U00096 Genomic DNA Translation: AAC75215.1
AP009048 Genomic DNA Translation: BAE76631.1
PIRiA64984
RefSeqiNP_416659.1, NC_000913.3
WP_000425438.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75215; AAC75215; b2154
BAE76631; BAE76631; BAE76631
GeneIDi949045
KEGGiecj:JW2141
eco:b2154
PATRICifig|1411691.4.peg.86

Similar proteinsi

Entry informationi

Entry nameiSFGH2_ECOLI
AccessioniPrimary (citable) accession number: P33018
Secondary accession number(s): Q2MAS5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 28, 2018
This is version 120 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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