Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

S-formylglutathione hydrolase YeiG

Gene

yeiG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei145 – 1451Charge relay systemCurated
Active sitei223 – 2231Charge relay systemCurated
Active sitei256 – 2561Charge relay systemCurated

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciEcoCyc:EG12026-MONOMER.
ECOL316407:JW2141-MONOMER.
MetaCyc:EG12026-MONOMER.
BRENDAi3.1.2.2. 2026.
SABIO-RKP33018.

Protein family/group databases

ESTHERiecoli-yeiG. A85-EsteraseD-FGH.
MEROPSiS09.A39.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12026. yeiG.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261C → A: Reduces catalytic efficiency, but has no effect on affinity for substrate. 1 Publication
Mutagenesisi54 – 541C → A: Reduces affinity for substrate and catalytic efficiency. 1 Publication
Mutagenesisi80 – 801D → A: Increases affinity for substrate, but reduces catalytic efficiency. 1 Publication
Mutagenesisi145 – 1451S → A: Loss of activity. 1 Publication
Mutagenesisi199 – 1991D → A: Reduces catalytic efficiency, but has no effect on affinity for substrate. 1 Publication
Mutagenesisi218 – 2181D → A: Reduces affinity for substrate and catalytic efficiency. 1 Publication
Mutagenesisi223 – 2231D → A: Loss of activity. 1 Publication
Mutagenesisi255 – 2551D → A: Increases affinity for substrate, but reduces catalytic efficiency. 1 Publication
Mutagenesisi256 – 2561H → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 278278S-formylglutathione hydrolase YeiGPRO_0000210345Add
BLAST

Proteomic databases

EPDiP33018.
PaxDbiP33018.

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. 8 interactions.
DIPiDIP-11919N.
IntActiP33018. 5 interactions.
STRINGi511145.b2154.

Structurei

3D structure databases

ProteinModelPortaliP33018.
SMRiP33018. Positions 1-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the esterase D family.Curated

Phylogenomic databases

eggNOGiENOG4105C4W. Bacteria.
COG0627. LUCA.
HOGENOMiHOG000263929.
InParanoidiP33018.
KOiK01070.
OMAiSVELKCK.
OrthoDBiEOG63587Z.
PhylomeDBiP33018.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000801. Esterase_put.
IPR014186. S-formylglutathione_hydrol.
[Graphical view]
PANTHERiPTHR10061. PTHR10061. 1 hit.
PfamiPF00756. Esterase. 1 hit.
[Graphical view]
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.
PATRICi32119655. VBIEscCol129921_2238.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP33018.
SMRiP33018. Positions 1-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260472. 8 interactions.
DIPiDIP-11919N.
IntActiP33018. 5 interactions.
STRINGi511145.b2154.

Protein family/group databases

ESTHERiecoli-yeiG. A85-EsteraseD-FGH.
MEROPSiS09.A39.

Proteomic databases

EPDiP33018.
PaxDbiP33018.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75215; AAC75215; b2154.
BAE76631; BAE76631; BAE76631.
GeneIDi949045.
KEGGiecj:JW2141.
eco:b2154.
PATRICi32119655. VBIEscCol129921_2238.

Organism-specific databases

EchoBASEiEB1961.
EcoGeneiEG12026. yeiG.

Phylogenomic databases

eggNOGiENOG4105C4W. Bacteria.
COG0627. LUCA.
HOGENOMiHOG000263929.
InParanoidiP33018.
KOiK01070.
OMAiSVELKCK.
OrthoDBiEOG63587Z.
PhylomeDBiP33018.

Enzyme and pathway databases

BioCyciEcoCyc:EG12026-MONOMER.
ECOL316407:JW2141-MONOMER.
MetaCyc:EG12026-MONOMER.
BRENDAi3.1.2.2. 2026.
SABIO-RKP33018.

Miscellaneous databases

PROiP33018.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000801. Esterase_put.
IPR014186. S-formylglutathione_hydrol.
[Graphical view]
PANTHERiPTHR10061. PTHR10061. 1 hit.
PfamiPF00756. Esterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR02821. fghA_ester_D. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Automated multiplex sequencing of the E.coli genome."
    Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / BHB2600.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Enzyme genomics: application of general enzymatic screens to discover new enzymes."
    Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F.
    FEMS Microbiol. Rev. 29:263-279(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG."
    Gonzalez C.F., Proudfoot M., Brown G., Korniyenko Y., Mori H., Savchenko A.V., Yakunin A.F.
    J. Biol. Chem. 281:14514-14522(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, MUTAGENESIS OF CYS-26; CYS-54; ASP-80; SER-145; ASP-199; ASP-218; ASP-223; ASP-255 AND HIS-256.

Entry informationi

Entry nameiSFGH2_ECOLI
AccessioniPrimary (citable) accession number: P33018
Secondary accession number(s): Q2MAS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 16, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.