SFGH2_ECOLI
ID SFGH2_ECOLI Reviewed; 278 AA.
AC P33018; Q2MAS5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=S-formylglutathione hydrolase YeiG;
DE Short=FGH;
DE EC=3.1.2.12;
GN Name=yeiG; OrderedLocusNames=b2154, JW2141;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, INDUCTION, AND MUTAGENESIS OF CYS-26; CYS-54; ASP-80;
RP SER-145; ASP-199; ASP-218; ASP-223; ASP-255 AND HIS-256.
RX PubMed=16567800; DOI=10.1074/jbc.m600996200;
RA Gonzalez C.F., Proudfoot M., Brown G., Korniyenko Y., Mori H.,
RA Savchenko A.V., Yakunin A.F.;
RT "Molecular basis of formaldehyde detoxification. Characterization of two S-
RT formylglutathione hydrolases from Escherichia coli, FrmB and YeiG.";
RL J. Biol. Chem. 281:14514-14522(2006).
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde. Hydrolyzes S-formylglutathione to glutathione and
CC formate. Shows also esterase activity against alpha-naphthyl acetate,
CC lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain
CC fatty acids. {ECO:0000269|PubMed:15808744,
CC ECO:0000269|PubMed:16567800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-formylglutathione = formate + glutathione + H(+);
CC Xref=Rhea:RHEA:14961, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:57688, ChEBI:CHEBI:57925; EC=3.1.2.12;
CC Evidence={ECO:0000269|PubMed:16567800};
CC -!- ACTIVITY REGULATION: Inhibited by the sulfhydryl inhibitors (N-
CC ethylmaleimide, iodoacetate, ZnCl(2) and CuCl(2)).
CC {ECO:0000269|PubMed:16567800}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.43 mM for S-formylglutathione {ECO:0000269|PubMed:16567800};
CC KM=1.03 mM for alpha-naphthyl acetate {ECO:0000269|PubMed:16567800};
CC KM=0.45 mM for pNP-acetate {ECO:0000269|PubMed:16567800};
CC KM=0.70 mM for pNP-butyrate {ECO:0000269|PubMed:16567800};
CC KM=0.95 mM for pNP-caproate {ECO:0000269|PubMed:16567800};
CC KM=0.48 mM for pNP-propionate {ECO:0000269|PubMed:16567800};
CC KM=0.58 mM for S-lactoylglutathione {ECO:0000269|PubMed:16567800};
CC Vmax=12.6 umol/min/mg enzyme with S-formylglutathione as substrate
CC {ECO:0000269|PubMed:16567800};
CC Vmax=9.79 umol/min/mg enzyme with alpha-naphthyl acetate as substrate
CC {ECO:0000269|PubMed:16567800};
CC Vmax=0.50 umol/min/mg enzyme with pNP-acetate as substrate
CC {ECO:0000269|PubMed:16567800};
CC Vmax=0.70 umol/min/mg enzyme with pNP-butyrate as substrate
CC {ECO:0000269|PubMed:16567800};
CC Vmax=0.64 umol/min/mg enzyme with pNP-caproate as substrate
CC {ECO:0000269|PubMed:16567800};
CC Vmax=0.71 umol/min/mg enzyme with pNP-propionate as substrate
CC {ECO:0000269|PubMed:16567800};
CC Vmax=1.97 umol/min/mg enzyme with S-lactoylglutathione as substrate
CC {ECO:0000269|PubMed:16567800};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16567800}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:16567800}.
CC -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR EMBL; U00007; AAA60510.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75215.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76631.1; -; Genomic_DNA.
DR PIR; A64984; A64984.
DR RefSeq; NP_416659.1; NC_000913.3.
DR RefSeq; WP_000425438.1; NZ_SSZK01000011.1.
DR AlphaFoldDB; P33018; -.
DR SMR; P33018; -.
DR BioGRID; 4260472; 13.
DR BioGRID; 853289; 1.
DR DIP; DIP-11919N; -.
DR IntAct; P33018; 5.
DR STRING; 511145.b2154; -.
DR ESTHER; ecoli-yeiG; A85-EsteraseD-FGH.
DR MEROPS; S09.A39; -.
DR jPOST; P33018; -.
DR PaxDb; P33018; -.
DR PRIDE; P33018; -.
DR EnsemblBacteria; AAC75215; AAC75215; b2154.
DR EnsemblBacteria; BAE76631; BAE76631; BAE76631.
DR GeneID; 949045; -.
DR KEGG; ecj:JW2141; -.
DR KEGG; eco:b2154; -.
DR PATRIC; fig|1411691.4.peg.86; -.
DR EchoBASE; EB1961; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_056472_0_0_6; -.
DR InParanoid; P33018; -.
DR OMA; TFMEDHL; -.
DR PhylomeDB; P33018; -.
DR BioCyc; EcoCyc:EG12026-MON; -.
DR BioCyc; MetaCyc:EG12026-MON; -.
DR BRENDA; 3.1.2.2; 2026.
DR SABIO-RK; P33018; -.
DR PRO; PR:P33018; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IDA:EcoCyc.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IDA:EcoCyc.
DR GO; GO:0046294; P:formaldehyde catabolic process; IMP:EcoCyc.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR PANTHER; PTHR10061; PTHR10061; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR02821; fghA_ester_D; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..278
FT /note="S-formylglutathione hydrolase YeiG"
FT /id="PRO_0000210345"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT MUTAGEN 26
FT /note="C->A: Reduces catalytic efficiency, but has no
FT effect on affinity for substrate."
FT /evidence="ECO:0000269|PubMed:16567800"
FT MUTAGEN 54
FT /note="C->A: Reduces affinity for substrate and catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:16567800"
FT MUTAGEN 80
FT /note="D->A: Increases affinity for substrate, but reduces
FT catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16567800"
FT MUTAGEN 145
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16567800"
FT MUTAGEN 199
FT /note="D->A: Reduces catalytic efficiency, but has no
FT effect on affinity for substrate."
FT /evidence="ECO:0000269|PubMed:16567800"
FT MUTAGEN 218
FT /note="D->A: Reduces affinity for substrate and catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:16567800"
FT MUTAGEN 223
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16567800"
FT MUTAGEN 255
FT /note="D->A: Increases affinity for substrate, but reduces
FT catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16567800"
FT MUTAGEN 256
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16567800"
SQ SEQUENCE 278 AA; 31259 MW; 69292AD902EF3E72 CRC64;
MEMLEEHRCF EGWQQRWRHD SSTLNCPMTF SIFLPPPRDH TPPPVLYWLS GLTCNDENFT
TKAGAQRVAA ELGIVLVMPD TSPRGEKVAN DDGYDLGQGA GFYLNATQPP WATHYRMYDY
LRDELPALVQ SQFNVSDRCA ISGHSMGGHG ALIMALKNPG KYTSVSAFAP IVNPCSVPWG
IKAFSSYLGE DKNAWLEWDS CALMYASNAQ DAIPTLIDQG DNDQFLADQL QPAVLAEAAR
QKAWPMTLRI QPGYDHSYYF IASFIEDHLR FHAQYLLK
