SFGH1_ECOLI
ID SFGH1_ECOLI Reviewed; 277 AA.
AC P51025; P77317; Q2MC69;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=S-formylglutathione hydrolase FrmB;
DE Short=FGH;
DE EC=3.1.2.12;
GN Name=frmB; Synonyms=yaiM; OrderedLocusNames=b0355, JW0346;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION.
RA Rudd K.E.;
RL Unpublished observations (MAR-1996).
RN [6]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15466022; DOI=10.1128/jb.186.20.6714-6720.2004;
RA Herring C.D., Blattner F.R.;
RT "Global transcriptional effects of a suppressor tRNA and the inactivation
RT of the regulator frmR.";
RL J. Bacteriol. 186:6714-6720(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
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 two pNP-esters (pNP-
CC acetate and pNP-propionate), alpha-naphthyl acetate and
CC lactoylglutathione. {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=0.41 mM for S-formylglutathione {ECO:0000269|PubMed:16567800};
CC KM=0.29 mM for pNP-acetate {ECO:0000269|PubMed:16567800};
CC KM=0.83 mM for pNP-propionate {ECO:0000269|PubMed:16567800};
CC KM=0.60 mM for S-lactoylglutathione {ECO:0000269|PubMed:16567800};
CC Vmax=55.0 umol/min/mg enzyme with S-formylglutathione as substrate
CC {ECO:0000269|PubMed:16567800};
CC Vmax=0.58 umol/min/mg enzyme with pNP-acetate as substrate
CC {ECO:0000269|PubMed:16567800};
CC Vmax=0.27 umol/min/mg enzyme with pNP-propionate as substrate
CC {ECO:0000269|PubMed:16567800};
CC Vmax=0.09 umol/min/mg enzyme with S-lactoylglutathione as substrate
CC {ECO:0000269|PubMed:16567800};
CC -!- INDUCTION: Induced by formaldehyde and repressed by FrmR.
CC {ECO:0000269|PubMed:15466022, ECO:0000269|PubMed:16567800}.
CC -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=D85613; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D85613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U73857; AAB18080.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73458.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76137.1; -; Genomic_DNA.
DR PIR; C64763; C64763.
DR RefSeq; NP_414889.1; NC_000913.3.
DR RefSeq; WP_000419081.1; NZ_LN832404.1.
DR AlphaFoldDB; P51025; -.
DR SMR; P51025; -.
DR BioGRID; 4261809; 19.
DR DIP; DIP-11274N; -.
DR IntAct; P51025; 5.
DR STRING; 511145.b0355; -.
DR ESTHER; ecoli-yaim; A85-EsteraseD-FGH.
DR MEROPS; S09.940; -.
DR jPOST; P51025; -.
DR PaxDb; P51025; -.
DR PRIDE; P51025; -.
DR EnsemblBacteria; AAC73458; AAC73458; b0355.
DR EnsemblBacteria; BAE76137; BAE76137; BAE76137.
DR GeneID; 944991; -.
DR KEGG; ecj:JW0346; -.
DR KEGG; eco:b0355; -.
DR PATRIC; fig|1411691.4.peg.1923; -.
DR EchoBASE; EB3080; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_056472_0_0_6; -.
DR InParanoid; P51025; -.
DR OMA; YFWRRMA; -.
DR PhylomeDB; P51025; -.
DR BioCyc; EcoCyc:G6208-MON; -.
DR BioCyc; MetaCyc:G6208-MON; -.
DR SABIO-RK; P51025; -.
DR PRO; PR:P51025; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IDA:EcoCyc.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
DR GO; GO:0046292; P:formaldehyde metabolic 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..277
FT /note="S-formylglutathione hydrolase FrmB"
FT /id="PRO_0000210343"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 277 AA; 31424 MW; C69C708293FA0AEC CRC64;
MELIEKHVSF GGWQNMYRHY SQSLKCEMNV GVYLPPKAAN EKLPVLYWLS GLTCNEQNFI
TKSGMQRYAA EHNIIVVAPD TSPRGSHVAD ADRYDLGQGA GFYLNATQAP WNEHYKMYDY
IRNELPDLVM HHFPATAKKS ISGHSMGGLG ALVLALRNPD EYVSVSAFSP IVSPSQVPWG
QQAFAAYLAE NKDAWLDYDP VSLISQGQRV AEIMVDQGLS DDFYAEQLRT PNLEKICQEM
NIKTLIRYHE GYDHSYYFVS SFIGEHIAYH ANKLNMR
