ID   SFGH1_ECOUT             Reviewed;         277 AA.
AC   Q1RFI8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=S-formylglutathione hydrolase FrmB;
DE            Short=FGH;
DE            EC=3.1.2.12;
GN   Name=frmB; OrderedLocusNames=UTI89_C0375;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC       formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate
CC       (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR   EMBL; CP000243; ABE05876.1; -; Genomic_DNA.
DR   RefSeq; WP_000419070.1; NC_007946.1.
DR   AlphaFoldDB; Q1RFI8; -.
DR   SMR; Q1RFI8; -.
DR   ESTHER; ecoli-yaim; A85-EsteraseD-FGH.
DR   MEROPS; S09.940; -.
DR   EnsemblBacteria; ABE05876; ABE05876; UTI89_C0375.
DR   KEGG; eci:UTI89_C0375; -.
DR   HOGENOM; CLU_056472_0_0_6; -.
DR   OMA; YFWRRMA; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0018738; F:S-formylglutathione hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Hydrolase; Serine esterase.
FT   CHAIN           1..277
FT                   /note="S-formylglutathione hydrolase FrmB"
FT                   /id="PRO_0000341657"
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;  31435 MW;  A16D0455C3693BA0 CRC64;
     MELIEKHASF GGWQNVYRHY SQSLKCEMNV GVYLPPKAEN EKLPVLYWLS GLTCNEQNFI
     TKSGMQRYAA EHNIIVVAPD TSPRGSHVAD ADRYDLGQGA GFYLNATQAP WNEHYKMYDY
     IRNELPNLVM HHFPATARKS ISGHSMGGLG ALVLALRNPD EYVSVSAFSP IVSPSQVPWG
     QQAFAAYLGE NKDAWLDYDP VSLISQGQRV AEIMVDQGLS DDFYAEQLRT PNLEKICQEM
     NIKTLIRYHE GYDHSYYFVS SFIGEHIAYH ANKLNMR