ID   SFGH2_ECOUT             Reviewed;         278 AA.
AC   Q1R9R8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=S-formylglutathione hydrolase YeiG;
DE            Short=FGH;
DE            EC=3.1.2.12;
GN   Name=yeiG; OrderedLocusNames=UTI89_C2428;
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; ABE07896.1; -; Genomic_DNA.
DR   RefSeq; WP_000425456.1; NC_007946.1.
DR   AlphaFoldDB; Q1R9R8; -.
DR   SMR; Q1R9R8; -.
DR   ESTHER; ecoli-yeiG; A85-EsteraseD-FGH.
DR   MEROPS; S09.A39; -.
DR   EnsemblBacteria; ABE07896; ABE07896; UTI89_C2428.
DR   KEGG; eci:UTI89_C2428; -.
DR   HOGENOM; CLU_056472_0_0_6; -.
DR   OMA; TFMEDHL; -.
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..278
FT                   /note="S-formylglutathione hydrolase YeiG"
FT                   /id="PRO_0000341668"
FT   ACT_SITE        145
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        223
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        256
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   278 AA;  31287 MW;  EA3B712CF39FB1C4 CRC64;
     MEMLEEHRCF EGWQQRWRHD SSTLNCPMTF SIFLPPPRDH TPPPVLYWLS GLTCNDENFT
     TKAGAQRVAA ELGIVLVMPD TSPRGEQVAN DDGYDLGQGA GFYLNATQPP WATHYRMYDY
     LRDELPALIQ SQFNVSDRCA ISGHSMGGHG ALIMALKNPG KYTSVSAFAP IVNPCSVPWG
     IKAFSTYLGE DKNAWLEWDS CALMYASNAQ DAIPTLIDQG DNDQFLADQL QPAVLAEAAR
     QKAWPMTLRI QPGYDHSYYF IASFIEDHLR FHAQYLLK