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SFGH1_ECO24
ID   SFGH1_ECO24             Reviewed;         277 AA.
AC   A7ZIA3;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=S-formylglutathione hydrolase FrmB;
DE            Short=FGH;
DE            EC=3.1.2.12;
GN   Name=frmB; OrderedLocusNames=EcE24377A_0380;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV18859.1; -; Genomic_DNA.
DR   RefSeq; WP_000419049.1; NC_009801.1.
DR   AlphaFoldDB; A7ZIA3; -.
DR   SMR; A7ZIA3; -.
DR   ESTHER; ecoli-yaim; A85-EsteraseD-FGH.
DR   MEROPS; S09.940; -.
DR   EnsemblBacteria; ABV18859; ABV18859; EcE24377A_0380.
DR   GeneID; 66671340; -.
DR   KEGG; ecw:EcE24377A_0380; -.
DR   HOGENOM; CLU_056472_0_0_6; -.
DR   OMA; YFWRRMA; -.
DR   Proteomes; UP000001122; 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_0000341658"
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;  31399 MW;  D87B291FAFA5AA9A CRC64;
     MELIEKHASF GGWQNVYRHY SQSLKCEMNV GVYLPPKAAN EKLPVLYWLS GLTCNEQNFI
     TKSGMQRYAA EHNIIVVAPD TSPRGSHVAD ADRYDLGQGA GFYLNATQAP WNEHYKMYDY
     IRNELPDLVM QHFPATTRKS ISGHSMGGLG ALVLALRNPD EYVSVSAFSP IVSPSQVPWG
     QQAFAAYLGE NKDAWLDYDP VSLISQGQRV AEIMVDQGLS DDFYAEQLRT PNLEKICQEM
     NIKTLIRYHE GYDHSYYFVS SFIGEHIAYH ANKLNMR
 
 
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