ID   SFGH2_SHIDS             Reviewed;         278 AA.
AC   Q32EQ3;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=S-formylglutathione hydrolase YeiG;
DE            Short=FGH;
DE            EC=3.1.2.12;
GN   Name=yeiG; OrderedLocusNames=SDY_2112;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB62202.1; -; Genomic_DNA.
DR   RefSeq; WP_000425501.1; NC_007606.1.
DR   RefSeq; YP_403693.1; NC_007606.1.
DR   AlphaFoldDB; Q32EQ3; -.
DR   SMR; Q32EQ3; -.
DR   STRING; 300267.SDY_2112; -.
DR   ESTHER; shiss-yeiG; A85-EsteraseD-FGH.
DR   EnsemblBacteria; ABB62202; ABB62202; SDY_2112.
DR   KEGG; sdy:SDY_2112; -.
DR   PATRIC; fig|300267.13.peg.2543; -.
DR   HOGENOM; CLU_056472_0_0_6; -.
DR   OMA; TFMEDHL; -.
DR   Proteomes; UP000002716; 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; Reference proteome; Serine esterase.
FT   CHAIN           1..278
FT                   /note="S-formylglutathione hydrolase YeiG"
FT                   /id="PRO_0000341676"
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;  31369 MW;  3AAD4C18D37FF8F3 CRC64;
     MEMLEEHRCF QGWQQRWRHD SSTLNCPMTF SIFLPPPRDH TPPPVLYWLS GLTCNDENFT
     TKAGAQRVAA ELGIVLVMPD TSPRGEKVAN GDGYDLGQSA GFYLNATQPP WATHYRMYDY
     LRDELPALVQ SQFNVSDRCA ISGHSMGGHG ALIMALKNPG KYTSVSAFAP IVNPCSVPWG
     IKAFSRYLGE DKNAWLEWDR CALMYASNAQ DAIPTLIDQG DNDQFLADQL QPAVLAEAAR
     QKAWPMTLRI QPGYDHSYYF IASFIEDHLR FHAQYLLK