ID   SFGH_PARDP              Reviewed;         279 AA.
AC   A1AXZ2; Q51671;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=S-formylglutathione hydrolase;
DE            Short=FGH;
DE            EC=3.1.2.12;
GN   Name=fghA; OrderedLocusNames=Pden_0019;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS A FORMYLGLUTATHIONE
RP   HYDROLASE.
RX   PubMed=8892832; DOI=10.1128/jb.178.21.6296-6299.1996;
RA   Harms N., Ras J., Reijnders W.N.M., van Spanning R.J.M., Stouthamer A.H.;
RT   "S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to
RT   human esterase D: a universal pathway for formaldehyde detoxification?";
RL   J. Bacteriol. 178:6296-6299(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC       formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate
CC       (Probable). {ECO:0000305|PubMed:8892832}.
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; U34346; AAC44554.1; -; Genomic_DNA.
DR   EMBL; CP000489; ABL68136.1; -; Genomic_DNA.
DR   RefSeq; WP_011746369.1; NC_008686.1.
DR   AlphaFoldDB; A1AXZ2; -.
DR   SMR; A1AXZ2; -.
DR   STRING; 318586.Pden_0019; -.
DR   ESTHER; parde-FGHA; A85-EsteraseD-FGH.
DR   MEROPS; S09.940; -.
DR   PRIDE; A1AXZ2; -.
DR   EnsemblBacteria; ABL68136; ABL68136; Pden_0019.
DR   KEGG; pde:Pden_0019; -.
DR   eggNOG; COG0627; Bacteria.
DR   HOGENOM; CLU_056472_0_0_5; -.
DR   OMA; TFMEDHL; -.
DR   Proteomes; UP000000361; Chromosome 1.
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   1: Evidence at protein level;
KW   Hydrolase; Reference proteome; Serine esterase.
FT   CHAIN           1..279
FT                   /note="S-formylglutathione hydrolase"
FT                   /id="PRO_0000341679"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        226
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        258
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        272..277
FT                   /note="RWHAER -> PLARGA (in Ref. 1; AAC44554)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   279 AA;  31276 MW;  A980EB9D179EDB26 CRC64;
     MTLAYETVSE NRSFGGIQGV YRHQSQATGT PMTFAIYLPP DARHGKVPVL WYLSGLTCTH
     ENAMTKAGAQ EWAAEYGIAV IFPDTSPRGE GVANDETYDL GQGAGFYVDA TEAPWAPHFR
     MWHYVTHELP ELVFNNFPLD REAQGITGHS MGGHGALTIA MTFPERYRSV SAFAPIAHPS
     ESDWGRKQFA AYLGDDKAAW KRHDSTILMR EKGYPGEVLI DQGASDQFLD LLKPEALAHA
     MAERRQPGTF RMQQGYDHSY FFVQSFMADH IRWHAERLG