ID   ESTD_RAT                Reviewed;         282 AA.
AC   B0BNE5;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=S-formylglutathione hydrolase;
DE            Short=FGH;
DE            EC=3.1.2.12;
DE   AltName: Full=Esterase D;
GN   Name=Esd;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC       formaldehyde. {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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR   EMBL; BC158790; AAI58791.1; -; mRNA.
DR   RefSeq; NP_001099521.1; NM_001106051.3.
DR   RefSeq; NP_001257794.1; NM_001270865.1.
DR   RefSeq; NP_001257795.1; NM_001270866.1.
DR   AlphaFoldDB; B0BNE5; -.
DR   SMR; B0BNE5; -.
DR   BioGRID; 253188; 1.
DR   STRING; 10116.ENSRNOP00000013324; -.
DR   ESTHER; rat-estd; A85-EsteraseD-FGH.
DR   iPTMnet; B0BNE5; -.
DR   PhosphoSitePlus; B0BNE5; -.
DR   World-2DPAGE; 0004:B0BNE5; -.
DR   jPOST; B0BNE5; -.
DR   PaxDb; B0BNE5; -.
DR   PeptideAtlas; B0BNE5; -.
DR   PRIDE; B0BNE5; -.
DR   Ensembl; ENSRNOT00000078013; ENSRNOP00000068608; ENSRNOG00000009512.
DR   GeneID; 290401; -.
DR   KEGG; rno:290401; -.
DR   UCSC; RGD:1592114; rat.
DR   CTD; 2098; -.
DR   RGD; 1592114; Esd.
DR   eggNOG; KOG3101; Eukaryota.
DR   GeneTree; ENSGT00390000011864; -.
DR   HOGENOM; CLU_056472_0_0_1; -.
DR   InParanoid; B0BNE5; -.
DR   OMA; TFMEDHL; -.
DR   OrthoDB; 942551at2759; -.
DR   PhylomeDB; B0BNE5; -.
DR   TreeFam; TF300793; -.
DR   Reactome; R-RNO-156590; Glutathione conjugation.
DR   PRO; PR:B0BNE5; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000009512; Expressed in kidney and 20 other tissues.
DR   Genevisible; B0BNE5; RN.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0018738; F:S-formylglutathione hydrolase activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Cytoplasmic vesicle; Hydrolase; Reference proteome;
KW   Serine esterase.
FT   CHAIN           1..282
FT                   /note="S-formylglutathione hydrolase"
FT                   /id="PRO_0000341966"
FT   ACT_SITE        149
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        260
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         4
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0P3"
FT   MOD_RES         200
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P10768"
SQ   SEQUENCE   282 AA;  31364 MW;  61D0CDDE45B9DEC5 CRC64;
     MELKQISSNK CFGGLQKVFE HSSVELKCKM KFAIYLPPQA ESAKCPALYW LSGLTCTEQN
     FISKSGCQQA ASEHGLVVIA PDTSPRGCNI KGEDDSWDFG TGAGFFVNAT EDPWNTNYRM
     YSYVTEELPQ LINANFPVDP QRISIFGHSM GGHGALICAL KNPGKYRSVS AFAPICNPVL
     CPWGKKAFNG YLGPDQSKWK AYDATCLVKS YSGPQIDILI DQGKDDEFLS NGQLLPDNFI
     AACTEKKIPV VFRLQEGYDH SYYFIATFIT DHIRHHAKYL NA