ID   ESTD_PIG                Reviewed;         282 AA.
AC   Q9GJT2; Q9GM98;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=S-formylglutathione hydrolase;
DE            Short=FGH;
DE            EC=3.1.2.12;
DE   AltName: Full=Esterase D;
GN   Name=ESD;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-196.
RC   STRAIN=Ohmini;
RX   PubMed=11167536; DOI=10.1046/j.1365-2052.2000.00690.x;
RA   Omi T., Tsuchida S., Onishi A., Amano T., Tanaka K., Iwamoto S., Kajii E.;
RT   "Molecular basis of esterase D polymorphism in the pig.";
RL   Anim. Genet. 31:413-414(2000).
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   -!- POLYMORPHISM: The sequence of allele A is shown (PubMed:11167536).
CC       {ECO:0000269|PubMed:11167536}.
CC   -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR   EMBL; AB032555; BAA92850.1; -; mRNA.
DR   EMBL; AB038362; BAB11922.1; -; mRNA.
DR   EMBL; AF254785; AAG17630.1; -; mRNA.
DR   RefSeq; NP_999225.1; NM_214060.1.
DR   RefSeq; XP_005668471.1; XM_005668414.2.
DR   AlphaFoldDB; Q9GJT2; -.
DR   SMR; Q9GJT2; -.
DR   STRING; 9823.ENSSSCP00000010038; -.
DR   BindingDB; Q9GJT2; -.
DR   ChEMBL; CHEMBL4063; -.
DR   ESTHER; pig-estd; A85-EsteraseD-FGH.
DR   MEROPS; S09.990; -.
DR   PaxDb; Q9GJT2; -.
DR   PeptideAtlas; Q9GJT2; -.
DR   PRIDE; Q9GJT2; -.
DR   Ensembl; ENSSSCT00000052541; ENSSSCP00000051039; ENSSSCG00000009407.
DR   Ensembl; ENSSSCT00025011320; ENSSSCP00025004554; ENSSSCG00025008498.
DR   Ensembl; ENSSSCT00035101467; ENSSSCP00035043187; ENSSSCG00035074723.
DR   Ensembl; ENSSSCT00065027476; ENSSSCP00065011280; ENSSSCG00065020640.
DR   Ensembl; ENSSSCT00070001272; ENSSSCP00070001112; ENSSSCG00070000676.
DR   Ensembl; ENSSSCT00070001276; ENSSSCP00070001115; ENSSSCG00070000676.
DR   GeneID; 397127; -.
DR   KEGG; ssc:397127; -.
DR   CTD; 2098; -.
DR   VGNC; VGNC:87788; ESD.
DR   eggNOG; KOG3101; Eukaryota.
DR   GeneTree; ENSGT00390000011864; -.
DR   HOGENOM; CLU_056472_0_0_1; -.
DR   InParanoid; Q9GJT2; -.
DR   OMA; TFMEDHL; -.
DR   OrthoDB; 942551at2759; -.
DR   TreeFam; TF300793; -.
DR   BRENDA; 3.1.2.12; 6170.
DR   Reactome; R-SSC-156590; Glutathione conjugation.
DR   PRO; PR:Q9GJT2; -.
DR   Proteomes; UP000008227; Chromosome 11.
DR   Proteomes; UP000314985; Chromosome 11.
DR   Bgee; ENSSSCG00000009407; Expressed in epididymis and 45 other tissues.
DR   ExpressionAtlas; Q9GJT2; baseline and differential.
DR   Genevisible; Q9GJT2; SS.
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:0042802; F:identical protein binding; IEA:Ensembl.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0P3"
FT   CHAIN           2..282
FT                   /note="S-formylglutathione hydrolase"
FT                   /id="PRO_0000210341"
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         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0P3"
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"
FT   VARIANT         196
FT                   /note="E -> G (in allele B)"
FT                   /evidence="ECO:0000269|PubMed:11167536"
SQ   SEQUENCE   282 AA;  31482 MW;  62846B9291591FBA CRC64;
     MALKQLSSNK CFGGLQKVFE HDSVELKCKM KFAIYLPPKA ETGKCPALYW LSGLTCTEQN
     FITKSGYHQA ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYLDAT EDPWKTNYRM
     YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICTL KNPGKYKSVS AFAPICNPVL
     CPWGKKAFSG YLGTDESKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLS DGQLLPDNFI
     AACTEKKIPV VFRSQEGYDH SYYFIATFIT DHIRHHAKYL NA