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 27-MAR-2024, entry version 121.
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.ENSSSCP00000051039; -.
DR BindingDB; Q9GJT2; -.
DR ChEMBL; CHEMBL4063; -.
DR ESTHER; pig-estd; A85-EsteraseD-FGH.
DR MEROPS; S09.990; -.
DR PaxDb; 9823-ENSSSCP00000010038; -.
DR PeptideAtlas; Q9GJT2; -.
DR Ensembl; ENSSSCT00000052541.2; ENSSSCP00000051039.1; ENSSSCG00000009407.5.
DR Ensembl; ENSSSCT00025011320.1; ENSSSCP00025004554.1; ENSSSCG00025008498.1.
DR Ensembl; ENSSSCT00035101467.1; ENSSSCP00035043187.1; ENSSSCG00035074723.1.
DR Ensembl; ENSSSCT00065027476.1; ENSSSCP00065011280.1; ENSSSCG00065020640.1.
DR Ensembl; ENSSSCT00070001272.1; ENSSSCP00070001112.1; ENSSSCG00070000676.1.
DR Ensembl; ENSSSCT00070001276.1; ENSSSCP00070001115.1; ENSSSCG00070000676.1.
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; PSDCPWG; -.
DR OrthoDB; 630at2759; -.
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 Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR Bgee; ENSSSCG00000009407; Expressed in epididymis and 45 other cell types or tissues.
DR ExpressionAtlas; Q9GJT2; baseline.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR NCBIfam; TIGR02821; fghA_ester_D; 1.
DR PANTHER; PTHR10061; S-FORMYLGLUTATHIONE HYDROLASE; 1.
DR PANTHER; PTHR10061:SF0; S-FORMYLGLUTATHIONE HYDROLASE; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//
