ID   SFGH_YEAST              Reviewed;         299 AA.
AC   P40363; D6VWB5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=S-formylglutathione hydrolase {ECO:0000303|PubMed:10427036};
DE            Short=FGH {ECO:0000303|PubMed:10427036};
DE            EC=3.1.2.12 {ECO:0000269|PubMed:10427036};
GN   OrderedLocusNames=YJL068C; ORFNames=HRE299, J1102;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7762302; DOI=10.1002/yea.320110108;
RA   Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.;
RT   "Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces
RT   cerevisiae includes the mitochondrial ribosomal protein L8.";
RL   Yeast 11:57-60(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-7, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10427036; DOI=10.1128/aem.65.8.3470-3472.1999;
RA   Degrassi G., Uotila L., Klima R., Venturi V.;
RT   "Purification and properties of an esterase from the yeast Saccharomyces
RT   cerevisiae and identification of the encoding gene.";
RL   Appl. Environ. Microbiol. 65:3470-3472(1999).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [7] {ECO:0007744|PDB:1PV1, ECO:0007744|PDB:3C6B}
RP   X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS).
RX   PubMed=18707125; DOI=10.1021/bi8010016;
RA   Legler P.M., Kumaran D., Swaminathan S., Studier F.W., Millard C.B.;
RT   "Structural characterization and reversal of the natural organophosphate
RT   resistance of a D-type esterase, Saccharomyces cerevisiae S-
RT   formylglutathione hydrolase.";
RL   Biochemistry 47:9592-9601(2008).
RN   [8] {ECO:0007744|PDB:4FLM, ECO:0007744|PDB:4FOL}
RP   X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH COPPER.
RX   PubMed=22906720; DOI=10.1016/j.abb.2012.08.001;
RA   Legler P.M., Leary D.H., Hervey W.J., Millard C.B.;
RT   "A role for His-160 in peroxide inhibition of S. cerevisiae S-
RT   formylglutathione hydrolase: evidence for an oxidation sensitive motif.";
RL   Arch. Biochem. Biophys. 528:7-20(2012).
CC   -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC       formaldehyde. {ECO:0000269|PubMed:10427036}.
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         Evidence={ECO:0000269|PubMed:10427036};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7. {ECO:0000269|PubMed:10427036};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:10427036};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10427036}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10427036}.
CC   -!- MISCELLANEOUS: Present with 1750 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR   EMBL; Z34288; CAA84054.1; -; Genomic_DNA.
DR   EMBL; Z49343; CAA89359.1; -; Genomic_DNA.
DR   EMBL; X88851; CAA61307.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08731.1; -; Genomic_DNA.
DR   PIR; S50803; S50803.
DR   RefSeq; NP_012467.1; NM_001181501.1.
DR   PDB; 1PV1; X-ray; 2.30 A; A/B/C/D=1-299.
DR   PDB; 3C6B; X-ray; 2.17 A; A=1-299.
DR   PDB; 4FLM; X-ray; 2.41 A; A/B=1-299.
DR   PDB; 4FOL; X-ray; 2.07 A; A/B/C/D=1-299.
DR   PDBsum; 1PV1; -.
DR   PDBsum; 3C6B; -.
DR   PDBsum; 4FLM; -.
DR   PDBsum; 4FOL; -.
DR   AlphaFoldDB; P40363; -.
DR   SMR; P40363; -.
DR   BioGRID; 33687; 114.
DR   DIP; DIP-4988N; -.
DR   IntAct; P40363; 4.
DR   MINT; P40363; -.
DR   STRING; 4932.YJL068C; -.
DR   ESTHER; yeast-yjg8; A85-EsteraseD-FGH.
DR   iPTMnet; P40363; -.
DR   MaxQB; P40363; -.
DR   PaxDb; 4932-YJL068C; -.
DR   PeptideAtlas; P40363; -.
DR   TopDownProteomics; P40363; -.
DR   EnsemblFungi; YJL068C_mRNA; YJL068C; YJL068C.
DR   GeneID; 853377; -.
DR   KEGG; sce:YJL068C; -.
DR   AGR; SGD:S000003604; -.
DR   SGD; S000003604; YJL068C.
DR   VEuPathDB; FungiDB:YJL068C; -.
DR   eggNOG; KOG3101; Eukaryota.
DR   GeneTree; ENSGT00390000011864; -.
DR   HOGENOM; CLU_056472_0_1_1; -.
DR   InParanoid; P40363; -.
DR   OMA; PSDCPWG; -.
DR   OrthoDB; 630at2759; -.
DR   BioCyc; YEAST:YJL068C-MONOMER; -.
DR   BRENDA; 3.1.2.12; 984.
DR   Reactome; R-SCE-156590; Glutathione conjugation.
DR   BioGRID-ORCS; 853377; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P40363; -.
DR   PRO; PR:P40363; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P40363; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0018738; F:S-formylglutathione hydrolase activity; IDA:SGD.
DR   GO; GO:0046294; P:formaldehyde catabolic process; IMP:SGD.
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   1: Evidence at protein level;
KW   3D-structure; Copper; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Reference proteome; Serine esterase.
FT   CHAIN           1..299
FT                   /note="S-formylglutathione hydrolase"
FT                   /id="PRO_0000210342"
FT   ACT_SITE        161
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P10768"
FT   ACT_SITE        241
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P10768"
FT   ACT_SITE        276
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P10768"
FT   BINDING         1
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:22906720,
FT                   ECO:0007744|PDB:4FLM"
FT   BINDING         140
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:22906720,
FT                   ECO:0007744|PDB:4FLM"
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   STRAND          12..20
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   STRAND          25..34
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           36..39
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   STRAND          51..55
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           62..68
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           71..78
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           117..120
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           125..130
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           132..141
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   STRAND          151..160
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           162..173
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   STRAND          181..187
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           192..194
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           196..205
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           218..221
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           222..224
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   STRAND          233..238
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           244..247
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           251..257
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   TURN            261..264
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   STRAND          266..271
FT                   /evidence="ECO:0007829|PDB:4FOL"
FT   HELIX           278..295
FT                   /evidence="ECO:0007829|PDB:4FOL"
SQ   SEQUENCE   299 AA;  33934 MW;  BFA5DC02729E9AEF CRC64;
     MKVVKEFSVC GGRLIKLSHN SNSTKTSMNV NIYLPKHYYA QDFPRNKRIP TVFYLSGLTC
     TPDNASEKAF WQFQADKYGF AIVFPDTSPR GDEVANDPEG SWDFGQGAGF YLNATQEPYA
     QHYQMYDYIH KELPQTLDSH FNKNGDVKLD FLDNVAITGH SMGGYGAICG YLKGYSGKRY
     KSCSAFAPIV NPSNVPWGQK AFKGYLGEEK AQWEAYDPCL LIKNIRHVGD DRILIHVGDS
     DPFLEEHLKP ELLLEAVKAT SWQDYVEIKK VHGFDHSYYF VSTFVPEHAE FHARNLGLI
//