SFGH_YEAST
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 03-AUG-2022, entry version 165.
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; P40363; -.
DR PRIDE; P40363; -.
DR TopDownProteomics; P40363; -.
DR EnsemblFungi; YJL068C_mRNA; YJL068C; YJL068C.
DR GeneID; 853377; -.
DR KEGG; sce:YJL068C; -.
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; TFMEDHL; -.
DR BioCyc; YEAST:YJL068C-MON; -.
DR BRENDA; 3.1.2.12; 984.
DR Reactome; R-SCE-156590; Glutathione conjugation.
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; -; 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 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
