ID A6ZPQ5_YEAS7 Unreviewed; 299 AA.
AC A6ZPQ5;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|ARBA:ARBA00016774, ECO:0000256|RuleBase:RU363068};
DE EC=3.1.2.12 {ECO:0000256|ARBA:ARBA00012479, ECO:0000256|RuleBase:RU363068};
GN ORFNames=SCY_2865 {ECO:0000313|EMBL:EDN63508.1};
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN63508.1, ECO:0000313|Proteomes:UP000007060};
RN [1] {ECO:0000313|EMBL:EDN63508.1, ECO:0000313|Proteomes:UP000007060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN63508.1,
RC ECO:0000313|Proteomes:UP000007060};
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde. {ECO:0000256|RuleBase:RU363068}.
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:0000256|RuleBase:RU363068};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU363068}.
CC -!- SIMILARITY: Belongs to the esterase D family.
CC {ECO:0000256|ARBA:ARBA00005622, ECO:0000256|RuleBase:RU363068}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDN63508.1}.
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DR EMBL; AAFW02000038; EDN63508.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZPQ5; -.
DR ESTHER; yeast-yjg8; A85-EsteraseD-FGH.
DR HOGENOM; CLU_056472_0_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU363068};
KW Hydrolase {ECO:0000256|RuleBase:RU363068, ECO:0000313|EMBL:EDN63508.1};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 299 AA; 33938 MW; DAF45EA84EF1D84F CRC64;
MKVVKEFSVC GGRLIKLSHN SNSTKTSMNV NVYLPKHYYA QDFPRNKRIP TVFYLSGLTC
TPDNASEKAF WQFQADKYGF AMVFPDTSPR GDEVANDPEG SWDFGQGAGF YLNATQEPYA
QHYQMYDYIH KELPQTLDSH FNKNGDVKLD FLDNVAITGH SMGGYGAICG YLKGYSGKRY
KSCSAFAPIV NPSNVPWGQK AFKGYLGEEK AQWEAYDPCL LIKNIRHVGD DRILIHVGDS
DPFLEEHLKP ELLLEAVKAT SWQDYVEIKK VHGFDHSYYF VSTFVPEHAE FHARNLGLI
//
