ID A0A2A9P1Y7_9AGAR Unreviewed; 291 AA.
AC A0A2A9P1Y7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=AMATHDRAFT_52815 {ECO:0000313|EMBL:PFH54832.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH54832.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH54832.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH54832.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KZ301969; PFH54832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9P1Y7; -.
DR STRING; 703135.A0A2A9P1Y7; -.
DR OrthoDB; 630at2759; -.
DR Proteomes; UP000242287; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000242287};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 269
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 291 AA; 32032 MW; E85C0D86BF9FD655 CRC64;
MADTNLQKLS SNKTFNGELI KYKFKSAALG GLDAQFNLYL PPQSTVVKVP LLVYLSGLTC
TEDNGAQKGG FFEAASKQGV AILFPDTSPR GAGIPGEDDD WDFGTGAGFY LNATNPKYSK
HYNMLTHVTI ELPQIMEAAG LPIDFKRQSI FGHSMGGHGA LTLYLASATQ QYKSASAFSP
ISNPMKCPWG EKAFKGYLQG GIEEAKLRYD ATELIARRKD PVHILIDYGT GDNFYIQGQL
LPENFLNAAR GAGHDESHVR VRRHEGYDHS YYFISTFASD HVLYHAGFLK I
//
