ID A7EPQ7_SCLS1 Unreviewed; 286 AA.
AC A7EPQ7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=SS1G_07306 {ECO:0000313|EMBL:EDO04823.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO04823.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476629; EDO04823.1; -; Genomic_DNA.
DR RefSeq; XP_001591860.1; XM_001591810.1.
DR AlphaFoldDB; A7EPQ7; -.
DR STRING; 665079.A7EPQ7; -.
DR ESTHER; scls1-a7epq7; A85-EsteraseD-FGH.
DR EnsemblFungi; EDO04823; EDO04823; SS1G_07306.
DR GeneID; 5488014; -.
DR KEGG; ssl:SS1G_07306; -.
DR eggNOG; KOG3101; Eukaryota.
DR HOGENOM; CLU_056472_0_1_1; -.
DR InParanoid; A7EPQ7; -.
DR OMA; PSDCPWG; -.
DR OrthoDB; 630at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:EnsemblFungi.
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:UP000001312};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 286 AA; 31256 MW; 84A0553B61B56457 CRC64;
MSFKTTATIS SFGGKLLKLT HNASTVGCEM ALNLYLPPKA SAEKKVPVIF YLAGLTCTGD
NGAEKGFFQS AASEKGIAVV YPDTSPRGLN IAGENDSWDF GTGAGFYIDA TNPPYSTNYK
MYSYITSELP SSLFSSFPEL DSSRKSIMGH SMGGHGALTL FLKNPGMYKS VSAFAPISNP
VKCPWGEKAF TGYFGEGKKE EWVKHDATEL IKGFKGEFPA LIDVGTGDNF YKQGQLLPEN
FAAAAKESRN DGNLTLRYQE EYDHSYFFIS TFGRDHIEHA AKYLFA
//
