ID A0A161W2K7_9PEZI Unreviewed; 295 AA.
AC A0A161W2K7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=CT0861_00261 {ECO:0000313|EMBL:KZL65403.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL65403.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL65403.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL65403.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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}.
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:KZL65403.1}.
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DR EMBL; LFIV01000222; KZL65403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161W2K7; -.
DR STRING; 708197.A0A161W2K7; -.
DR OrthoDB; 630at2759; -.
DR Proteomes; UP000076552; 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:KZL65403.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 155
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 267
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 295 AA; 32638 MW; DD93D69B9AB1563E CRC64;
MAAAAAFQTK ATITSFGGQL LKLSHKSSTT GTDMAVNLYL PPQCTTRAVP VLFYLSGLTC
TPDNCTEKGF FQAQASARGV AIVYPDTSPR GLDLPGERDS WDFGEAASFY VDATREPFRQ
NYRMETYITK ELPELLFREF AGKLDRSRIS ITGHSMGGHG ALSLYLRHPG MYRSVSAFAP
IANPSNCPWG EKAFSGYLGD DRAEWAKHDS TELVKNWSYG PLNALIDVGL GDNFYIQKQL
LPENFEKAVK EKNLEGLSLR YHYGYDHSYF FMASFAKDHV DHAAKHLGLG NATSA
//
