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Database: UniProt
Entry: L1JU56_GUITC
LinkDB: L1JU56_GUITC
Original site: L1JU56_GUITC 
ID   L1JU56_GUITC            Unreviewed;       281 AA.
AC   L1JU56;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=GUITHDRAFT_157099 {ECO:0000313|EMBL:EKX52106.1};
OS   Guillardia theta (strain CCMP2712) (Cryptophyte).
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX52106.1};
RN   [1] {ECO:0000313|EMBL:EKX52106.1, ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX52106.1,
RC   ECO:0000313|Proteomes:UP000011087};
RX   PubMed=23201678; DOI=10.1038/nature11681;
RG   DOE Joint Genome Institute;
RA   Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA   Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA   Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA   Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA   Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA   Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT   "Algal genomes reveal evolutionary mosaicism and the fate of
RT   nucleomorphs.";
RL   Nature 492:59-65(2012).
RN   [2] {ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA   Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA   Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA   Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA   Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA   Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA   Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblProtists:EKX52106}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (MAR-2016) to UniProtKB.
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; JH992973; EKX52106.1; -; Genomic_DNA.
DR   RefSeq; XP_005839086.1; XM_005839029.1.
DR   AlphaFoldDB; L1JU56; -.
DR   STRING; 905079.L1JU56; -.
DR   PaxDb; 55529-EKX52106; -.
DR   EnsemblProtists; EKX52106; EKX52106; GUITHDRAFT_157099.
DR   GeneID; 17308799; -.
DR   KEGG; gtt:GUITHDRAFT_157099; -.
DR   eggNOG; KOG3101; Eukaryota.
DR   HOGENOM; CLU_056472_0_0_1; -.
DR   OMA; PSDCPWG; -.
DR   OrthoDB; 630at2759; -.
DR   Proteomes; UP000011087; 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:UP000011087};
KW   Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT   ACT_SITE        147
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        225
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        259
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ   SEQUENCE   281 AA;  31175 MW;  D5ABFBE92241C995 CRC64;
     MARLLESKKA FNAEVNQYEH NSPTLGCVMK FSVINGGSGS DEKLPVIYWL SGLTCSDRNF
     IEKAGAFRAA VENRVIIVCP DTSPRGVDIE GDSESWDFGK GAGFYLNATQ PKWAANYKMY
     DYVTNELMEI IEQTVKTNGK KAIMGHSMGG HGALTIALRN PGVYTSVSAF APICNPMQCP
     WGNKAFTGYL GDDQEQWKAY DATEQMKGMK AAPFDDILID VGDKDNFLTA GQLLPENFKA
     ACDQVGQKCS LRMQPGYDHS YFFIATFIED HIKFHKQRLA N
//
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