ID   D3VWY9_COMTE            Unreviewed;       282 AA.
AC   D3VWY9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=S-formylglutathione hydrolase {ECO:0000256|ARBA:ARBA00012479, ECO:0000256|RuleBase:RU363068};
DE            EC=3.1.2.12 {ECO:0000256|ARBA:ARBA00012479, ECO:0000256|RuleBase:RU363068};
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285 {ECO:0000313|EMBL:ADC80459.1};
RN   [1] {ECO:0000313|EMBL:ADC80459.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMCB014 {ECO:0000313|EMBL:ADC80459.1};
RA   Rosewarne C.P., Pettigrove V., Stokes H.W., Parsons Y.M.;
RT   "Class 1 integrons in benthic bacterial communities: abundance, association
RT   with Tn402-like transposition modules and evidence for coselection with
RT   heavy-metal resistance.";
RL   FEMS Microbiol. Ecol. 72:35-46(2010).
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|ARBA:ARBA00000080,
CC         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; GQ281704; ADC80459.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3VWY9; -.
DR   ESTHER; comte-d3vwy9; A85-EsteraseD-FGH.
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   Hydrolase {ECO:0000256|RuleBase:RU363068, ECO:0000313|EMBL:ADC80459.1};
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        227
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        260
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ   SEQUENCE   282 AA;  31224 MW;  63220BA787AD480B CRC64;
     MNIGNNMERI EHHASSEGWQ DVYQHASTTL GCTMKVGVYL PPQAQHGKVP VLYWLSGLTC
     TEQNFITKSA VQRFAAEYGI AVVAPDTSPR GEGVANDAAY DLGQGAGFYV NATQEPWAAN
     YRMYDYVVHE LPARIEAQFP VTTERGISGH SMGGHGALVI ALRNPGRYRS VSAFSPIVAP
     TQVPWGQKAF GAYLGGDQEA WKQYDSVELI RTARERLPLL VDQGLNDEFI ESQLRPELLR
     KVCEETGHPL TLNLRPGHDH SYYFIASFIG EHMAHHASAL NR
//