ID   A5WCZ7_PSYWF            Unreviewed;       284 AA.
AC   A5WCZ7;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
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};
GN   OrderedLocusNames=PsycPRwf_0583 {ECO:0000313|EMBL:ABQ93538.1};
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ93538.1};
RN   [1] {ECO:0000313|EMBL:ABQ93538.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ93538.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) 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|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; CP000713; ABQ93538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5WCZ7; -.
DR   STRING; 349106.PsycPRwf_0583; -.
DR   ESTHER; psywf-a5wcz7; A85-EsteraseD-FGH.
DR   KEGG; prw:PsycPRwf_0583; -.
DR   eggNOG; COG0627; Bacteria.
DR   HOGENOM; CLU_056472_0_0_6; -.
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:ABQ93538.1};
KW   Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        226
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   284 AA;  31856 MW;  2CFED97AB94A923D CRC64;
     MSTLTLTSKN RCFNGEQYYY THQSAVTQTE MSFSIYLPDE ALAGQTCPAL LYLSGLTCSP
     DNVTHKAHFQ QKCSELGMIF IAPDTSPKGE SVPNDERYFV GQGASYYVNA TEDKWSKHFN
     MHSYIIDEFY ELIRSQFAIS SVGITGHSMG GHGALMFGFK YPSKFISVSA IAPICVASES
     DWGRAAFSEY FGAESEQTWA QFDAVNIVEK AGKQYPHILV DQGAADDFYV DGYLRPEALQ
     KVCQQVEQPL TLRYHAGFDH SYYFIQSIIN DHIEHHYNAA LTAI
//