ID A0A239PXE6_9RHOB Unreviewed; 296 AA.
AC A0A239PXE6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 ORFNames=SAMN05444959_10982 {ECO:0000313|EMBL:SNT75001.1};
OS Paracoccus seriniphilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=184748 {ECO:0000313|EMBL:SNT75001.1, ECO:0000313|Proteomes:UP000198307};
RN [1] {ECO:0000313|EMBL:SNT75001.1, ECO:0000313|Proteomes:UP000198307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14827 {ECO:0000313|EMBL:SNT75001.1,
RC ECO:0000313|Proteomes:UP000198307};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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; FZQB01000009; SNT75001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239PXE6; -.
DR Proteomes; UP000198307; Unassembled WGS sequence.
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:SNT75001.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198307};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 296 AA; 33089 MW; 4DAA7E70F89C0EAB CRC64;
MGLVGRRTGP QYLAEKGHDV TIETLSENRS FGGTQGVYRH KSQSTGTDMT FALFLPEEAQ
HGRVPVLWYL SGLTCTHENA MTKAAAQEWC AEAGIAIVFP DTSPRGDEVA DDEAYDLGKG
AGFYVNATQD PWKPHYQMWQ YIVHELPELV SDNFAIDRDA MGITGHSMGG HGALTIAMTH
PDRYRSVSAF SPIANPTESD WGRKQLSAYL GEDRATWRAH DATILMTERG YPGEVLIDQG
SEDQFLDLLK PEALAQAMMA RRQPGQFRMQ PGYDHSYFFV QTFMADHILW HAERLA
//
