ID A0A2X4TM51_SALER Unreviewed; 285 AA.
AC A0A2X4TM51;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|RuleBase:RU363068};
DE EC=3.1.2.12 {ECO:0000256|RuleBase:RU363068};
GN Name=yeiG {ECO:0000313|EMBL:SQI22852.1};
GN ORFNames=NCTC7304_01867 {ECO:0000313|EMBL:SUG32436.1}, NCTC7307_01992
GN {ECO:0000313|EMBL:SQI22852.1};
OS Salmonella enterica subsp. arizonae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=59203 {ECO:0000313|EMBL:SQI22852.1, ECO:0000313|Proteomes:UP000248731};
RN [1] {ECO:0000313|Proteomes:UP000248731, ECO:0000313|Proteomes:UP000254762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC7304 {ECO:0000313|EMBL:SUG32436.1,
RC ECO:0000313|Proteomes:UP000254762}, and NCTC7307
RC {ECO:0000313|EMBL:SQI22852.1, ECO:0000313|Proteomes:UP000248731};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; LS483466; SQI22852.1; -; Genomic_DNA.
DR EMBL; UGXD01000002; SUG32436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X4TM51; -.
DR Proteomes; UP000248731; Chromosome 1.
DR Proteomes; UP000254762; 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:SF1; S-FORMYLGLUTATHIONE HYDROLASE YEIG; 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:SQI22852.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248731};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 285 AA; 31991 MW; 4A7ABE3B1C1CFACB CRC64;
MEMLEEHRCF GGWQQRWRHH AATLNCAMTF SIFLPPTQDN EPPPVLYWLS GLTCNDENFT
TKAGAQRIAA ELGIVLVMPD TSPRGEQVAN DSGYDLGHGA GFYLNATQPP WVSHYRMYDY
LRDELPALIQ TQFNVSDRCA ISGHSMGGHG ALIMALKNPG KYTSVSAFAP IVNPSRVPWG
TKAFTAYLGE DESAWAPWDS CELMLTSQPQ DAIPTLIDQG DSDQFLADQL QPAVLAEAAR
QTAWPMTLRI QPGYDHSYYF IASFIEDHLR FHARYLRDER ETSPT
//