ID A7MLK0_CROS8 Unreviewed; 249 AA.
AC A7MLK0;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|RuleBase:RU363068};
DE EC=3.1.2.12 {ECO:0000256|RuleBase:RU363068};
GN OrderedLocusNames=ESA_01083 {ECO:0000313|EMBL:ABU76351.1};
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU76351.1, ECO:0000313|Proteomes:UP000000260};
RN [1] {ECO:0000313|EMBL:ABU76351.1, ECO:0000313|Proteomes:UP000000260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU76351.1,
RC ECO:0000313|Proteomes:UP000000260};
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(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; CP000783; ABU76351.1; -; Genomic_DNA.
DR AlphaFoldDB; A7MLK0; -.
DR ESTHER; ents8-a7mlk0; A85-EsteraseD-FGH.
DR MEROPS; S09.A39; -.
DR KEGG; esa:ESA_01083; -.
DR HOGENOM; CLU_056472_0_0_6; -.
DR Proteomes; UP000000260; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000260};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 117
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 249 AA; 27285 MW; 235C6F0A41AA58DD CRC64;
MTFSIYLPPD AQTPPPVVWW LSGLTCSDEN FTTKAGAQRV AAELGLALVM PDTSPRGDAV
ADDAGYDLGK GAGFYLNATE TPWAAHYRMF DYLSEELPQV LAENFTLAPK AAISGHSMGG
HGALIMALKN PGRFSSVSAF APIVNPAGVP WGKKAFAAYL GDDENLWRAW DSCALMEQAS
AENAISTLID QGDNDPFFGE QLQPERLDEA ARKAGWPLTL RMQPGYDHSY YFIATFIEEH
LRFHAQHLR
//
