SFGH2_ECO24
ID SFGH2_ECO24 Reviewed; 278 AA.
AC A7ZNX7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=S-formylglutathione hydrolase YeiG;
DE Short=FGH;
DE EC=3.1.2.12;
GN Name=yeiG; OrderedLocusNames=EcE24377A_2450;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate
CC (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR EMBL; CP000800; ABV19713.1; -; Genomic_DNA.
DR RefSeq; WP_000425428.1; NC_009801.1.
DR AlphaFoldDB; A7ZNX7; -.
DR SMR; A7ZNX7; -.
DR ESTHER; ecoli-yeiG; A85-EsteraseD-FGH.
DR MEROPS; S09.A39; -.
DR EnsemblBacteria; ABV19713; ABV19713; EcE24377A_2450.
DR KEGG; ecw:EcE24377A_2450; -.
DR HOGENOM; CLU_056472_0_0_6; -.
DR OMA; TFMEDHL; -.
DR Proteomes; UP000001122; 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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR PANTHER; PTHR10061; PTHR10061; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR02821; fghA_ester_D; 1.
PE 3: Inferred from homology;
KW Hydrolase; Serine esterase.
FT CHAIN 1..278
FT /note="S-formylglutathione hydrolase YeiG"
FT /id="PRO_0000341669"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 278 AA; 31271 MW; C9D209CC172EF67F CRC64;
MEMLEEHRCF EGWQQRWRHD SSTLNCPMTF SIFLPPPRDH TPPPVLYWLS GLTCNDENFT
IKAGAQRVAA ELGIVLVMPD TSPRGEQVAN DDGYDLGQGA GFYLNATQPP WATHYRMYDY
LRDELPALVQ SQFNVSDRCA ISGHSMGGHG ALIMALKNPG KYTSVSAFAP IVNPCSVPWG
IKAFSSYLGE DKNAWLEWDS CALMYASNAQ DAIPTLIDQG DNDQFLADQL QPAVLAEAAR
QKAWPMTLRI QPGYDHSYYF IASFIEDHLR FHAQYLLK