SFGH1_ECO57
ID SFGH1_ECO57 Reviewed; 277 AA.
AC Q8X5J5; Q7AH46;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=S-formylglutathione hydrolase FrmB;
DE Short=FGH;
DE EC=3.1.2.12;
GN Name=frmB; OrderedLocusNames=Z0455, ECs0410;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG54706.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33833.1; -; Genomic_DNA.
DR PIR; B90680; B90680.
DR PIR; F85530; F85530.
DR RefSeq; NP_308437.1; NC_002695.1.
DR RefSeq; WP_000419032.1; NZ_SEKU01000007.1.
DR AlphaFoldDB; Q8X5J5; -.
DR SMR; Q8X5J5; -.
DR STRING; 155864.EDL933_0417; -.
DR ESTHER; ecoli-yaim; A85-EsteraseD-FGH.
DR MEROPS; S09.940; -.
DR EnsemblBacteria; AAG54706; AAG54706; Z0455.
DR EnsemblBacteria; BAB33833; BAB33833; ECs_0410.
DR GeneID; 914512; -.
DR KEGG; ece:Z0455; -.
DR KEGG; ecs:ECs_0410; -.
DR PATRIC; fig|386585.9.peg.505; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_056472_0_0_6; -.
DR OMA; YFWRRMA; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Serine esterase.
FT CHAIN 1..277
FT /note="S-formylglutathione hydrolase FrmB"
FT /id="PRO_0000341659"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 277 AA; 31248 MW; 53FBA7661CF4238B CRC64;
MELIEKHASF GGWQNVYRHY SASLKCEMNV GVYLPPKAAG EKLPVLYWLS GLTCNEQNFI
TKSGVQRYAA EHNIIVVAPD TSPRGSHVAD ADRYDLGQGA GFYLNATQAP WNEHYKMYDY
IRNELPDLVM NHFPATAKKS ISGHSMGGLG ALVLALRNPD EYVSVSAFSP IVSPSQVPWG
QQAFAAYLGE NKEAWLDYHP VSLISQGQRV AEIMVDQGLS DDFYAEQLRT QNLEKICQEM
NIKTLIRYHE GYDHSYYFVS SFIGEHIAYH ANKLNMR