(data stored in ACNUC7421 zone)

SWISSPROT: SFGH1_ECOL5

ID   SFGH1_ECOL5             Reviewed;         277 AA.
AC   Q0TKS8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 77.
DE   RecName: Full=S-formylglutathione hydrolase FrmB;
DE            Short=FGH;
DE            EC=3.1.2.12;
GN   Name=frmB; OrderedLocusNames=ECP_0420;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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}.
DR   EMBL; CP000247; ABG68453.1; -; Genomic_DNA.
DR   RefSeq; WP_000419066.1; NC_008253.1.
DR   SMR; Q0TKS8; -.
DR   ESTHER; ecoli-yaim; A85-EsteraseD-FGH.
DR   EnsemblBacteria; ABG68453; ABG68453; ECP_0420.
DR   KEGG; ecp:ECP_0420; -.
DR   eggNOG; ENOG4105C4W; Bacteria.
DR   eggNOG; COG0627; LUCA.
DR   HOGENOM; HOG000263929; -.
DR   KO; K01070; -.
DR   OMA; GQHFRAD; -.
DR   BioCyc; ECOL362663:G1G5S-440-MONOMER; -.
DR   Proteomes; UP000009182; 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_put.
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;
DR   PRODOM; Q0TKS8.
DR   SWISS-2DPAGE; Q0TKS8.
KW   Hydrolase; Serine esterase.
FT   CHAIN           1..277
FT                   /note="S-formylglutathione hydrolase FrmB"
FT                   /id="PRO_0000341662"
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;  31407 MW;  E66D0A7148048D7B CRC64;
     MELIEKHASF GGWQNVYRHY SQSLKCEMNV GVYLPPKAEN EKLPVLYWLS GLTCNEQNFI
     TKSGMQRYAA EHNIIVVAPD TSPRGSHVAD ADRYDLGQGA GFYLNATQAP WNEHYKMYDY
     IRNELPNLVM HHFPATARKS ISGHSMGGLG ALVLALRNPD EYASVSAFSP IVSPSQVPWG
     QQAFAAYLGE NKDAWLDYDP VSLISQGQRV AEIMVDQGLS DDFYAEQLRT PNLEKICQEM
     NIKTLIRYHE GYDHSYYFVS SFIGEHIAYH ANKLNMR
//

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