(data stored in SCRATCH zone)

SWISSPROT: C8U248_ECO10

ID   C8U248_ECO10            Unreviewed;       277 AA.
AC   C8U248;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 48.
DE   RecName: Full=S-formylglutathione hydrolase {ECO:0000256|RuleBase:RU363068};
DE            EC=3.1.2.12 {ECO:0000256|RuleBase:RU363068};
GN   Name=frmB {ECO:0000313|EMBL:BAI29206.1};
GN   OrderedLocusNames=ECO103_0337 {ECO:0000313|EMBL:BAI29206.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29206.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29206.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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;
CC         EC=3.1.2.12; Evidence={ECO:0000256|RuleBase:RU363068};
CC   -!- SIMILARITY: Belongs to the esterase D family.
CC       {ECO:0000256|RuleBase:RU363068}.
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DR   EMBL; AP010958; BAI29206.1; -; Genomic_DNA.
DR   RefSeq; WP_000419051.1; NC_013353.1.
DR   ESTHER; ecoli-yaim; A85-EsteraseD-FGH.
DR   EnsemblBacteria; BAI29206; BAI29206; ECO103_0337.
DR   KEGG; eoh:ECO103_0337; -.
DR   HOGENOM; HOG000263929; -.
DR   KO; K01070; -.
DR   OMA; WAPHYRM; -.
DR   BioCyc; ECOL585395:ECO103_RS01760-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U248.
DR   SWISS-2DPAGE; C8U248.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000256|RuleBase:RU363068};
KW   Serine esterase {ECO:0000256|RuleBase:RU363068}.
SQ   SEQUENCE   277 AA;  31398 MW;  D51B2472CFA8CA9A CRC64;
     MELIEKHASF GGWQNVYRHY SQSLKCEMNV GVYLPPKAAN EKLPVLYWLS GLTCNEQNFI
     TKSGMQRYAA EHNIIVVAPD TSPRGSHVAD ADRYDLGQGA GFYLNATQAP WNEHYKMYDY
     IRNELPDLVM QHFPATTRKS ISGHSMGGLG ALVLALRNPD EYVSVSAFSP IVSPSQVPWG
     QQAFAAYLGE NKDAWLNYDP VSLISQGQRV AEIMVDQGLS DDFYAEQLRT PNLEKICQEM
     NIKTLIRYHE GYDHSYYFVS SFIGEHIAYH ANKLNMR
//

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