(data stored in ACNUC7421 zone)

SWISSPROT: 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   07-JUN-2017, entry version 93.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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
CC       formate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-formylglutathione + H(2)O = glutathione +
CC       formate.
CC   -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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_LPWC02000002.1.
DR   ProteinModelPortal; Q8X5J5; -.
DR   SMR; Q8X5J5; -.
DR   STRING; 155864.Z0455; -.
DR   ESTHER; ecoli-yaim; A85-EsteraseD-FGH.
DR   EnsemblBacteria; AAG54706; AAG54706; Z0455.
DR   EnsemblBacteria; BAB33833; BAB33833; BAB33833.
DR   GeneID; 914512; -.
DR   KEGG; ece:Z0455; -.
DR   KEGG; ecs:ECs0410; -.
DR   PATRIC; fig|386585.9.peg.505; -.
DR   eggNOG; ENOG4105C4W; Bacteria.
DR   eggNOG; COG0627; LUCA.
DR   HOGENOM; HOG000263929; -.
DR   KO; K01070; -.
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_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; Q8X5J5.
DR   SWISS-2DPAGE; Q8X5J5.
KW   Complete proteome; Hydrolase; Serine esterase.
FT   CHAIN         1    277       S-formylglutathione hydrolase FrmB.
FT                                /FTId=PRO_0000341659.
FT   ACT_SITE    145    145       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    221    221       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    254    254       Charge relay system. {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
//

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