(data stored in ACNUC7421 zone)

SWISSPROT: SFGH_PARDP

ID   SFGH_PARDP              Reviewed;         279 AA.
AC   A1AXZ2; Q51671;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=S-formylglutathione hydrolase;
DE            Short=FGH;
DE            EC=3.1.2.12;
GN   Name=fghA; OrderedLocusNames=Pden_0019;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS A FORMYLGLUTATHIONE
RP   HYDROLASE.
RX   PubMed=8892832; DOI=10.1128/jb.178.21.6296-6299.1996;
RA   Harms N., Ras J., Reijnders W.N.M., van Spanning R.J.M.,
RA   Stouthamer A.H.;
RT   "S-formylglutathione hydrolase of Paracoccus denitrificans is
RT   homologous to human esterase D: a universal pathway for formaldehyde
RT   detoxification?";
RL   J. Bacteriol. 178:6296-6299(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC       formaldehyde. Hydrolyzes S-formylglutathione to glutathione and
CC       formate (Probable). {ECO:0000305|PubMed:8892832}.
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;
CC   -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
DR   EMBL; U34346; AAC44554.1; -; Genomic_DNA.
DR   EMBL; CP000489; ABL68136.1; -; Genomic_DNA.
DR   RefSeq; WP_011746369.1; NC_008686.1.
DR   SMR; A1AXZ2; -.
DR   STRING; 318586.Pden_0019; -.
DR   ESTHER; parde-FGHA; A85-EsteraseD-FGH.
DR   MEROPS; S09.A38; -.
DR   PRIDE; A1AXZ2; -.
DR   EnsemblBacteria; ABL68136; ABL68136; Pden_0019.
DR   KEGG; pde:Pden_0019; -.
DR   eggNOG; ENOG4105C4W; Bacteria.
DR   eggNOG; COG0627; LUCA.
DR   HOGENOM; HOG000263929; -.
DR   KO; K01070; -.
DR   OMA; EDHLRHH; -.
DR   BioCyc; PDEN318586:G1GW1-19-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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   1: Evidence at protein level;
DR   PRODOM; A1AXZ2.
DR   SWISS-2DPAGE; A1AXZ2.
KW   Complete proteome; Hydrolase; Reference proteome; Serine esterase.
FT   CHAIN         1    279       S-formylglutathione hydrolase.
FT                                /FTId=PRO_0000341679.
FT   ACT_SITE    150    150       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    226    226       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    258    258       Charge relay system. {ECO:0000250}.
FT   CONFLICT    272    277       RWHAER -> PLARGA (in Ref. 1; AAC44554).
FT                                {ECO:0000305}.
SQ   SEQUENCE   279 AA;  31276 MW;  A980EB9D179EDB26 CRC64;
     MTLAYETVSE NRSFGGIQGV YRHQSQATGT PMTFAIYLPP DARHGKVPVL WYLSGLTCTH
     ENAMTKAGAQ EWAAEYGIAV IFPDTSPRGE GVANDETYDL GQGAGFYVDA TEAPWAPHFR
     MWHYVTHELP ELVFNNFPLD REAQGITGHS MGGHGALTIA MTFPERYRSV SAFAPIAHPS
     ESDWGRKQFA AYLGDDKAAW KRHDSTILMR EKGYPGEVLI DQGASDQFLD LLKPEALAHA
     MAERRQPGTF RMQQGYDHSY FFVQSFMADH IRWHAERLG
//

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