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Database: UniProt
Entry: B4EA00_BURCJ
LinkDB: B4EA00_BURCJ
Original site: B4EA00_BURCJ 
ID   B4EA00_BURCJ            Unreviewed;       282 AA.
AC   B4EA00;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=S-formylglutathione hydrolase {ECO:0000256|ARBA:ARBA00012479, ECO:0000256|RuleBase:RU363068};
DE            EC=3.1.2.12 {ECO:0000256|ARBA:ARBA00012479, ECO:0000256|RuleBase:RU363068};
GN   ORFNames=BCAL2816 {ECO:0000313|EMBL:CAR53116.1};
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR53116.1, ECO:0000313|Proteomes:UP000001035};
RN   [1] {ECO:0000313|EMBL:CAR53116.1, ECO:0000313|Proteomes:UP000001035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC   CF5610 {ECO:0000313|Proteomes:UP000001035};
RX   PubMed=18931103; DOI=10.1128/JB.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(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; EC=3.1.2.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00000080,
CC         ECO:0000256|RuleBase:RU363068};
CC   -!- SIMILARITY: Belongs to the esterase D family.
CC       {ECO:0000256|ARBA:ARBA00005622, ECO:0000256|RuleBase:RU363068}.
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DR   EMBL; AM747720; CAR53116.1; -; Genomic_DNA.
DR   RefSeq; WP_006483753.1; NC_011000.1.
DR   AlphaFoldDB; B4EA00; -.
DR   ESTHER; burcm-q0bcb6; A85-EsteraseD-FGH.
DR   MEROPS; S09.990; -.
DR   KEGG; bcj:BCAL2816; -.
DR   eggNOG; COG0627; Bacteria.
DR   HOGENOM; CLU_056472_0_0_4; -.
DR   BioCyc; BCEN216591:G1G1V-3117-MONOMER; -.
DR   Proteomes; UP000001035; 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; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000801; Esterase-like.
DR   InterPro; IPR014186; S-formylglutathione_hydrol.
DR   NCBIfam; TIGR02821; fghA_ester_D; 1.
DR   PANTHER; PTHR10061; S-FORMYLGLUTATHIONE HYDROLASE; 1.
DR   PANTHER; PTHR10061:SF0; S-FORMYLGLUTATHIONE HYDROLASE; 1.
DR   Pfam; PF00756; Esterase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU363068, ECO:0000313|EMBL:CAR53116.1};
KW   Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        227
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        260
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ   SEQUENCE   282 AA;  30343 MW;  25A6053F78DB8666 CRC64;
     MLELVSSHAC HGGEQRFYRH DSAVIGLPMK FSVYLPPQAA HGRVPALFYL AGLTSTDETF
     AIKAGAQQYA AQHGIALVMP DTSPRGAGVP GETDAWDFGV GAGFYVDATE APWSTHYRME
     SYVTGELREL VAAELPIDGA RLGIFGHSMG GHGALTLALR HPGLYRSVSA FAPIAAPTRC
     PWGEKAFSGY LGADRDAWKA HDASELVARA DAPKFADGIL VDQGLADQFL ANQLNPDVFE
     AACAKAGQPL TLRRHPGYDH GYYFISTFIA DHLAHHARVL AR
//
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