ID E6LE54_ENTI1 Unreviewed; 265 AA.
AC E6LE54;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 Name=fghA {ECO:0000313|EMBL:EFU74509.1};
GN ORFNames=HMPREF9088_0644 {ECO:0000313|EMBL:EFU74509.1};
OS Enterococcus italicus (strain DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=888064 {ECO:0000313|EMBL:EFU74509.1, ECO:0000313|Proteomes:UP000010296};
RN [1] {ECO:0000313|EMBL:EFU74509.1, ECO:0000313|Proteomes:UP000010296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5
RC {ECO:0000313|Proteomes:UP000010296};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFU74509.1}.
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DR EMBL; AEPV01000024; EFU74509.1; -; Genomic_DNA.
DR AlphaFoldDB; E6LE54; -.
DR STRING; 888064.HMPREF9088_0644; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_056472_0_1_9; -.
DR Proteomes; UP000010296; Unassembled WGS sequence.
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:EFU74509.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010296};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
SQ SEQUENCE 265 AA; 29765 MW; E2FA02EFB876619F CRC64;
MEENEMRIER IEQHQAFGGQ QLKYRHHSDS LHCSMTFSLY LPKPSASPTS LIWWLSGLTC
TDDNFSQKGA FQKYASQENV AFLIPDTSPR GELPDDEAWD LGQGAGFYVN ATCEPWKQNY
QMYDYLVNEL PGIVYDLIPN YSGKESIMGH SMGGHGALIV GLKQPERFSA ISAFAPILNP
SNVPWGKKAF TAYLGTDETT WKTWDATELL QKVGEIHPPI LLTQGTADPF YAVQLNETAF
LANVKDTDEQ VRYEKKKGMT IVISP
//
