ID A0A1B7JJ86_9GAMM Unreviewed; 276 AA.
AC A0A1B7JJ86;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|RuleBase:RU363068};
DE EC=3.1.2.12 {ECO:0000256|RuleBase:RU363068};
GN ORFNames=M998_3416 {ECO:0000313|EMBL:OAT47990.1};
OS Providencia heimbachae ATCC 35613.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1354272 {ECO:0000313|EMBL:OAT47990.1, ECO:0000313|Proteomes:UP000078224};
RN [1] {ECO:0000313|EMBL:OAT47990.1, ECO:0000313|Proteomes:UP000078224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35613 {ECO:0000313|EMBL:OAT47990.1,
RC ECO:0000313|Proteomes:UP000078224};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (APR-2016) 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:OAT47990.1}.
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DR EMBL; LXEW01000048; OAT47990.1; -; Genomic_DNA.
DR RefSeq; WP_068909957.1; NZ_LXEW01000048.1.
DR AlphaFoldDB; A0A1B7JJ86; -.
DR GeneID; 79027408; -.
DR PATRIC; fig|1354272.4.peg.3495; -.
DR OrthoDB; 9782200at2; -.
DR Proteomes; UP000078224; 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:OAT47990.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078224};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 254
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 276 AA; 30738 MW; 2BB4F5CE4AD2DC8E CRC64;
MERIERHACF SGWQDVYQHQ SEVLGCTMKF AAYLPPQAEK NHCPVIYWLS GLTCNEQNFI
TKAGAQQFAA QHGIILIVPD TSPRGEQVAD DEAYDLGQGA GFYLNATQAP WNRHYHMYDY
IVSELPSLVE ANLPASNKRA ISGHSMGGHG ALMIGLRNAA RYCSLSAFAP IVAPSQVPWG
QKAFSAYLGE ETATWQEYDS VHLLDNATAI PPILVDVGTG DAFYHDQLKP ELLSDVCDKQ
QHNYTLNLRD GYDHSYYFIS SFIGEHIAFH AQHLKG
//
