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Database: UniProt
Entry: A0A1Y6CFC0_9ALTE
LinkDB: A0A1Y6CFC0_9ALTE
Original site: A0A1Y6CFC0_9ALTE 
ID   A0A1Y6CFC0_9ALTE        Unreviewed;       278 AA.
AC   A0A1Y6CFC0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=S-formylglutathione hydrolase {ECO:0000256|RuleBase:RU363068};
DE            EC=3.1.2.12 {ECO:0000256|RuleBase:RU363068};
GN   ORFNames=SAMN02745866_03349 {ECO:0000313|EMBL:SMF52675.1};
OS   Alteromonadaceae bacterium Bs31.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae.
OX   NCBI_TaxID=1304903 {ECO:0000313|EMBL:SMF52675.1, ECO:0000313|Proteomes:UP000192901};
RN   [1] {ECO:0000313|EMBL:SMF52675.1, ECO:0000313|Proteomes:UP000192901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bs31 {ECO:0000313|EMBL:SMF52675.1,
RC   ECO:0000313|Proteomes:UP000192901};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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}.
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DR   EMBL; FXAI01000009; SMF52675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6CFC0; -.
DR   STRING; 1304903.SAMN02745866_03349; -.
DR   OrthoDB; 9782200at2; -.
DR   Proteomes; UP000192901; 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:SF1; S-FORMYLGLUTATHIONE HYDROLASE YEIG; 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:SMF52675.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192901};
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        224
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        257
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ   SEQUENCE   278 AA;  30945 MW;  DCE5D26A0A9FAF46 CRC64;
     MEKVDKHICF GGEQLQYKHR SSVLNCDMHF SVYLPPQAKT MTVPVLYWLS GLTCTDQNFV
     TKAGAQKYAA KHGIAIVAPD TSPRGEGVPD DKDASYDFGL GAGFYLNATL SPWAQHYNMY
     DYVVKELPEL ISQHFPVQRG RTAISGHSMG GHGALSIALK NPGVYTSVSA FSPIVSPSQC
     PWGEKAYTGY LGEDRKAWAQ YDACLLLPKA KEKLPVLVDQ GSADDFLYEQ LNTHLLFDAS
     EQSSYPMTIR MQPGYDHSYF FIASFIGEHI RFHASHLF
//
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