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Database: UniProt
Entry: K2JBH8_9PROT
LinkDB: K2JBH8_9PROT
Original site: K2JBH8_9PROT 
ID   K2JBH8_9PROT            Unreviewed;       278 AA.
AC   K2JBH8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=P24_14184 {ECO:0000313|EMBL:EKE72112.1};
OS   Oceanibaculum indicum P24.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Oceanibaculaceae; Oceanibaculum.
OX   NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE72112.1, ECO:0000313|Proteomes:UP000006746};
RN   [1] {ECO:0000313|EMBL:EKE72112.1, ECO:0000313|Proteomes:UP000006746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P24 {ECO:0000313|EMBL:EKE72112.1,
RC   ECO:0000313|Proteomes:UP000006746};
RX   PubMed=23209207; DOI=10.1128/JB.01859-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL   J. Bacteriol. 194:6942-6942(2012).
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:EKE72112.1}.
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DR   EMBL; AMRL01000021; EKE72112.1; -; Genomic_DNA.
DR   RefSeq; WP_008945440.1; NZ_AMRL01000021.1.
DR   AlphaFoldDB; K2JBH8; -.
DR   STRING; 1207063.P24_14184; -.
DR   PATRIC; fig|1207063.3.peg.2864; -.
DR   eggNOG; COG0627; Bacteria.
DR   Proteomes; UP000006746; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006746};
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   278 AA;  30370 MW;  2ECF33AA0DE49E6D CRC64;
     MELTESNRAF GGTQQVWRHE SRTLGCAMNV AVYVPPHAEG ARLPVIYWLS GLTCTEQNFI
     TKAGAQRYAA EQGVVLVAPD TSPRGGDVAD DPAYDLGKGA GFYLNATQAP WSPHYRMYDY
     IVEELPALIE AHFPVDDRRG ITGHSMGGHG ALVIALRNPG RYKAVSAFAP IVAPSQVPWG
     RKAFAAYLGE NEAEWAAYDA TALLGGARER LPILIDQGDA DDFLEKQLKP EIFEAEAARV
     GHPLELRMQP GYGHSYYFIA SFIGDHIAHH AKALNPKP
//
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