ID G2J1L2_PSEUL Unreviewed; 283 AA.
AC G2J1L2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|RuleBase:RU363068};
DE EC=3.1.2.12 {ECO:0000256|RuleBase:RU363068};
GN OrderedLocusNames=NH8B_1368 {ECO:0000313|EMBL:BAK76190.1};
OS Pseudogulbenkiania sp. (strain NH8B).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK76190.1, ECO:0000313|Proteomes:UP000001274};
RN [1] {ECO:0000313|Proteomes:UP000001274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX PubMed=22038961; DOI=10.1128/JB.06127-11;
RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT Pseudogulbenkiania sp. strain NH8B.";
RL J. Bacteriol. 193:6395-6396(2011).
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; AP012224; BAK76190.1; -; Genomic_DNA.
DR AlphaFoldDB; G2J1L2; -.
DR STRING; 748280.NH8B_1368; -.
DR MEROPS; S09.A39; -.
DR KEGG; pse:NH8B_1368; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_056472_0_0_4; -.
DR OrthoDB; 9782200at2; -.
DR Proteomes; UP000001274; Chromosome.
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:BAK76190.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001274};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 261
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 283 AA; 31153 MW; 50FA822F73C88875 CRC64;
MTDTLKLVSC NKSFGGWHKR YAHHSSTLNC TMHFSIYLPP SANPEARVPV LYWLSGLTCT
DENFMQKAGA QRVAAELGIA LVAPDTSPRG EGVPGDPAGG WDFGLGAGFY LNATQAPWSS
HYRMHDYVVH ELPTLIEAVF PVDGRRAVSG HSMGGHGALV CALRNPGRYR SVSAFAPIAN
PVNCPWGEKA FNGYLGPERS RWREWDASLL LASAEERLPL LVDQGDADDF LATQLHPEAL
RQAADKAGYP LTLRLQPGYD HSYYFIASFI EEHLRFHATA LQD
//