ID A0A1F4HQ41_9BURK Unreviewed; 286 AA.
AC A0A1F4HQ41;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=A3E25_07935 {ECO:0000313|EMBL:OGA99516.1};
OS Burkholderiales bacterium RIFCSPHIGHO2_12_FULL_69_20.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1797561 {ECO:0000313|EMBL:OGA99516.1, ECO:0000313|Proteomes:UP000177017};
RN [1] {ECO:0000313|EMBL:OGA99516.1, ECO:0000313|Proteomes:UP000177017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGA99516.1}.
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DR EMBL; MESD01000135; OGA99516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4HQ41; -.
DR Proteomes; UP000177017; 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:OGA99516.1};
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 231
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 286 AA; 30945 MW; F5B7A6E623D0C2D4 CRC64;
MIVAWELISE HASFGGVQRF HRHASAEIGL PMRFALYLPP QAQAGTPVPL LVYLAGLTCT
EETFTMKAGA QRLAAELGLA LLMPDTSPRG AGVAGEADRW DFGVGAGFYL DATQAPWATH
WRMESYLLRD LLPQVWAQAP VRQDRTGIFG HSMGGHGAMT LALRHPGVFK SLSALAPICA
PMLCPWGVKA FSGYLGEDRS RWAAHDASAL MAAQAGAPYP QGILVDQGLA DKFLAEQLHP
EAFEAACAAV GQPLLLRRHA GYDHGYYFIA SVIDDHLRHH ARQLVG
//
