ID A0A1X3DEP8_9NEIS Unreviewed; 280 AA.
AC A0A1X3DEP8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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=BWD09_02605 {ECO:0000313|EMBL:OSI18306.1};
OS Neisseria dentiae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=194197 {ECO:0000313|EMBL:OSI18306.1, ECO:0000313|Proteomes:UP000193118};
RN [1] {ECO:0000313|Proteomes:UP000193118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19151 {ECO:0000313|Proteomes:UP000193118};
RA Wolfgang W.J., Cole J., Wroblewski D., Mcginnis J., Musser K.A.;
RL Submitted (JAN-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}.
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:OSI18306.1}.
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DR EMBL; MTBO01000003; OSI18306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X3DEP8; -.
DR STRING; 194197.BWD09_02605; -.
DR OrthoDB; 9782200at2; -.
DR Proteomes; UP000193118; 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:OSI18306.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193118};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 280 AA; 30741 MW; DE443ED2987AF14E CRC64;
MSVLTLISRN KMFNGSHERY RHFSDANQCE MTFAVYLPPQ ALQGYRVPVL YWLSGLTCTD
ENFSTKSGAQ RFAAQWGIAL VMPDTSPRGA GVADDDAYNL GQGAGFYLDA TRAPWAANYQ
MYSYIVHELP ALIEAHFPVN GQRSIAGHSM GGHGALQIAL KNPGRYAAVS AFAPIANPSQ
TPWGQKAFAA YLGDNPELWA QYDSTELAKT AVKKLPVLID QGSADEFYPH DLQAQAFVNA
ARGNGFNVQF NLREGYGHGY YFIATFIDSH IEFHADALGL
//
