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Database: UniProt
Entry: C6M2Z3_NEISI
LinkDB: C6M2Z3_NEISI
Original site: C6M2Z3_NEISI 
ID   C6M2Z3_NEISI            Unreviewed;       275 AA.
AC   C6M2Z3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   Name=fghA {ECO:0000313|EMBL:EET45257.1};
GN   ORFNames=NEISICOT_00884 {ECO:0000313|EMBL:EET45257.1};
OS   Neisseria sicca ATCC 29256.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=547045 {ECO:0000313|EMBL:EET45257.1, ECO:0000313|Proteomes:UP000005365};
RN   [1] {ECO:0000313|EMBL:EET45257.1, ECO:0000313|Proteomes:UP000005365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29256 {ECO:0000313|EMBL:EET45257.1,
RC   ECO:0000313|Proteomes:UP000005365};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2009) 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:EET45257.1}.
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DR   EMBL; ACKO02000004; EET45257.1; -; Genomic_DNA.
DR   RefSeq; WP_003756743.1; NZ_ACKO02000004.1.
DR   AlphaFoldDB; C6M2Z3; -.
DR   STRING; 490.A6J88_08105; -.
DR   ESTHER; neime-ESD; A85-EsteraseD-FGH.
DR   eggNOG; COG0627; Bacteria.
DR   Proteomes; UP000005365; 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:EET45257.1};
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   275 AA;  31344 MW;  74A29C18BA8D27B8 CRC64;
     MKLIEQHQIF GGSQQVWAHH AQTLQCEMKF AVYLPDNQEN RPLGVIYWLS GLTCTEQNFI
     TKSGFQRYAA EHQVIVVAPD TSPRGEQVPN DAAYDLGQGA GFYLNATEQP WATNYQMYDY
     ILNELPRLIE ENFPTNGKCS IMGHSMGGHG ALVLALRNQE RYQSVSAFSP ILSPSLVPWG
     EKAFSAYLGK DREKWQQYDA NSLIQQGYKV QGMRIDQGLE DEFLPTQLRT EDFIETCRAA
     NQPIDVRFHK GYDHSYYFIA SFIGEHIAYH AAFLK
//
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