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Database: UniProt
Entry: A0A2S4HKU7_9GAMM
LinkDB: A0A2S4HKU7_9GAMM
Original site: A0A2S4HKU7_9GAMM 
ID   A0A2S4HKU7_9GAMM        Unreviewed;       286 AA.
AC   A0A2S4HKU7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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:POP54500.1};
GN   ORFNames=C0068_01565 {ECO:0000313|EMBL:POP54500.1};
OS   Marortus luteolus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Marortus.
OX   NCBI_TaxID=2067667 {ECO:0000313|EMBL:POP54500.1, ECO:0000313|Proteomes:UP000237222};
RN   [1] {ECO:0000313|EMBL:POP54500.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZX-21 {ECO:0000313|EMBL:POP54500.1};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) 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:POP54500.1}.
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DR   EMBL; PQGG01000005; POP54500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4HKU7; -.
DR   OrthoDB; 9782200at2; -.
DR   Proteomes; UP000237222; 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:POP54500.1};
KW   Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT   ACT_SITE        147
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        223
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT   ACT_SITE        256
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ   SEQUENCE   286 AA;  32347 MW;  A9CBB1171EC9696B CRC64;
     MKIHSQHLCF GGTQYYCQHS SIATGTAMNF SVFLPYQARI QELPALYYLP SLNCTEETFM
     IKAGAQRIAA ELGMILVSSD TSPRGLAFPS ESDHRDLGVG AGFYLDATKE PWAKHYRMGS
     YINLELPTYI EKHFPACNKY RGIFGHSMGG HGALVTALRN PDRWHSVSAF APICNPSQVP
     WGEKAFTNYL GDNQLHWQDW DASLLLAKSA YPGDILIDQG LDDEFLQREL RPDALEKAAV
     TSHRKLNLRR HLGYGHDYYF IQSFIDDHLQ HHARQLQRSV KACVGR
//
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