ID E6XJQ6_SHEP2 Unreviewed; 280 AA.
AC E6XJQ6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|RuleBase:RU363068};
DE EC=3.1.2.12 {ECO:0000256|RuleBase:RU363068};
GN OrderedLocusNames=Sput200_1837 {ECO:0000313|EMBL:ADV54293.1};
OS Shewanella putrefaciens (strain 200).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV54293.1, ECO:0000313|Proteomes:UP000008209};
RN [1] {ECO:0000313|EMBL:ADV54293.1, ECO:0000313|Proteomes:UP000008209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200 {ECO:0000313|EMBL:ADV54293.1,
RC ECO:0000313|Proteomes:UP000008209};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Kolker E., Lawrence C., McCue L.A., DiChristina T., Nealson K.,
RA Fredrickson J.K., Woyke T.;
RT "Complete sequence of Shewanella putrefaciens 200.";
RL Submitted (JAN-2011) 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}.
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DR EMBL; CP002457; ADV54293.1; -; Genomic_DNA.
DR AlphaFoldDB; E6XJQ6; -.
DR KEGG; shp:Sput200_1837; -.
DR PATRIC; fig|399804.5.peg.1894; -.
DR HOGENOM; CLU_056472_0_0_6; -.
DR OrthoDB; 9782200at2; -.
DR Proteomes; UP000008209; 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:ADV54293.1};
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; 31466 MW; F956BD7E14325858 CRC64;
MTIENISCNK SFGGWHKQYR HQSQSLNCEM RFAIYLPPEA VNKPVPVLYW LSGLTCTDEN
FMQKAGAQRM AAELGMAIVA PDTSPRGDDV PDAADKAYDL GLGAGFYLNA TKAPWNRHYK
MYDYIVHELP NLIEAHFPVT TQRAISGHSM GGHGALVIGL SNPHRYSSIS AFSPISNPSN
APWGIKAFSE YLGENREHWR QYDACELLKL AISEVPVLID QGEADSFLDT QLMPQSLVDI
AHTKGYPLDV RMQAGYDHSY YFIASFIEEH LKFHSLYFKP
//
