ID   P73137_SYNY3            Unreviewed;       276 AA.
AC   P73137;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 120.
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   OrderedLocusNames=sll0992 {ECO:0000313|EMBL:BAA17163.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA17163.1, ECO:0000313|Proteomes:UP000001425};
RN   [1] {ECO:0000313|EMBL:BAA17163.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17163.1; -; Genomic_DNA.
DR   PIR; S75249; S75249.
DR   AlphaFoldDB; P73137; -.
DR   IntAct; P73137; 4.
DR   STRING; 1148.gene:10498025; -.
DR   ESTHER; synsp-SLL0992; A85-EsteraseD-FGH.
DR   MEROPS; S09.940; -.
DR   PaxDb; 1148-1652240; -.
DR   EnsemblBacteria; BAA17163; BAA17163; BAA17163.
DR   KEGG; syn:sll0992; -.
DR   eggNOG; COG0627; Bacteria.
DR   InParanoid; P73137; -.
DR   PhylomeDB; P73137; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0018738; F:S-formylglutathione hydrolase activity; IBA:GO_Central.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001425};
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   276 AA;  30562 MW;  E8378528A199DB15 CRC64;
     MERLEHHASF GGWQSVYSHH SAVLNCTMNV GVYLPPQATN QHCPVLYWLS GLTCTEQNAI
     TKSGLQQHAA KHGLIMVTPD TSPRGEGVTD SEDYDLGMGA GFYLNATQPP WAAHYQMHDY
     IVQELPTWIE ANFAATDARS IFGHSMGGHG ALVIALRNPG RYRSVSTFSP IVAPTQVPWG
     QKAFQAYLGD NQLSWQAWDT CALIKSAPER LPFFVDYGDA DPFLPTQLRP ELLQAACTAA
     NHPLTLRMQP GYDHSYYFIA SFIGDHMDWH GAALLN
//