ID A0A2Y9NCB0_DELLE Unreviewed; 282 AA.
AC A0A2Y9NCB0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|ARBA:ARBA00016774, ECO:0000256|RuleBase:RU363068};
DE EC=3.1.2.12 {ECO:0000256|ARBA:ARBA00012479, ECO:0000256|RuleBase:RU363068};
GN Name=ESD {ECO:0000313|RefSeq:XP_022430559.1,
GN ECO:0000313|RefSeq:XP_022430560.1, ECO:0000313|RefSeq:XP_022430561.1,
GN ECO:0000313|RefSeq:XP_022430562.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022430561.1};
RN [1] {ECO:0000313|RefSeq:XP_022430559.1, ECO:0000313|RefSeq:XP_022430560.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022430559.1,
RC ECO:0000313|RefSeq:XP_022430560.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde. {ECO:0000256|ARBA:ARBA00002608,
CC 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|RuleBase:RU363068};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}.
CC -!- SIMILARITY: Belongs to the esterase D family.
CC {ECO:0000256|ARBA:ARBA00005622, ECO:0000256|RuleBase:RU363068}.
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DR RefSeq; XP_022430559.1; XM_022574851.2.
DR RefSeq; XP_022430560.1; XM_022574852.2.
DR RefSeq; XP_022430561.1; XM_022574853.2.
DR RefSeq; XP_022430562.1; XM_022574854.2.
DR Ensembl; ENSDLET00000010004; ENSDLEP00000009064; ENSDLEG00000006636.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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 Cytoplasm {ECO:0000256|RuleBase:RU363068};
KW Hydrolase {ECO:0000256|RuleBase:RU363068,
KW ECO:0000313|RefSeq:XP_022430559.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
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 226
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 282 AA; 31418 MW; 0A083CA9610E0918 CRC64;
MALKQISSNK CFGGLQKVFE HDSVELKCKM KFAIYLPPKA ETGKCPALYW LSGLTCTEQN
FISKSGYHQA ASEHGLVVIA PDTSPRGCNI KGEDETWDFG SGAGFYVDAT EDPWKTNYRM
YSYVTEELPQ LINTNFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL
CPWGKKAFSG YLGTDQSKWE AYDATHLVKA CPGTQLDILI DQGKDDQFLS DGQLLPDNFI
AACTEKKIPV VFRLQEGYDH SYYFIATFIT DHIRHHAKYL NA
//
