ID L5MHQ9_MYODS Unreviewed; 469 AA.
AC L5MHQ9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=MDA_GLEAN10010742 {ECO:0000313|EMBL:ELK38169.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK38169.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SPIN/STSY family.
CC {ECO:0000256|ARBA:ARBA00009467}.
CC -!- SIMILARITY: Belongs to the esterase D family.
CC {ECO:0000256|ARBA:ARBA00005622, ECO:0000256|RuleBase:RU363068}.
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DR EMBL; KB099365; ELK38169.1; -; Genomic_DNA.
DR AlphaFoldDB; L5MHQ9; -.
DR MEROPS; S09.990; -.
DR eggNOG; ENOG502QRYD; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
DR GO; GO:0007276; P:gamete generation; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.80.10.70; Spindlin/Ssty; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR InterPro; IPR003671; SPIN/Ssty.
DR InterPro; IPR042567; SPIN/Ssty_sf.
DR NCBIfam; TIGR02821; fghA_ester_D; 1.
DR PANTHER; PTHR10405; SPINDLIN; 1.
DR PANTHER; PTHR10405:SF15; SPINDLIN-1; 1.
DR Pfam; PF00756; Esterase; 1.
DR Pfam; PF02513; Spin-Ssty; 3.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cytoplasm {ECO:0000256|RuleBase:RU363068};
KW Hydrolase {ECO:0000256|RuleBase:RU363068};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Serine esterase {ECO:0000256|RuleBase:RU363068}.
FT REGION 235..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 52451 MW; EF84E74417511706 CRC64;
MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAIYLPPKA ETGKCPALYW LSGLTCTEQN
FISKSGYHQA ASEHGLVVIA PDTSPRGYNI KGEDESWDFG TGAGFYVDAT EHPWKTNYRM
YSYVTEELPQ LINANFPVDP QRMPIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL
CPWGKKAFNG YLGADQSKWK AYDATHLVKS FPGSQLDILI DQGKGHAGVS ASMMKKRTSH
KKHRSSVGPS KPVSQPRRNI VGCRIQHGWK EGSGPVTQWK GTVLDQVPVN PSLYLIKYDG
FDCVYGLELN KDERVSALEV LPDRVATSRI SDAHLADTMI GKAVEHMFET EDGSKDEWRG
MVLARAPIMN TWFYITYEKD PVLYMYQLLD DYKEGDLRIM PDSNDSPPAE REPGEVVDSL
VGKQVEYAKE DGSKRTGMVI HQVEAKPSVY FIKFDDDFHI YVYDLVKTS
//
