SFGH2_SHIF8
ID SFGH2_SHIF8 Reviewed; 278 AA.
AC Q0T2X0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=S-formylglutathione hydrolase YeiG;
DE Short=FGH;
DE EC=3.1.2.12;
GN Name=yeiG; OrderedLocusNames=SFV_2229;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate
CC (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR EMBL; CP000266; ABF04345.1; -; Genomic_DNA.
DR RefSeq; WP_000425441.1; NC_008258.1.
DR AlphaFoldDB; Q0T2X0; -.
DR SMR; Q0T2X0; -.
DR ESTHER; shiss-yeiG; A85-EsteraseD-FGH.
DR EnsemblBacteria; ABF04345; ABF04345; SFV_2229.
DR GeneID; 58388973; -.
DR KEGG; sfv:SFV_2229; -.
DR HOGENOM; CLU_056472_0_0_6; -.
DR OMA; TFMEDHL; -.
DR BioCyc; SFLE373384:SFV_RS12485-MON; -.
DR Proteomes; UP000000659; 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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR PANTHER; PTHR10061; PTHR10061; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR02821; fghA_ester_D; 1.
PE 3: Inferred from homology;
KW Hydrolase; Serine esterase.
FT CHAIN 1..278
FT /note="S-formylglutathione hydrolase YeiG"
FT /id="PRO_0000341677"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 278 AA; 31273 MW; 2C3D7FC905983902 CRC64;
MEMLEEHRCF EGWQQRWRHD SSTLNCPMTF SIFLPPPRDH TPPPVLYWLS GLTCNDENFT
TKAGAQRVAA ELGIVLVMPD TSPRGEKVAN DDGYDLGQGA GFYLNATQPP WATHYRMYDY
LRDELPALVQ SQFNVSDRCA ISGHSMGGHG ALIMALKNPG KYTSVSAFAP IVNPCSVPWG
IKAFSTYLGE DKNAWLEWDS CALMYASNAQ DAIPTLIDQG DNDQFLADQL QPAVLAEAAR
QKAWPMTLRI QPGYDHSYYF IASFIEDHLR FHAQYLLK