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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
 
 
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