ID   YFCF_ECOLI              Reviewed;         214 AA.
AC   P77544;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Glutathione S-transferase YfcF;
DE            EC=2.5.1.18;
GN   Name=yfcF; OrderedLocusNames=b2301, JW2298;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION IN DEFENSE AGAINST OXIDATIVE STRESS, GSH TRANSFERASE ACTIVITY,
RP   PEROXIDASE ACTIVITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-10 AND
RP   SER-16.
RC   STRAIN=K12;
RX   PubMed=17018556; DOI=10.1093/jb/mvj199;
RA   Kanai T., Takahashi K., Inoue H.;
RT   "Three distinct-type glutathione S-transferases from Escherichia coli
RT   important for defense against oxidative stress.";
RL   J. Biochem. 140:703-711(2006).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RC   STRAIN=K12;
RG   Joint center for structural genomics (JCSG);
RT   "Crystal structure of glutathione S-transferase (NP_416804.1) from
RT   Escherichia coli K12 at 1.85 A resolution.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Exhibits glutathione (GSH) S-transferase activity toward 1-
CC       chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1%
CC       of that of GstA. Also displays a GSH-dependent peroxidase activity
CC       toward cumene hydroperoxide. Is involved in defense against oxidative
CC       stress, probably via its peroxidase activity.
CC       {ECO:0000269|PubMed:17018556}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000269|PubMed:17018556};
CC   -!- ACTIVITY REGULATION: GSH transferase activity is inhibited by S-hexyl
CC       glutathione. {ECO:0000269|PubMed:17018556}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.24 mM for glutathione {ECO:0000269|PubMed:17018556};
CC         KM=1.1 mM for 1-chloro-2,4-dinitrobenzene
CC         {ECO:0000269|PubMed:17018556};
CC         Note=kcat is 0.11 sec(-1) for the GSH transferase reaction with CDNB
CC         as substrate.;
CC       pH dependence:
CC         Activity decreases as pH is lowered from neutral to acidic.
CC         {ECO:0000269|PubMed:17018556};
CC   -!- DISRUPTION PHENOTYPE: Deletion of yfcF decreases the resistance of the
CC       bacteria to hydrogen peroxide. {ECO:0000269|PubMed:17018556}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; U00096; AAC75361.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16138.1; -; Genomic_DNA.
DR   PIR; C65002; C65002.
DR   RefSeq; NP_416804.1; NC_000913.3.
DR   RefSeq; WP_000042442.1; NZ_LN832404.1.
DR   PDB; 3BBY; X-ray; 1.85 A; A=1-214.
DR   PDBsum; 3BBY; -.
DR   AlphaFoldDB; P77544; -.
DR   SMR; P77544; -.
DR   BioGRID; 4260516; 12.
DR   IntAct; P77544; 3.
DR   STRING; 511145.b2301; -.
DR   jPOST; P77544; -.
DR   PaxDb; 511145-b2301; -.
DR   EnsemblBacteria; AAC75361; AAC75361; b2301.
DR   GeneID; 75205653; -.
DR   GeneID; 946749; -.
DR   KEGG; ecj:JW2298; -.
DR   KEGG; eco:b2301; -.
DR   PATRIC; fig|1411691.4.peg.4433; -.
DR   EchoBASE; EB3862; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_17_0_6; -.
DR   InParanoid; P77544; -.
DR   OMA; FSPYVMS; -.
DR   OrthoDB; 8857552at2; -.
DR   PhylomeDB; P77544; -.
DR   BioCyc; EcoCyc:G7193-MONOMER; -.
DR   BioCyc; MetaCyc:G7193-MONOMER; -.
DR   EvolutionaryTrace; P77544; -.
DR   PRO; PR:P77544; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:EcoCyc.
DR   GO; GO:0016034; F:maleylacetoacetate isomerase activity; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:EcoCyc.
DR   CDD; cd03195; GST_C_4; 1.
DR   CDD; cd00570; GST_N_family; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR034338; GST_4_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR   PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR   Pfam; PF14834; GST_C_4; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Oxidoreductase; Peroxidase; Reference proteome; Transferase.
FT   CHAIN           1..214
FT                   /note="Glutathione S-transferase YfcF"
FT                   /id="PRO_0000186015"
FT   DOMAIN          6..87
FT                   /note="GST N-terminal"
FT   DOMAIN          95..214
FT                   /note="GST C-terminal"
FT   MUTAGEN         10
FT                   /note="S->A: Nearly no effect on GSH transferase activity."
FT                   /evidence="ECO:0000269|PubMed:17018556"
FT   MUTAGEN         16
FT                   /note="S->G: 2% of wild-type GSH transferase activity."
FT                   /evidence="ECO:0000269|PubMed:17018556"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   HELIX           17..29
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   HELIX           72..82
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   TURN            85..87
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   HELIX           96..111
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   HELIX           114..119
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   HELIX           123..126
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   HELIX           136..152
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   TURN            153..155
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   HELIX           166..179
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   HELIX           187..197
FT                   /evidence="ECO:0007829|PDB:3BBY"
FT   HELIX           200..210
FT                   /evidence="ECO:0007829|PDB:3BBY"
SQ   SEQUENCE   214 AA;  24326 MW;  6B2308D403DA3077 CRC64;
     MSKPAITLWS DAHFFSPYVL SAWVALQEKG LSFHIKTIDL DSGEHLQPTW QGYGQTRRVP
     LLQIDDFELS ESSAIAEYLE DRFAPPTWER IYPLDLENRA RARQIQAWLR SDLMPIREER
     PTDVVFAGAK KAPLTAEGKA SAEKLFAMAE HLLVLGQPNL FGEWCIADTD LALMINRLVL
     HGDEVPERLV DYATFQWQRA SVQRFIALSA KQSG
//