YFCF_ECOLI
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 03-AUG-2022, entry version 142.
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; Proteobacteria; 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; P77544; -.
DR PRIDE; P77544; -.
DR EnsemblBacteria; AAC75361; AAC75361; b2301.
DR EnsemblBacteria; BAA16138; BAA16138; BAA16138.
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 PhylomeDB; P77544; -.
DR BioCyc; EcoCyc:G7193-MON; -.
DR BioCyc; MetaCyc:G7193-MON; -.
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 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 Pfam; PF14834; GST_C_4; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 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
