YFCG_ECOLI
ID YFCG_ECOLI Reviewed; 215 AA.
AC P77526;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Disulfide-bond oxidoreductase YfcG;
DE EC=1.8.4.-;
DE AltName: Full=GSH-dependent disulfide-bond oxidoreductase YfcG;
DE AltName: Full=GST N1-1;
DE AltName: Full=GST-like protein YfcG;
DE AltName: Full=Organic hydroperoxidase;
DE EC=1.11.1.-;
GN Name=yfcG; OrderedLocusNames=b2302, JW2299;
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, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-9; ASN-11
RP AND LYS-14.
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 FAMILY NAME.
RC STRAIN=K12;
RX PubMed=21222452; DOI=10.1021/bi101861a;
RA Stourman N.V., Branch M.C., Schaab M.R., Harp J.M., Ladner J.E.,
RA Armstrong R.N.;
RT "Structure and function of YghU, a nu-class glutathione transferase related
RT to YfcG from Escherichia coli.";
RL Biochemistry 50:1274-1281(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
RP DISULFIDE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC
RP PARAMETERS, SUBUNIT, AND MUTAGENESIS OF CYS-166.
RC STRAIN=K12;
RX PubMed=19537707; DOI=10.1021/bi9008825;
RA Wadington M.C., Ladner J.E., Stourman N.V., Harp J.M., Armstrong R.N.;
RT "Analysis of the structure and function of YfcG from Escherichia coli
RT reveals an efficient and unique disulfide bond reductase.";
RL Biochemistry 48:6559-6561(2009).
CC -!- FUNCTION: Exhibits a very robust glutathione (GSH)-dependent disulfide-
CC bond reductase activity toward the model substrate, 2-hydroxyethyl
CC disulfide; the actual physiological substrates are not known. Has also
CC a low GSH-dependent hydroperoxidase activity toward cumene
CC hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide,
CC benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH
CC transferase activity with most typical electrophilic substrates, and
CC has no detectable transferase activity using glutathionylspermidine
CC (GspSH) as the nucleophilic substrate. Is involved in defense against
CC oxidative stress, probably via its peroxidase activity.
CC {ECO:0000269|PubMed:17018556, ECO:0000269|PubMed:19537707}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for glutathione (when assaying the disulfide-bond reductase
CC activity with 2-hydroxyethyl disulfide)
CC {ECO:0000269|PubMed:19537707};
CC Note=kcat is 180 sec(-1) for the disulfide-bond reductase reaction
CC toward 2-hydroxyethyl disulfide. kcat is 0.27 sec(-1) for the
CC hydroperoxidase reaction with cumene hydroperoxide. kcat is 0.1 sec(-
CC 1) for the GSH transferase reaction with chloro-2,4-dinitrobenzene
CC (CDNB) as substrate.;
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:19537707}.
CC -!- DISRUPTION PHENOTYPE: Deletion of yfcG decreases the resistance of the
CC bacteria to hydrogen peroxide. {ECO:0000269|PubMed:17018556}.
CC -!- MISCELLANEOUS: The reductase activity of YfcG is unique in that no
CC sulfhydryl groups in the protein appear to be covalently involved in
CC the redox chemistry. {ECO:0000305|PubMed:19537707}.
CC -!- MISCELLANEOUS: Glutathionylspermidine (GspSH) binds YfcG about 10 times
CC more tightly than GSH. Moreover, GSSG binds 100 times more tightly than
CC GSH and 10 times more tightly than the GSH analog, GSO(3-)
CC (PubMed:19537707). {ECO:0000305|PubMed:19537707}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Nu-class GSH transferase
CC family. {ECO:0000305}.
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DR EMBL; U00096; AAC75362.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16139.1; -; Genomic_DNA.
DR PIR; D65002; D65002.
DR RefSeq; NP_416805.1; NC_000913.3.
DR RefSeq; WP_000566471.1; NZ_STEB01000008.1.
DR PDB; 3GX0; X-ray; 2.30 A; A=1-215.
DR PDB; 5HFK; X-ray; 1.55 A; A/B=1-215.
DR PDBsum; 3GX0; -.
DR PDBsum; 5HFK; -.
DR AlphaFoldDB; P77526; -.
DR SMR; P77526; -.
DR BioGRID; 4260517; 13.
DR IntAct; P77526; 2.
DR STRING; 511145.b2302; -.
DR jPOST; P77526; -.
DR PaxDb; P77526; -.
DR PRIDE; P77526; -.
DR EnsemblBacteria; AAC75362; AAC75362; b2302.
DR EnsemblBacteria; BAA16139; BAA16139; BAA16139.
DR GeneID; 66673815; -.
DR GeneID; 946763; -.
DR KEGG; ecj:JW2299; -.
DR KEGG; eco:b2302; -.
DR PATRIC; fig|1411691.4.peg.4432; -.
DR EchoBASE; EB3863; -.
DR eggNOG; COG0625; Bacteria.
DR HOGENOM; CLU_011226_14_4_6; -.
DR InParanoid; P77526; -.
DR OMA; SGSIMQY; -.
DR PhylomeDB; P77526; -.
DR BioCyc; EcoCyc:G7194-MON; -.
DR BioCyc; MetaCyc:G7194-MON; -.
DR EvolutionaryTrace; P77526; -.
DR PRO; PR:P77526; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:EcoCyc.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 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.
FT CHAIN 1..215
FT /note="Disulfide-bond oxidoreductase YfcG"
FT /id="PRO_0000186016"
FT DOMAIN 1..87
FT /note="GST N-terminal"
FT DOMAIN 90..215
FT /note="GST C-terminal"
FT BINDING 11
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19537707"
FT BINDING 38
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19537707"
FT BINDING 40
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08263"
FT BINDING 52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19537707"
FT BINDING 71..72
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19537707"
FT BINDING 132
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19537707"
FT MUTAGEN 9
FT /note="T->A: No effect on GSH transferase activity."
FT /evidence="ECO:0000269|PubMed:17018556"
FT MUTAGEN 11
FT /note="N->A: Loss of GSH transferase activity."
FT /evidence="ECO:0000269|PubMed:17018556"
FT MUTAGEN 14
FT /note="K->A: 10-fold reduction in GSH transferase
FT activity."
FT /evidence="ECO:0000269|PubMed:17018556"
FT MUTAGEN 166
FT /note="C->A: No effect on disulfide-bond reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:19537707"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:5HFK"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:5HFK"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5HFK"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 91..106
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 127..148
FT /evidence="ECO:0007829|PDB:5HFK"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:5HFK"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:5HFK"
SQ SEQUENCE 215 AA; 24516 MW; 058CEBAC879A3050 CRC64;
MIDLYFAPTP NGHKITLFLE EAELDYRLIK VDLGKGGQFR PEFLRISPNN KIPAIVDHSP
ADGGEPLSLF ESGAILLYLA EKTGLFLSHE TRERAATLQW LFWQVGGLGP MLGQNHHFNH
AAPQTIPYAI ERYQVETQRL YHVLNKRLEN SPWLGGENYS IADIACWPWV NAWTRQRIDL
AMYPAVKNWH ERIRSRPATG QALLKAQLGD ERSDS
