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 13-FEB-2019, entry version 131. 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., RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., RA Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli- RT K12 genome corresponding to 50.0-68.8 min on the linkage map and RT analysis of 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., RA Mau B., 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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP FUNCTION IN DEFENSE AGAINST OXIDATIVE STRESS, GSH TRANSFERASE RP ACTIVITY, PEROXIDASE ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS RP OF THR-9; ASN-11 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 RT related 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, RP KINETIC 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 CC disulfide-bond reductase activity toward the model substrate, 2- CC hydroxyethyl disulfide; the actual physiological substrates are CC not known. Has also a low GSH-dependent hydroperoxidase activity CC toward cumene hydroperoxide, but does not reduce H(2)O(2), tert- CC butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. CC Exhibits little or no GSH transferase activity with most typical CC electrophilic substrates, and has no detectable transferase CC activity using glutathionylspermidine (GspSH) as the nucleophilic CC substrate. Is involved in defense against oxidative stress, CC 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 CC reductase activity with 2-hydroxyethyl disulfide) CC {ECO:0000269|PubMed:19537707}; CC Note=kcat is 180 sec(-1) for the disulfide-bond reductase CC reaction toward 2-hydroxyethyl disulfide. kcat is 0.27 sec(-1) CC for the hydroperoxidase reaction with cumene hydroperoxide. kcat CC is 0.1 sec(-1) for the GSH transferase reaction with chloro-2,4- CC dinitrobenzene (CDNB) as substrate.; CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:19537707}. CC -!- DISRUPTION PHENOTYPE: Deletion of yfcG decreases the resistance of CC the 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 CC in the redox chemistry. {ECO:0000305|PubMed:19537707}. CC -!- MISCELLANEOUS: Glutathionylspermidine (GspSH) binds YfcG about 10 CC times more tightly than GSH. Moreover, GSSG binds 100 times more CC tightly than GSH and 10 times more tightly than the GSH analog, CC GSO(3-) (PubMed:19537707). {ECO:0000305|PubMed:19537707}. CC -!- SIMILARITY: Belongs to the GST superfamily. Nu-class GSH CC transferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_LN832404.1. 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 ProteinModelPortal; P77526; -. DR SMR; P77526; -. DR BioGrid; 4260517; 13. DR IntAct; P77526; 2. DR STRING; 316385.ECDH10B_2464; -. DR jPOST; P77526; -. DR PaxDb; P77526; -. DR PRIDE; P77526; -. DR EnsemblBacteria; AAC75362; AAC75362; b2302. DR EnsemblBacteria; BAA16139; BAA16139; BAA16139. DR GeneID; 946763; -. DR KEGG; ecj:JW2299; -. DR KEGG; eco:b2302; -. DR PATRIC; fig|1411691.4.peg.4432; -. DR EchoBASE; EB3863; -. DR EcoGene; EG14110; yfcG. DR eggNOG; ENOG4105CYM; Bacteria. DR eggNOG; COG0625; LUCA. DR HOGENOM; HOG000125752; -. DR InParanoid; P77526; -. DR KO; K11209; -. DR PhylomeDB; P77526; -. DR BioCyc; EcoCyc:G7194-MONOMER; -. DR BioCyc; ECOL316407:JW2299-MONOMER; -. DR BioCyc; MetaCyc:G7194-MONOMER; -. 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: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; Complete proteome; Oxidoreductase; Peroxidase; KW Reference proteome. FT CHAIN 1 215 Disulfide-bond oxidoreductase YfcG. FT /FTId=PRO_0000186016. FT DOMAIN 1 87 GST N-terminal. FT DOMAIN 90 215 GST C-terminal. FT REGION 71 72 Glutathione 1 binding. FT {ECO:0000269|PubMed:19537707}. FT BINDING 11 11 Glutathione 1. FT {ECO:0000269|PubMed:19537707}. FT BINDING 38 38 Glutathione 1. FT {ECO:0000269|PubMed:19537707}. FT BINDING 40 40 Glutathione. FT {ECO:0000250|UniProtKB:P08263}. FT BINDING 52 52 Glutathione 1; via amide nitrogen and FT carbonyl oxygen. FT {ECO:0000269|PubMed:19537707}. FT BINDING 132 132 Glutathione 2. FT {ECO:0000269|PubMed:19537707}. FT MUTAGEN 9 9 T->A: No effect on GSH transferase FT activity. {ECO:0000269|PubMed:17018556}. FT MUTAGEN 11 11 N->A: Loss of GSH transferase activity. FT {ECO:0000269|PubMed:17018556}. FT MUTAGEN 14 14 K->A: 10-fold reduction in GSH FT transferase activity. FT {ECO:0000269|PubMed:17018556}. FT MUTAGEN 166 166 C->A: No effect on disulfide-bond FT reductase activity. FT {ECO:0000269|PubMed:19537707}. FT STRAND 2 6 {ECO:0000244|PDB:5HFK}. FT HELIX 10 22 {ECO:0000244|PDB:5HFK}. FT STRAND 26 30 {ECO:0000244|PDB:5HFK}. FT HELIX 33 35 {ECO:0000244|PDB:5HFK}. FT HELIX 37 39 {ECO:0000244|PDB:5HFK}. FT HELIX 41 44 {ECO:0000244|PDB:5HFK}. FT STRAND 54 59 {ECO:0000244|PDB:5HFK}. FT STRAND 67 71 {ECO:0000244|PDB:5HFK}. FT HELIX 72 83 {ECO:0000244|PDB:5HFK}. FT HELIX 91 106 {ECO:0000244|PDB:5HFK}. FT HELIX 108 120 {ECO:0000244|PDB:5HFK}. FT HELIX 127 148 {ECO:0000244|PDB:5HFK}. FT STRAND 156 158 {ECO:0000244|PDB:5HFK}. FT HELIX 161 170 {ECO:0000244|PDB:5HFK}. FT HELIX 171 175 {ECO:0000244|PDB:5HFK}. FT HELIX 180 182 {ECO:0000244|PDB:5HFK}. FT HELIX 184 194 {ECO:0000244|PDB:5HFK}. FT HELIX 197 205 {ECO:0000244|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 //