ID YGHU_ECOLI Reviewed; 288 AA.
AC Q46845; Q2M9K6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Disulfide-bond oxidoreductase YghU;
DE EC=1.8.4.-;
DE AltName: Full=GSH-dependent disulfide-bond oxidoreductase YghU;
DE AltName: Full=GST N2-2;
DE AltName: Full=Organic hydroperoxidase;
DE EC=1.11.1.-;
GN Name=yghU; OrderedLocusNames=b2989, JW5492;
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 / 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 [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP FAMILY NAME, AND SUBUNIT.
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).
CC -!- FUNCTION: Exhibits a robust glutathione (GSH)-dependent disulfide-bond
CC reductase activity toward the model substrate, 2-hydroxyethyl
CC disulfide; the actual physiological substrates are not known. Also
CC displays a modest GSH-dependent peroxidase activity toward several
CC organic hydroperoxides, such as cumene hydroperoxide and linoleic acid
CC 13(S)-hydroperoxide, but does not reduce H(2)O(2) or tert-butyl
CC hydroperoxide at appreciable rates. Exhibits little or no GSH
CC transferase activity with most typical electrophilic substrates, and
CC has no detectable transferase activity toward 1-chloro-2,4-
CC dinitrobenzene (CDNB) with glutathionylspermidine (GspSH) as the
CC nucleophilic substrate. {ECO:0000269|PubMed:21222452}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for glutathione (when assaying the GSH transferase activity
CC with CDNB) {ECO:0000269|PubMed:21222452};
CC KM=1.1 mM for glutathione (when assaying the disulfide-bond reductase
CC activity with 2-hydroxyethyl disulfide)
CC {ECO:0000269|PubMed:21222452};
CC KM=16 uM for cumene hydroperoxide {ECO:0000269|PubMed:21222452};
CC KM=130 uM for linoleic acid 13(S)-hydroperoxide
CC {ECO:0000269|PubMed:21222452};
CC KM=28 uM for 15(S)-HpETE {ECO:0000269|PubMed:21222452};
CC Note=kcat is 74 sec(-1) for the disulfide-bond reductase reaction
CC toward 2-hydroxyethyl disulfide. kcat is 0.050, 0.19 and 0.096 sec(-
CC 1) for the hydroperoxidase reaction with cumene hydroperoxide,
CC linoleic acid 13(S)-hydroperoxide, and 15(S)-HpETE as substrate,
CC respectively. kcat is 0.109 sec(-1) for the GSH transferase reaction
CC with CDNB as substrate.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21222452}.
CC -!- MISCELLANEOUS: Binds two molecules of GSH in each active site; there is
CC one tight and one weak binding site for GSH.
CC -!- SIMILARITY: Belongs to the GST superfamily. Nu-class GSH transferase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69156.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U28377; AAA69156.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76025.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77050.1; -; Genomic_DNA.
DR RefSeq; NP_417463.4; NC_000913.3.
DR RefSeq; WP_001295515.1; NZ_STEB01000001.1.
DR PDB; 3C8E; X-ray; 1.50 A; A/B=1-288.
DR PDBsum; 3C8E; -.
DR AlphaFoldDB; Q46845; -.
DR SMR; Q46845; -.
DR BioGRID; 4261179; 14.
DR DIP; DIP-12212N; -.
DR STRING; 511145.b2989; -.
DR jPOST; Q46845; -.
DR PaxDb; 511145-b2989; -.
DR EnsemblBacteria; AAC76025; AAC76025; b2989.
DR GeneID; 75173122; -.
DR GeneID; 947472; -.
DR KEGG; ecj:JW5492; -.
DR KEGG; eco:b2989; -.
DR PATRIC; fig|1411691.4.peg.3740; -.
DR EchoBASE; EB2827; -.
DR eggNOG; COG0625; Bacteria.
DR HOGENOM; CLU_011226_14_4_6; -.
DR InParanoid; Q46845; -.
DR OMA; GHSGAEY; -.
DR OrthoDB; 9803562at2; -.
DR PhylomeDB; Q46845; -.
DR BioCyc; EcoCyc:G7553-MONOMER; -.
DR BioCyc; MetaCyc:G7553-MONOMER; -.
DR EvolutionaryTrace; Q46845; -.
DR PRO; PR:Q46845; -.
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:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR CDD; cd10292; GST_C_YghU_like; 1.
DR CDD; cd03048; GST_N_Ure2p_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01151; Main.2:_Nu-like; 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.
FT CHAIN 1..288
FT /note="Disulfide-bond oxidoreductase YghU"
FT /id="PRO_0000186017"
FT DOMAIN 46..133
FT /note="GST N-terminal"
FT DOMAIN 139..265
FT /note="GST C-terminal"
FT REGION 260..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21222452"
FT BINDING 52..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT BINDING 87
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21222452"
FT BINDING 101
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21222452"
FT BINDING 117..118
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT BINDING 151
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21222452"
FT BINDING 178
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21222452"
FT TURN 21..25
FT /evidence="ECO:0007829|PDB:3C8E"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3C8E"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:3C8E"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3C8E"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3C8E"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 137..159
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 173..194
FT /evidence="ECO:0007829|PDB:3C8E"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:3C8E"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:3C8E"
FT TURN 228..232
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3C8E"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3C8E"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3C8E"
SQ SEQUENCE 288 AA; 32392 MW; 799B17697A3C1C42 CRC64;
MTDNTYQPAK VWTWDKSAGG AFANINRPVS GPTHEKTLPV GKHPLQLYSL GTPNGQKVTI
MLEELLALGV TGAEYDAWLI RIGDGDQFSS GFVEVNPNSK IPALRDHTHN PPIRVFESGS
ILLYLAEKFG YFLPQDLAKR TETMNWLFWL QGAAPFLGGG FGHFYHYAPV KIEYAINRFT
MEAKRLLDVL DKQLAQHKFV AGDEYTIADM AIWPWFGNVV LGGVYDAAEF LDAGSYKHVQ
RWAKEVGERP AVKRGRIVNR TNGPLNEQLH ERHDASDFET NTEDKRQG
//
