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YGHU_ECOLI
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   03-AUG-2022, entry version 138.
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; Proteobacteria; 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; Q46845; -.
DR   PRIDE; Q46845; -.
DR   EnsemblBacteria; AAC76025; AAC76025; b2989.
DR   EnsemblBacteria; BAE77050; BAE77050; BAE77050.
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; IAVWPWY; -.
DR   PhylomeDB; Q46845; -.
DR   BioCyc; EcoCyc:G7553-MON; -.
DR   BioCyc; MetaCyc:G7553-MON; -.
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:0006749; P:glutathione metabolic process; IEA:InterPro.
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   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.
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
 
 
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