Tag | Content |
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CPLM ID | CPLM-013210 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Disulfide-bond oxidoreductase YghU |
Protein Synonyms/Alias | GSH-dependent disulfide-bond oxidoreductase YghU; GST N2-2; Organic hydroperoxidase |
Gene Name | yghU |
Gene Synonyms/Alias | b2989; JW5492 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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16 | AKVWTWDKSAGGAFA | acetylation | [1] | 36 | VSGPTHEKTLPVGKH | acetylation | [1] | 42 | EKTLPVGKHPLQLYS | acetylation | [1] | 139 | FLPQDLAKRTETMNW | acetylation | [1] | 192 | RLLDVLDKQLAQHKF | acetylation | [1] | 244 | KHVQRWAKEVGERPA | acetylation | [1] | 285 | FETNTEDKRQG**** | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Exhibits a robust glutathione (GSH)-dependent disulfide- bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also displays a modest GSH-dependent peroxidase activity toward several organic hydroperoxides, such as cumene hydroperoxide and linoleic acid 13(S)-hydroperoxide, but does not reduce H(2)O(2) or tert- butyl hydroperoxide at appreciable rates. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB) with glutathionylspermidine (GspSH) as the nucleophilic substrate. |
Sequence Annotation | DOMAIN 46 133 GST N-terminal. DOMAIN 139 265 GST C-terminal. REGION 52 54 Glutathione 1 binding. REGION 117 118 Glutathione 1 binding. BINDING 26 26 Glutathione 2. BINDING 87 87 Glutathione 1. BINDING 101 101 Glutathione 1; via amide nitrogen and BINDING 151 151 Glutathione 1. BINDING 178 178 Glutathione 2. |
Keyword | 3D-structure; Complete proteome; Oxidoreductase; Peroxidase; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 288 AA |
Protein Sequence | MTDNTYQPAK VWTWDKSAGG AFANINRPVS GPTHEKTLPV GKHPLQLYSL GTPNGQKVTI 60 MLEELLALGV TGAEYDAWLI RIGDGDQFSS GFVEVNPNSK IPALRDHTHN PPIRVFESGS 120 ILLYLAEKFG YFLPQDLAKR TETMNWLFWL QGAAPFLGGG FGHFYHYAPV KIEYAINRFT 180 MEAKRLLDVL DKQLAQHKFV AGDEYTIADM AIWPWFGNVV LGGVYDAAEF LDAGSYKHVQ 240 RWAKEVGERP AVKRGRIVNR TNGPLNEQLH ERHDASDFET NTEDKRQG 288 |
Gene Ontology | GO:0015036; F:disulfide oxidoreductase activity; IDA:EcoCyc. GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. |
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