Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Disulfide-bond oxidoreductase YghU |
Protein Synonyms/Alias | |
Gene Name | yghU |
Gene Synonyms/Alias | b2989, JW5492 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 17 | KVWTWDKSAGGAFAN | S | HTP | [1] | |
Reference | [1]Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium. Soares NC,Spät P,Krug K,Macek B J. Proteome Res. 2013, Jun, 7;12(6):2611-21. [ PMID:23590516] |
Functional Description From UniProt | FUNCTION: 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 |
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| 3D-structure; Completeproteome; Oxidoreductase; Peroxidase; Referenceproteome |
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 |
| GO:0015036 F:disulfide oxidoreductase activity IDA:EcoCyc GO:0004601 F:peroxidase activity IEA:UniProtKB-KW |
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