Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glutaredoxin-3 |
Protein Synonyms/Alias | Grx3 |
Gene Name | grxC |
Gene Synonyms/Alias | yibM; OrderedLocusNames=b3610, JW3585 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 28 | LLSSKGVSFQELPID | 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: The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase |
| DISULFID 12 15 Redox-active (By similarity) |
| 3D-structure; Completeproteome; Deoxyribonucleotidesynthesis; Directproteinsequencing; Disulfidebond; Electrontransport; Redox-activecenter; Referenceproteome; Transport |
Protein Sequence | MANVEIYTKE TCPYCHRAKA LLSSKGVSFQ ELPIDGNAAK REEMIKRSGR TTVPQIFIDA 60 QHIGGCDDLY ALDARGGLDP LLK 83 |
| GO:0009055 F:electron carrier activity IEA:InterPro GO:0043295 F:glutathione binding IDA:EcoCyc GO:0015035 F:protein disulfide oxidoreductase activity IDA:EcoCyc GO:0045454 P:cell redox homeostasis IEA:InterPro GO:0009263 P:deoxyribonucleotide biosynthetic process IEA:UniProtKB-KW |
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