Thioredoxin reductase
Details
- Name
- Thioredoxin reductase
- Synonyms
- 1.8.1.9
- TRXR
- Gene Name
- trxB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0016668|Thioredoxin reductase MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDL TGPLLMERMHEHATKFETEIIFDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASARYL GLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG FRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSA GTGCMAALDAERYLDGLADAK
- Number of residues
- 321
- Molecular Weight
- 34622.76
- Theoretical pI
- 5.2
- GO Classification
- Functionsflavin adenine dinucleotide binding / thioredoxin-disulfide reductase activityProcessesremoval of superoxide radicalsComponentscytosol
- General Function
- Thioredoxin-disulfide reductase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Pyr_redox_2 (PF07992)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0016669|Thioredoxin reductase (trxB) ATGGGCACGACCAAACACAGTAAACTGCTTATCCTGGGTTCAGGCCCGGCGGGATACACC GCTGCTGTCTACGCGGCGCGCGCCAACCTGCAACCTGTGCTGATTACCGGCATGGAAAAA GGCGGCCAACTGACCACCACCACGGAAGTGGAAAACTGGCCTGGCGATCCAAACGATCTG ACCGGTCCGTTATTAATGGAGCGCATGCACGAACATGCCACCAAGTTTGAAACTGAGATC ATTTTTGATCATATCAACAAGGTGGATCTGCAAAACCGTCCGTTCCGTCTGAATGGCGAT AACGGCGAATACACTTGCGACGCGCTGATTATTGCCACCGGAGCTTCTGCACGCTATCTC GGCCTGCCCTCTGAAGAAGCCTTTAAAGGCCGTGGGGTTTCTGCTTGTGCAACCTGCGAC GGTTTCTTCTATCGCAACCAGAAAGTTGCGGTCATCGGCGGCGGCAATACCGCGGTTGAA GAGGCGCTGTATCTGTCTAACATCGCTTCGGAAGTGCATCTGATTCACCGCCGTGACGGT TTCCGCGCGGAAAAAATCCTCATTAAGCGCCTGATGGATAAAGTGGAGAACGGCAACATC ATTCTGCACACCAACCGTACGCTGGAAGAAGTGACCGGCGATCAAATGGGTGTCACTGGC GTTCGTCTGCGCGATACGCAAAACAGCGATAACATCGAGTCACTCGACGTTGCCGGTCTG TTTGTTGCTATCGGTCACAGCCCGAATACTGCGATTTTCGAAGGGCAGCTGGAACTGGAA AACGGCTACATCAAAGTACAGTCGGGTATTCATGGTAATGCCACCCAGACCAGCATTCCT GGCGTCTTTGCCGCAGGCGACGTGATGGATCACATTTATCGCCAGGCCATTACTTCGGCC GGTACAGGCTGCATGGCAGCACTTGATGCGGAACGCTACCTCGATGGTTTAGCTGACGCA AAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A9P4 UniProtKB Entry Name TRXB_ECOLI GenBank Gene ID J03762 - General References
- Russel M, Model P: Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases. J Biol Chem. 1988 Jun 25;263(18):9015-9. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
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- Poole RK, Hatch L, Cleeter MW, Gibson F, Cox GB, Wu G: Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter. Mol Microbiol. 1993 Oct;10(2):421-30. [Article]
- Ueshima R, Fujita N, Ishihama A: Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit. Biochem Biophys Res Commun. 1992 Apr 30;184(2):634-9. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Kuriyan J, Krishna TS, Wong L, Guenther B, Pahler A, Williams CH Jr, Model P: Convergent evolution of similar function in two structurally divergent enzymes. Nature. 1991 Jul 11;352(6331):172-4. [Article]
- Waksman G, Krishna TS, Williams CH Jr, Kuriyan J: Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. J Mol Biol. 1994 Feb 25;236(3):800-16. [Article]
- Lennon BW, Williams CH Jr, Ludwig ML: Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor. Protein Sci. 1999 Nov;8(11):2366-79. [Article]
- Lennon BW, Williams CH Jr, Ludwig ML: Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Science. 2000 Aug 18;289(5482):1190-4. [Article]