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
Functions
flavin adenine dinucleotide binding / thioredoxin-disulfide reductase activity
Processes
removal of superoxide radicals
Components
cytosol
General Function
Thioredoxin-disulfide reductase activity
Specific Function
Not Available
Pfam Domain Function
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
ResourceLink
UniProtKB IDP0A9P4
UniProtKB Entry NameTRXB_ECOLI
GenBank Gene IDJ03762
General References
  1. 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]
  2. 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]
  3. 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]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Delaney JM, Wall D, Georgopoulos C: Molecular characterization of the Escherichia coli htrD gene: cloning, sequence, regulation, and involvement with cytochrome d oxidase. J Bacteriol. 1993 Jan;175(1):166-75. [Article]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails