Thioredoxin reductase (P0A9P4)

Identification
Name:Thioredoxin reductase
Synonyms:
  • TRXR
Gene Name:trxB
Enzyme Class:
Biological Properties
General Function:Involved in oxidation-reduction process
Specific Function:Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thioredoxin+1.0Thumb+1.0Thumb ↔ 1.0Thioredoxin disulfide+1.0Thumb+1.0Thumb+1.0Thioredoxin disulfide
1.0Thioredoxin + 1.0NADP + 1.0Thioredoxin ↔ 1.0Thioredoxin disulfide + 1.0NADPH + 1.0Hydrogen ion + 1.0Thioredoxin disulfide
ReactionCard
1.0Thumb+3.0Thumb+3.0Thumb ↔ 1.0Thumb+3.0Thumb+5.0Thumb
1.0Hydrogen selenide + 3.0NADP + 3.0Water ↔ 1.0Selenite + 3.0NADPH + 5.0Hydrogen ion
ReactionCard
2.0Thumb+2.0Thumb+1.0Methylselenic acid ↔ 2.0Thumb+2.0Thumb+1.0Methaneselenol
2.0NADPH + 2.0Hydrogen ion + 1.0Methylselenic acid ↔ 2.0NADP + 2.0Water + 1.0Methaneselenol
ReactionCard
SMPDB Reactions:
1.0oxidized thioredoxin +1.0Thumb+1.0Thumb → 1.0reduced thioredoxin+1.0Thumb
1.0oxidized thioredoxin + 1.0NADPH + 1.0Hydrogen ion → 1.0reduced thioredoxin + 1.0NADP
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin → 1.0Thumb+1.0Reduced Thioredoxin
1.0Hydrogen ion + 1.0NADPH + 1.0Oxidized Thioredoxin → 1.0NADP + 1.0Reduced Thioredoxin
ReactionCard
1.0Thioredoxin+1.0Thumb → 1.0thioredoxin disulfide+1.0Thumb
1.0Thioredoxin + 1.0NADP → 1.0thioredoxin disulfide + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB11110Hydrogen selenideMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB21355SeleniteMetaboCard
ECMDB23749ThioredoxinMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
antioxidant activity
binding
catalytic activity
FAD or FADH2 binding
nucleoside binding
oxidoreductase activity
purine nucleoside binding
thioredoxin-disulfide reductase activity
Process
cellular metabolic process
metabolic process
oxidation reduction
oxygen and reactive oxygen species metabolic process
removal of superoxide radicals
superoxide metabolic process
Gene Properties
Blattner:b0888
Gene OrientationCounterclockwise
Centisome Percentage:20.05
Left Sequence End930308
Right Sequence End931273
Gene Sequence:
>966 bp
ATGGGCAAAGCAGTCATTGCAATTCATGGTGGCGCAGGTGCAATTAGCCGCGCGCAGATG
AGTCTGCAACAGGAATTACGCTACATCGAGGCGTTGTCTGCCATTGTTGAAACCGGGCAG
AAAATGCTGGAAGCGGGCGAAAGTGCGCTGGATGTGGTGACGGAAGCGGTGCGTCTGCTG
GAAGAGTGTCCACTGTTTAACGCCGGAATTGGCGCTGTCTTTACGCGTGATGAAACCCAT
GAACTGGACGCCTGTGTGATGGATGGTAACACCCTGAAAGCCGGTGCGGTGGCGGGCGTT
AGTCATCTGCGTAATCCGGTTCTTGCCGCCCGGCTGGTGATGGAGCAAAGCCCGCATGTG
ATGATGATTGGCGAAGGGGCAGAAAATTTTGCGTTTGCTCGTGGCATGGAGCGCGTCTCG
CCGGAGATTTTCTCCACGTCTTTGCGTTATGAACAACTACTGGCAGCGCGCAAGGAAGGG
GCAACCGTCCTCGACCATAGCGGTGCGCCACTGGATGAAAAACAGAAAATGGGCACCGTG
GGGGCCGTGGCGTTGGATTTAGACGGCAATTTGGCGGCAGCCACGTCCACAGGCGGAATG
ACCAATAAATTACCCGGACGAGTTGGCGATAGTCCCTTAGTGGGTGCCGGATGCTACGCC
AATAACGCCAGTGTGGCGGTTTCTTGTACCGGCACGGGCGAAGTCTTCATCCGCGCGCTG
GCGGCATATGACATCGCCGCGTTAATGGATTACGGCGGATTAAGTCTCGCGGAAGCCTGC
GAGCGGGTAGTAATGGAAAAACTCCCTGCGCTTGGCGGTAGCGGTGGCTTAATCGCTATC
GACCATGAAGGGAATGTCGCGCTACCGTTTAACACCGAAGGAATGTATCGCGCCTGGGGC
TACGCAGGCGATACGCCAACCACCGGTATCTACCGTGAAAAAGGGGACACCGTTGCCACA
CAGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:321
Protein Molecular Weight:34623
Protein Theoretical pI:5
PDB File:1CL0
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Thioredoxin reductase
MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDL
TGPLLMERMHEHATKFETEIIFDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASARYL
GLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG
FRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL
FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSA
GTGCMAALDAERYLDGLADAK
References
External Links:
ResourceLink
Uniprot ID:P0A9P4
Uniprot Name:TRXB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062400
PDB ID:1CL0
Ecogene ID:EG11032
Ecocyc:EG11032
ColiBase:b0888
Kegg Gene:b0888
EchoBASE ID:EB1025
CCDB:TRXB_ECOLI
BacMap:16128855
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Delaney, J. M., Wall, D., Georgopoulos, C. (1993). "Molecular characterization of the Escherichia coli htrD gene: cloning, sequence, regulation, and involvement with cytochrome d oxidase." J Bacteriol 175:166-175. Pubmed: 8380150
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kuriyan, J., Krishna, T. S., Wong, L., Guenther, B., Pahler, A., Williams, C. H. Jr, Model, P. (1991). "Convergent evolution of similar function in two structurally divergent enzymes." Nature 352:172-174. Pubmed: 2067578
  • Lennon, B. W., Williams, C. H. Jr, Ludwig, M. L. (1999). "Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor." Protein Sci 8:2366-2379. Pubmed: 10595539
  • Lennon, B. W., Williams, C. H. Jr, Ludwig, M. L. (2000). "Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase." Science 289:1190-1194. Pubmed: 10947986
  • 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, a. l. .. (1996). "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 3:137-155. Pubmed: 8905232
  • Poole, R. K., Hatch, L., Cleeter, M. W., Gibson, F., Cox, G. B., Wu, G. (1993). "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 10:421-430. Pubmed: 7934832
  • Russel, M., Model, P. (1988). "Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases." J Biol Chem 263:9015-9019. Pubmed: 3288628
  • Ueshima, R., Fujita, N., Ishihama, A. (1992). "Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit." Biochem Biophys Res Commun 184:634-639. Pubmed: 1575737
  • Waksman, G., Krishna, T. S., Williams, C. H. Jr, Kuriyan, J. (1994). "Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis." J Mol Biol 236:800-816. Pubmed: 8114095