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Treponema denticola Search Results

Record: 1 of 1 MiniMap

Gene ID:TDE0743DNA Molecule Name: 1 GenBank ID: 42526256Gene Name: trxB Definition: thioredoxin reductaseCellular Location: Cytoplasm [Evidence]Gene Start: 778858Gene Stop: 779808Gene Length: 951Molecular Weight*: 34203pI*:Net Charge*:EC: 1.8.1.9 Functional Class: Biosynthesis of cofactors, prosthetic groups, and carriers; Thioredoxin, glutaredoxin, and glutathione Gene Ontology:Pathway: pathway table Pyrimidine metabolismSecondary Evidence: Tong Q, Yang YG, Zhang HT, Chen Y, Yang SL, Gong Y. The Thioredoxin Reductase-deficient E.coli Mutant Enhances Expression into Solution of Recombinant Proteins Containing Cys Residues. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001;33(1):30-34. PMID: 12053185 Lee JH, Kim MS, Cho JH, Kim SC. Enhanced expression of tandem multimers of the antimicrobial peptide buforin II in Escherichia coli by the DEAD-box protein and trxB mutant. Appl Microbiol Biotechnol. 2002 May;58(6):790-6. PMID: 12021800 Liu S, Graham JE, Bigelow L, Morse PD, Wilkinson BJ. Identification of Listeria monocytogenes genes expressed in response to growth at low temperature. Appl Environ Microbiol. 2002 Apr;68(4):1697-705. PMID: 11916687Comment: The thioredoxin (trxA) is TDE0744.View in HOMD Genome ViewerBlast Summary: PSI-Blast Search TDE0743 has significant similarity to the Treponema pallidum gene TP0814 (1e-70). TDE0743 has significant similarity to the Borrelia burgdorferi gene 15594860 (4e-50).Top Blast Hits: Updated monthly Click here to view the entire PsiBlast results. gi|42526256|ref|NP_971354.1| thioredoxin reductase [Trepone... 590 e-167 gi|11065685|emb|CAC14297.1| thioredoxin reductase [Clostrid... 317 8e-85 gi|150391327|ref|YP_001321376.1| thioredoxin reductase [Alk... 300 6e-80 gi|126699972|ref|YP_001088869.1| thioredoxin reductase [Clo... 299 1e-79 gi|54303220|ref|YP_133213.1| Hypothetical thioredoxin reduc... 296 9e-79 gi|153853545|ref|ZP_01994925.1| hypothetical protein DORLON... 296 1e-78 gi|90410185|ref|ZP_01218202.1| Hypothetical thioredoxin red... 294 5e-78 gi|78044856|ref|YP_361186.1| thioredoxin-disulfide reductas... 292 2e-77 gi|1717776|sp|P52213|TRXB_CLOLI Thioredoxin reductase (TRXR... 289 2e-76 gi|76797132|ref|ZP_00779471.1| Thioredoxin reductase [Therm... 286 1e-75COGS Summary: COGS Search BeTs to clades of COG0492 COG name: Thioredoxin reductase Functional Class:� O The phylogenetic pattern of COG0492 is aompkzyqvdrlbcefghsnujxitw Number of proteins in this genome belonging to this COG isBlocks Summary: Blocks Search Significant hit ( 1.2e-68) to 5/5 blocks of the IPB000103 family, which is described as "Pyridine nucleotide-disulphide oxidoreductase class-II". Interpro entry for IPR000103. IPB000103A 6-26 3.3e-12 IPB000103B 40-54 1.3e-06 IPB000103C 115-163 5.4e-28 IPB000103D 235-246 0.00029 IPB000103E 269-306 7.3e-12 IPB000103A 149-169 0.17 Significant hit ( 1.2e-31) to 5/5 blocks of the PR00368 family, which is described as "FAD-dependent pyridine nucleotide reductase signature". Prints database entry for PR00368. PR00368A 6-28 5e-11 PR00368B 110-119 0.061 PR00368C 149-174 2e-09 PR00368D 234-248 0.2 PR00368E 274-281 0.61 Significant hit ( 8.9e-06) to 1/5 blocks of the IPB000171 family, which is described as "Bacterial-type phytoene dehydrogenase". Interpro entry for IPR000171. IPB000171A 8-38 8.8e-06 IPB000171A 151-181 0.0058ProDom Summary: Protein Domain Search Residues 109 to 180 match (2e-24) PD:PD329455 which is described as REDUCTASE OXIDOREDUCTASE THIOREDOXIN FLAVOPROTEIN FAD COMPLETE PROTEOME REDOX-ACTIVE CENTER NADP Residues 73 to 290 match (3e-23) PD:PD396826 which is described as PROTEOME PHOSPHORYLATION MLR4645 COMPLETE THIOREDOXIN REDUCTASE FLAVOPROTEIN SENSORY FAD OXIDOREDUCTASE Residues 105 to 180 match (9e-23) PD:PD000139 which is described as OXIDOREDUCTASE FLAVOPROTEIN FAD REDUCTASE COMPLETE PROTEOME DEHYDROGENASE CENTER REDOX-ACTIVE DIHYDROLIPOAMIDE Residues 110 to 176 match (2e-11) PD:PD586287 which is described as PROTEOME REDUCTASE COMPLETE FLAVOPROTEIN FAD OXIDOREDUCTASE THIOREDOXIN F PROBABLE ALKYL Residues 183 to 290 match (2e-09) PD:PD574794 which is described as FLAVOPROTEIN FAD OXIDOREDUCTASE PROTEOME COMPLETE THIOREDOXIN REDUCTASE NADP CENTER TRXR Residues 110 to 188 match (2e-09) PD:PD518786 which is described as NADP CENTER PROTEOME COMPLETE REDOX-ACTIVE FLAVOPROTEIN MJ1536 FAD OXIDOREDUCTASE NAD Residues 203 to 261 match (2e-08) PD:PD338946 which is described as OXIDOREDUCTASE FLAVOPROTEIN FAD REDUCTASE PROTEOME COMPLETE DEHYDROGENASE NADH NAD SUBUNIT Residues 100 to 283 match (3e-08) PD:PD329335 which is described as OXIDOREDUCTASE COMPLETE PROTEOME FAD FLAVOPROTEIN REDUCTASE NUCLEOTIDE-DISULPHIDE PYRIDINE OXIDOREDUCTASE CLASS Residues 215 to 266 match (1e-07) PD:PD591170 which is described as THIOREDOXIN REDUCTASE OXIDOREDUCTASE FAD FLAVOPROTEIN NADP REDOX-ACTIVE CENTER COMPLETE PROTEOMEParalogs: Local Blast Search TDE0743 is paralogously related to TDE1629 (dihydrolipoamide dehydrogenase (glutathione oxidoreductase)) (5e-14), TDE2644 (uncharacterized NAD(FAD)-dependent dehydrogenase) (6e-08), TDE0407 (NADPH-dependent glutamate synthase beta chain (small subunit)) (7e-07), TDE0096 (NADH oxidase/peroxidase) (8e-06), TDE0153 (NADH oxidase) (3e-05), TDE0135 (oxidoreductase) (2e-04) and TDE1594 (possible NADPH-dependent glutamate synthase beta chain (small subunit); possible formate dehydrogenase) (2e-04).Pfam Summary: Pfam Search Residues 6 to 290 (E-value = 5.6e-71) place TDE0743 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)Top PDB Hits: PDB hits to TDE0743 from Psi-BLAST round 5 vs. nr database 37.0% similar to PDB:1CL0 Crystal Structure Of Reduced Thioredoxin Reductase From Escherichia Coli (Chain A; 2e-85) 37.5% similar to PDB:1TDE Thioredoxin Reductase (E.C.1.6.4.5) (Wild Type) (6e-85) 36.7% similar to PDB:1F6M Crystal Structure Of A Complex Between Thioredoxin Reductase, Thioredoxin, And T (Chain A,B,E,F; 8e-85) 36.7% similar to PDB:1TRB Thioredoxin Reductase (E.C.1.6.4.5) Mutant With Cys 138 Replaced By Ser (C138s) (2e-84) 37.2% similar to PDB:1TDF Thioredoxin Reductase (E.C.1.6.4.5) Mutant With Cys 138 Replaced By Ser (C138s) (7e-84) 36.7% similar to PDB:1VDC Structure Of Nadph Dependent Thioredoxin Reductase (2e-78) 26.4% similar to PDB:1HYU Crystal Structure Of Intact Ahpf (Chain A; 3e-74) 27.5% similar to PDB:1FL2 Catalytic Core Component Of The Alkylhydroperoxide Reductase Ahpf From E.Coli (Chain A; 2e-71) 18.2% similar to PDB:1DXL Dihydrolipoamide Dehydrogenase Of Glycine Decarboxylase From Pisum Sativum (Chain A,B,C,D; 4e-61) 17.4% similar to PDB:1LPF Dihydrolipoamide Dehydrogenase (E.C.1.8.1.4) Complex With Flavin-Adenine-Dinucle (Chain A,B; 4e-57)Gene Protein Sequence: MSEKYDLVIIGGGPGGMAAGIYAARSKLKTVILEEKPNQGGQCYITEEIE NYPGFPESSGPALTEAFKKHAEKFGVEFKRARAEKIELVPNSPTRIVHGS DGVKYECLAVVVATGASARELGCKGEKEHWGKGVSYCATCDGAFFEECEI VVIGGGDSAVEEAMYLTKFADKVTIIHRRDELRAAKSIQEKAFANPKMAF KWNAVVEEVCGEGLVDSVILKDTKTGETSKFDTEGVFVFIGHNPQTAFIQ GLVDLDENGYILTNGKMETNVPGIYGVGDVIQKESRQVVTAAADGALAGI WAGHYIDDIKAKMAMKKGene Nucleotide Sequence: Sequence Viewer ATGTCAGAAAAATATGATTTGGTTATAATTGGAGGCGGTCCCGGCGGTAT GGCCGCAGGAATTTATGCAGCCCGTTCAAAATTAAAGACGGTTATTCTTG AAGAAAAGCCCAATCAAGGCGGACAGTGCTATATCACTGAAGAAATCGAA AACTACCCCGGTTTCCCTGAATCTTCAGGTCCTGCTCTGACCGAAGCCTT TAAAAAACATGCCGAAAAATTCGGTGTTGAATTCAAAAGAGCAAGAGCCG AAAAAATCGAGCTTGTTCCCAATTCACCTACGCGCATTGTTCACGGAAGT GACGGCGTAAAGTATGAATGCTTGGCTGTTGTTGTTGCAACAGGTGCAAG TGCCAGAGAGCTCGGCTGTAAGGGCGAAAAAGAGCACTGGGGCAAGGGTG TTTCATACTGCGCAACATGCGACGGTGCCTTCTTTGAAGAGTGCGAAATC GTAGTTATCGGCGGCGGAGACTCTGCTGTTGAAGAAGCTATGTATCTTAC AAAATTTGCCGACAAGGTAACTATCATTCACCGAAGGGATGAACTTAGAG CTGCAAAATCCATTCAGGAAAAGGCTTTTGCCAACCCCAAAATGGCCTTT AAGTGGAATGCCGTTGTTGAAGAAGTTTGCGGAGAAGGCCTTGTAGACAG CGTTATCTTAAAGGATACAAAAACAGGCGAAACCTCCAAATTCGATACAG AAGGCGTATTCGTATTTATCGGACACAATCCTCAAACCGCCTTTATTCAG GGCTTGGTAGACCTTGATGAAAACGGCTACATCCTCACAAACGGAAAAAT GGAAACAAACGTACCCGGTATTTACGGCGTAGGCGATGTTATTCAAAAAG AATCACGGCAGGTTGTTACAGCAGCTGCCGACGGTGCGCTTGCCGGTATT TGGGCAGGCCACTATATCGACGATATCAAAGCCAAAATGGCTATGAAAAA A

Los Alamos National Laboratory • Est 1943