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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0829 [new locus tag: SACOL_RS04260 ]
- pan locus tag?: SAUPAN002684000
- symbol: trxB
- pan gene symbol?: trxB
- synonym:
- product: thioredoxin-disulfide reductase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0829 [new locus tag: SACOL_RS04260 ]
- symbol: trxB
- product: thioredoxin-disulfide reductase
- replicon: chromosome
- strand: +
- coordinates: 854776..855711
- length: 936
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238649 NCBI
- RefSeq: YP_185703 NCBI
- BioCyc: see SACOL_RS04260
- MicrobesOnline: 912301 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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901ATGACTGAAATAGATTTTGATATAGCAATTATCGGTGCAGGTCCAGCTGGTATGACTGCT
GCAGTATACGCATCACGTGCTAATTTAAAAACAGTTATGATTGAAAGAGGTATTCCAGGC
GGTCAAATGGCTAATACAGAAGAAGTAGAGAACTTCCCTGGTTTCGAAATGATTACAGGT
CCAGATTTATCTACAAAAATGTTTGAACACGCTAAAAAGTTTGGTGCAGTTTATCAATAT
GGAGATATTAAATCTGTAGAAGATAAAGGCGAATATAAAGTGATTAACTTTGGTAATAAA
GAATTAACAGCGAAAGCGGTTATTATTGCTACAGGTGCAGAATACAAGAAAATTGGTGTT
CCGGGTGAACAAGAACTTGGTGGACGCGGTGTAAGTTATTGTGCAGTATGTGATGGTGCA
TTCTTTAAAAATAAACGCCTATTCGTTATCGGTGGTGGTGATTCAGCAGTAGAAGAGGGA
ACATTCTTAACTAAATTTGCTGACAAAGTAACAATCGTTCACCGTCGTGATGAGTTACGT
GCACAGCGTATTTTACAAGATAGAGCATTCAAAAATGATAAAATCGACTTTATTTGGAGT
CATACTTTGAAATCAATTAATGAAAAAGACGGCAAAGTGGGTTCTGTGACATTAACGTCT
ACAAAAGATGGTTCAGAAGAAACACACGAGGCTGATGGTGTATTCATCTATATTGGTATG
AAACCATTAACAGCGCCATTTAAAGACTTAGGTATTACAAATGATGTTGGTTATATTGTA
ACAAAAGATGATATGACAACATCAGTACCAGGTATTTTTGCAGCAGGAGATGTTCGCGAC
AAAGGTTTACGCCAAATTGTCACTGCTACTGGCGATGGTAGTATTGCAGCGCAAAGTGCA
GCGGAATATATTGAACATTTAAACGATCAAGCTTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0829 [new locus tag: SACOL_RS04260 ]
- symbol: TrxB
- description: thioredoxin-disulfide reductase
- length: 311
- theoretical pI: 5.00403
- theoretical MW: 33615.8
- GRAVY: -0.218006
⊟Function[edit | edit source]
- reaction: EC 1.8.1.9? ExPASyThioredoxin-disulfide reductase Thioredoxin + NADP+ = thioredoxin disulfide + NADPH
- TIGRFAM: Energy metabolism Electron transport thioredoxin-disulfide reductase (TIGR01292; EC 1.8.1.9; HMM-score: 398.3)and 44 moreputative alkyl hydroperoxide reductase F subunit (TIGR03143; EC 1.6.4.-; HMM-score: 303.7)Cellular processes Detoxification alkyl hydroperoxide reductase subunit F (TIGR03140; EC 1.8.1.-; HMM-score: 255.2)Cellular processes Adaptations to atypical conditions alkyl hydroperoxide reductase subunit F (TIGR03140; EC 1.8.1.-; HMM-score: 255.2)dihydrolipoyl dehydrogenase (TIGR01350; EC 1.8.1.4; HMM-score: 98.1)Cellular processes Detoxification mercury(II) reductase (TIGR02053; EC 1.16.1.1; HMM-score: 94.6)Unknown function Enzymes of unknown specificity putative bacillithiol system oxidoreductase, YpdA family (TIGR04018; EC 1.8.-.-; HMM-score: 87.6)Amino acid biosynthesis Glutamate family glutamate synthase (NADPH), homotetrameric (TIGR01316; EC 1.4.1.13; HMM-score: 52.1)glutamate synthase, small subunit (TIGR01318; HMM-score: 48.5)Energy metabolism Electron transport glutathione-disulfide reductase (TIGR01424; EC 1.8.1.7; HMM-score: 47.9)glutamate synthase, NADH/NADPH, small subunit (TIGR01317; EC 1.4.1.-; HMM-score: 46.4)Energy metabolism Electron transport glutathione-disulfide reductase (TIGR01421; EC 1.8.1.7; HMM-score: 45.8)thioredoxin and glutathione reductase (TIGR01438; EC 1.6.4.-; HMM-score: 42.8)Cellular processes Detoxification CoA-disulfide reductase (TIGR03385; EC 1.8.1.14; HMM-score: 42.7)putative selenate reductase, YgfK subunit (TIGR03315; HMM-score: 40.6)Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll geranylgeranyl reductase family (TIGR02032; EC 1.3.1.-; HMM-score: 35.1)mycofactocin system FadH/OYE family oxidoreductase 2 (TIGR03997; EC 1.-.-.-; HMM-score: 30)Unknown function Enzymes of unknown specificity flavoprotein, HI0933 family (TIGR00275; HMM-score: 28.9)Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine thiazole biosynthesis enzyme (TIGR00292; HMM-score: 28.8)Central intermediary metabolism Nitrogen metabolism nitrite reductase [NAD(P)H], large subunit (TIGR02374; EC 1.7.1.4; HMM-score: 24.8)mycothione reductase (TIGR03452; EC 1.8.1.15; HMM-score: 24.3)Energy metabolism Amino acids and amines sarcosine oxidase, alpha subunit family (TIGR01372; HMM-score: 23)Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll geranylgeranyl reductase (TIGR02023; EC 1.3.1.-; HMM-score: 21.4)pyridine nucleotide-disulfide oxidoreductase family protein (TIGR03169; HMM-score: 19.4)Energy metabolism Anaerobic glycerol-3-phosphate dehydrogenase, anaerobic, B subunit (TIGR03378; EC 1.1.5.3; HMM-score: 17.9)Protein synthesis tRNA and rRNA base modification tRNA uridine 5-carboxymethylaminomethyl modification enzyme GidA (TIGR00136; HMM-score: 16.6)lycopene cyclase family protein (TIGR01790; HMM-score: 16.2)flavin-dependent oxidoreductase, MSMEG_0569 family (TIGR04046; HMM-score: 16.2)Energy metabolism Electron transport flavocytochrome c (TIGR01813; HMM-score: 16.1)Biosynthesis of cofactors, prosthetic groups, and carriers Pyridine nucleotides L-aspartate oxidase (TIGR00551; EC 1.4.3.16; HMM-score: 15.8)Protein synthesis tRNA and rRNA base modification tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain (TIGR03197; HMM-score: 15.4)FAD dependent oxidoreductase TIGR03364 (TIGR03364; HMM-score: 15.4)Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone 2-polyprenyl-6-methoxyphenol 4-hydroxylase (TIGR01984; EC 1.14.13.-; HMM-score: 15.3)Energy metabolism TCA cycle succinate dehydrogenase, flavoprotein subunit (TIGR01816; HMM-score: 15.2)squalene-associated FAD-dependent desaturase (TIGR03467; HMM-score: 15.2)Biosynthesis of cofactors, prosthetic groups, and carriers Other phytoene desaturase (TIGR02734; EC 1.14.99.-; HMM-score: 15.1)Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family (TIGR01988; EC 1.14.13.-; HMM-score: 14.9)Energy metabolism TCA cycle succinate dehydrogenase or fumarate reductase, flavoprotein subunit (TIGR01812; HMM-score: 14.7)Energy metabolism Anaerobic succinate dehydrogenase or fumarate reductase, flavoprotein subunit (TIGR01812; HMM-score: 14.7)Energy metabolism Aerobic succinate dehydrogenase or fumarate reductase, flavoprotein subunit (TIGR01812; HMM-score: 14.7)Biosynthesis of cofactors, prosthetic groups, and carriers Other C-3',4' desaturase CrtD (TIGR02733; EC 1.3.99.-; HMM-score: 14.2)Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine glycine oxidase ThiO (TIGR02352; EC 1.4.3.19; HMM-score: 13)fumarate reductase (quinol), flavoprotein subunit (TIGR01176; EC 1.3.5.4; HMM-score: 12.3)Energy metabolism Amino acids and amines sarcosine oxidase, monomeric form (TIGR01377; HMM-score: 11.5)Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll geranylgeranyl reductase (TIGR02028; HMM-score: 11.5)
- TheSEED :
- Thioredoxin reductase (EC 1.8.1.9)
and 1 more - PFAM: NADP_Rossmann (CL0063) Pyr_redox_2; Pyridine nucleotide-disulphide oxidoreductase (PF07992; HMM-score: 179.2)and 17 morePyr_redox_3; Pyridine nucleotide-disulphide oxidoreductase (PF13738; HMM-score: 88.5)Pyr_redox; Pyridine nucleotide-disulphide oxidoreductase (PF00070; HMM-score: 76.5)FAD_oxidored; FAD dependent oxidoreductase (PF12831; HMM-score: 36.2)DAO; FAD dependent oxidoreductase (PF01266; HMM-score: 34.7)FAD_binding_2; FAD binding domain (PF00890; HMM-score: 32.3)GIDA; Glucose inhibited division protein A (PF01134; HMM-score: 29.4)NAD_binding_8; NAD(P)-binding Rossmann-like domain (PF13450; HMM-score: 29.3)HI0933_like; HI0933-like protein (PF03486; HMM-score: 28.1)Thi4; Thi4 family (PF01946; HMM-score: 27.9)Lycopene_cycl; Lycopene cyclase protein (PF05834; HMM-score: 23.3)K_oxygenase; L-lysine 6-monooxygenase (NADPH-requiring) (PF13434; HMM-score: 23.2)FAD_binding_3; FAD binding domain (PF01494; HMM-score: 19.5)NAD_binding_7; Putative NAD(P)-binding (PF13241; HMM-score: 17.8)NAD_binding_9; FAD-NAD(P)-binding (PF13454; HMM-score: 16.7)FMO-like; Flavin-binding monooxygenase-like (PF00743; HMM-score: 12.2)Shikimate_DH; Shikimate / quinate 5-dehydrogenase (PF01488; HMM-score: 12.1)no clan defined BBS2_C; Ciliary BBSome complex subunit 2, C-terminal (PF14782; HMM-score: 10.2)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: FAD
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.67
- Cytoplasmic Membrane Score: 0.01
- Cellwall Score: 0.15
- Extracellular Score: 0.17
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.070319
- TAT(Tat/SPI): 0.032442
- LIPO(Sec/SPII): 0.007824
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MTEIDFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANTEEVENFPGFEMITGPDLSTKMFEHAKKFGAVYQYGDIKSVEDKGEYKVINFGNKELTAKAVIIATGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDELRAQRILQDRAFKNDKIDFIWSHTLKSINEKDGKVGSVTLTSTKDGSEETHEADGVFIYIGMKPLTAPFKDLGITNDVGYIVTKDDMTTSVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAAEYIEHLNDQA
⊟Experimental data[edit | edit source]
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: 30.61 h [6]
⊟Biological Material[edit | edit source]
⊟Mutants[edit | edit source]
⊟Expression vector[edit | edit source]
⊟lacZ fusion[edit | edit source]
⊟GFP fusion[edit | edit source]
⊟two-hybrid system[edit | edit source]
⊟FLAG-tag construct[edit | edit source]
⊟Antibody[edit | edit source]
⊟Other Information[edit | edit source]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
PLoS One: 2009, 4(12);e8176
[PubMed:19997597] [WorldCat.org] [DOI] (I e) - ↑ Kristina Hempel, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
J Proteome Res: 2010, 9(3);1579-90
[PubMed:20108986] [WorldCat.org] [DOI] (I p) - ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
J Proteome Res: 2011, 10(4);1657-66
[PubMed:21323324] [WorldCat.org] [DOI] (I p) - ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
The Staphylococcus aureus proteome.
Int J Med Microbiol: 2014, 304(2);110-20
[PubMed:24439828] [WorldCat.org] [DOI] (I p) - ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
Sci Rep: 2016, 6;28172
[PubMed:27344979] [WorldCat.org] [DOI] (I e) - ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
Mol Cell Proteomics: 2012, 11(9);558-70
[PubMed:22556279] [WorldCat.org] [DOI] (I p)