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InterPro: IPR012335 Thioredoxin fold

Protein matchesHelp
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UniProtKB
Matches:
51719 proteins
AccessionHelp
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IPR012335 Thioredoxin_fold
TypeHelp
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Domain
SignaturesHelp
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InterPro RelationshipsHelp
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Parent IPR012336 Thioredoxin-like fold
Children IPR004045 Glutathione S-transferase, N-terminal
IPR017936 Thioredoxin-like
Found in IPR000643 Iodothyronine deiodinase
IPR000889 Glutathione peroxidase
IPR001200 Phosducin
IPR001393 Calsequestrin
IPR001853 DSBA oxidoreductase
IPR002023 NADH:ubiquinone oxidoreductase, 24kDa subunit
IPR002946 Intracellular chloride channel
IPR003782 Copper chaperone SCO1/SenC
IPR004123 mRNA splicing factor, thioredoxin-like U5 snRNP
IPR004480 Glutaredoxin-related protein
IPR004508 Thioredoxin-independent 5'-adenylylsulphate reductase
IPR004799 Periplasmic protein thiol:disulphide oxidoreductase DsbE
IPR005243 Redox-active disulphide protein 2
IPR005788 Disulphide isomerase
IPR005792 Protein disulphide isomerase
IPR005985 Bacteriocin transport accessory protein
IPR006503 Nitrogenase-associated protein
IPR006504 Conserved hypothetical protein, ArsC related
IPR006659 Arsenate reductase
IPR006660 Arsenate reductase-like
IPR006844 OST3/OST6
IPR006993 SH3-binding, glutamic acid-rich protein
IPR007332 Protein of unknown function DUF411
IPR008554 Glutaredoxin 2
IPR009737 Sucraseferredoxin-like
IPR010357 Protein of unknown function DUF953, thioredoxin-like
IPR010893 Hydrogenase-1 expression HyaE
IPR011900 Glutaredoxin, GrxC
IPR011902 Glutaredoxin, GrxA
IPR011903 Glutaredoxin-like
IPR011905 Glutaredoxin-like, plant II
IPR011909 Glutaredoxin-like protein NrdH
IPR011911 Glutaredoxin-like protein, YruB
IPR011915 Glutaredoxin-like protein GlrX
IPR012081 Alkyl hydroperoxide reductase, subunit F
IPR013376 Glutathione peroxidase Gpx7, putative
IPR013478 Methylamine dehydrogenase accessory protein MauD
IPR014025 Glutaredoxin subgroup
IPR014434 Monothiol glutaredoxin
IPR015450 Glutaredoxin-2
IPR016855 Endoplasmic reticulum, protein ERp29
IPR017068 Protein disulphide-isomerase A4
IPR017276 Synthesis of cytochrome c oxidase, Sco1/Sco2
IPR017559 Peroxiredoxin
IPR017561 Putative alkyl hydroperoxide reductase F subunit
Contains IPR000866 Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen
IPR002109 Glutaredoxin
IPR004879 Protein of unknown function DUF255
IPR006662 Thioredoxin-like subdomain
IPR011767 Glutaredoxin active site
IPR011899 Glutaredoxin, eukaryotic/virial
IPR011906 Glutaredoxin-like domain
IPR017937 Thioredoxin, conserved site
IPR018219 Antioxidant Tpx conserved site
IPR018233 Calsequestrin, conserved site
IPR019479 Peroxiredoxin, C-terminal
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp
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Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2), where a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system, the NADP/thioredoxin system, and the glutathione/glutaredoxin system [1]. Several of these disulphide proteins share a common structure, consisting of a three-layer alpha/beta/alpha core. Proteins that contain domains with a thioredoxin fold include:

  • Arsenate reductase (ArsC) [2]
  • Calsequestrin (contains three tandem repeats of this fold) [3]
  • Circadian oscillation regulator KaiB [4]
  • Disulphide bond isomerase DsbC and DsbG (C-terminal domain) [5, 6]
  • Disulphide bond facilitator DsbA (contains an alpha-helical insertion) [7]
  • Endoplasmic reticulum protein ERP29 (N-terminal domain) [8]
  • Glutathione S-transferase (GST) (N-terminal domain) [9]
  • Mitochondrial ribosomal protein L51/S25/CI-B8 domain (variable positions for Cys residues in active site) [10]
  • Phosducin [11]
  • Protein disulphide isomerase (PDI) (contains two tandem repeats of this fold) [12]
  • Glutathione peroxidase-like enzymes [13]
  • Selenoprotein W-related [14]
  • SH3-binding glutamic acid-rich protein like (SH3BGR) (lacks both conserved Cys residues) [15]
  • Spliceosomal protein U5-15Kd [16]
  • Thioltransferases, including thioredoxin [17], glutaredoxon [18], hybrid peroxiredoxin hyPrx5 [19]
  • Thioredoxin-like 2Fe-2S ferredoxin [20]
Structural linksHelp
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10gs , 11gs , 12gs , 13gs , 14gs , 16gs , 17gs , 18gs , 19gs , 1a0f , 1a0r , 1a23 , 1a24 , 1a2j , 1a2l , 1a2m , 1a8l , 1a8y , 1aaz , 1aba , 1ac1 , 1acv , 1ags , 1aiu , 1aqv , 1aqw , 1aqx , 1auc , 1aw9 , 1axd , 1b48 , 1b4p , 1b4q , 1b8x , 1b9x , 1b9y , 1bay , 1bed , 1bg5 , 1bjx , 1bq7 , 1bx9 , 1bye , 1c72 , 1cqg , 1cqh , 1dby , 1de1 , 1de2 , 1dsb , 1dug , 1e2y , 1e6b , 1eej , 1eem , 1ego , 1egr , 1eog , 1eoh , 1ep7 , 1ep8 , 1ert , 1eru , 1erv , 1erw , 1ev4 , 1ev9 , 1ewx , 1ezk , 1f2e , 1f37 , 1f3a , 1f3b , 1f6m , 1f9m , 1faa , 1fb0 , 1fb6 , 1fg4 , 1fhe , 1fo5 , 1fov , 1fvj , 1fvk , 1fw1 , 1g0t , 1g6w , 1g6y , 1g7e , 1g7o , 1gh2 , 1gl8 , 1glp , 1glq , 1gnw , 1gp1 , 1grx , 1gsb , 1gsc , 1gsd , 1gse , 1gsf , 1gsq , 1gss , 1gsu , 1gsy , 1gta , 1gtb , 1gti , 1gtu , 1guh , 1guk , 1gul , 1gum , 1gwc , 1h4o , 1h75 , 1hd2 , 1hna , 1hnb , 1hnc , 1hqo , 1hyu , 1i5g , 1i9d , 1ilo , 1iyh , 1iyi , 1j08 , 1j0f , 1j9b , 1jfu , 1jhb , 1jzd , 1jzo , 1jzr , 1jzw , 1k0a , 1k0b , 1k0c , 1k0d , 1k0m , 1k0n , 1k0o , 1k3l , 1k3o , 1k3y , 1kbn , 1keb , 1kng , 1kte , 1lbk , 1ljr , 1lu4 , 1m2a , 1m2b , 1m2d , 1m7t , 1m99 , 1m9a , 1m9b , 1md3 , 1md4 , 1mdi , 1mdj , 1mdk , 1mek , 1ml6 , 1mtc , 1n2a , 1n8j , 1nho , 1nhy , 1nm3 , 1nsw , 1nw2 , 1o6j , 1o73 , 1o7u , 1o81 , 1o85 , 1o8w , 1o8x , 1oaz , 1oc3 , 1oc8 , 1oc9 , 1oe7 , 1oe8 , 1okd , 1okt , 1on4 , 1ovn , 1oyj , 1pa3 , 1pd2 , 1pgt , 1pkw , 1pkz , 1pl1 , 1pl2 , 1pmt , 1pqn , 1prx , 1psq , 1px6 , 1px7 , 1q4j , 1q98 , 1qfn , 1qgv , 1qk8 , 1qmv , 1qq2 , 1quw , 1qxh , 1r26 , 1r7h , 1rk4 , 1rqm , 1rw1 , 1sen , 1sj6 , 1sji , 1skr , 1sks , 1skw , 1sl0 , 1sl1 , 1sl2 , 1srx , 1st9 , 1su9 , 1syr , 1syx , 1t00 , 1t1v , 1t3b , 1t7p , 1t8e , 1tdi , 1tho , 1thx , 1ti1 , 1ti3 , 1tjd , 1tk0 , 1tk5 , 1tk8 , 1tkd , 1tof , 1tp9 , 1trs , 1tru , 1trv , 1trw , 1ttz , 1tu7 , 1tu8 , 1tw9 , 1txx , 1u3a , 1u3i , 1u87 , 1u88 , 1ua5 , 1uc7 , 1un2 , 1urm , 1usb , 1uul , 1uvz , 1v40 , 1v57 , 1v58 , 1v98 , 1v9w , 1vf1 , 1vf2 , 1vf3 , 1vf4 , 1vrs , 1w4v , 1w89 , 1we0 , 1wik , 1wjk , 1wou , 1wp0 , 1x0r , 1x5d , 1x9m , 1x9s , 1x9w , 1xbs , 1xcc , 1xfl , 1xiy , 1xoa , 1xob , 1xpv , 1xvq , 1xvw , 1xw5 , 1xw6 , 1xw9 , 1xwa , 1xwb , 1xwc , 1xwg , 1xwk , 1xxu , 1xzo , 1y25 , 1y6e , 1ydk , 1yep , 1yex , 1yf0 , 1yf1 , 1yj6 , 1ykc , 1yq1 , 1z3e , 1z5y , 1z9h , 1zcp , 1zgn , 1zl9 , 1zof , 1zye , 1zyn , 1zyp , 1zyq , 1zzo , 1zzy , 20gs , 22gs , 2a2r , 2a2s , 2a4v , 2aaw , 2ab6 , 2ahe , 2ajq , 2alb , 2av4 , 2b3s , 2b5e , 2b6m , 2b7j , 2b7k , 2bjx , 2bmx , 2bto , 2c0d , 2c0e , 2c0f , 2c0g , 2c1y , 2c3n , 2c3q , 2c3t , 2c4j , 2c80 , 2c8u , 2ca8 , 2cai , 2caq , 2cv4 , 2cvb , 2cvd , 2cx3 , 2cx4 , 2cz2 , 2cz3 , 2d2z , 2dc5 , 2diz , 2djj , 2djk , 2dml , 2dsa , 2e0q , 2e2g , 2eio , 2eiq , 2eir , 2f3m , 2f51 , 2f8a , 2f8f , 2f9s , 2fch , 2fd3 , 2fhe , 2fno , 2fug , 2fwe , 2fwf , 2fwg , 2fwh , 2fy6 , 2gdr , 2ggt , 2glr , 2gqk , 2gql , 2gqm , 2gsq , 2gsr , 2gss , 2gst , 2gt5 , 2gt6 , 2gtu , 2gvp , 2h01 , 2h0g , 2h0h , 2h0i , 2h19 , 2h1a , 2h1b , 2h1d , 2h1g , 2h66 , 2h6x , 2h6y , 2h6z , 2h70 , 2h71 , 2h72 , 2h73 , 2h74 , 2h75 , 2h76 , 2he3 , 2hi7 , 2hnl , 2hrf , 2hrn , 2hsh , 2hxk , 2hyx , 2hze , 2hzf , 2i1u , 2i3y , 2ifq , 2iiy , 2ijy , 2iyj , 2j9h , 2jzr , 2jzs , 2ljr , 2nto , 2nvl , 2o8v , 2oa7 , 2oac , 2oad , 2oe0 , 2oe1 , 2oe3 , 2pbj , 2pgt , 2pmt , 2pn8 , 2pu9 , 2puk , 2pvo , 2pvq , 2r3x , 2r6k , 2rii , 2tir , 2trc , 2trx , 2v2g , 2v32 , 2v41 , 2vcq , 2vcw , 2vcx , 2vcz , 2vd0 , 2vd1 , 2vl2 , 2vl3 , 2ywo , 2yzh , 2zct , 3csh , 3csi , 3csj , 3ee2 , 3fyg , 3grx , 3gss , 3gst , 3gtu , 3ljr , 3pgt , 3trx , 4gss , 4gst , 4gtu , 4pgt , 4trx , 5fwg , 5gss , 5gst , 6gss , 6gst , 6gsu , 6gsv , 6gsw , 6gsx , 6gsy , 7gss , 8gss , 9gss

Taxonomic coverageHelp
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Overlapping InterPro entriesHelp
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IPR012335 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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O00299 Chloride intracellular channel protein 1

O44342 Protein windbeutel

P08003 Protein disulfide-isomerase A4

P17695 Glutaredoxin-2, mitochondrial

Q09596 Probable glutathione S-transferase 5

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR012883 ERp29, N-terminal
IPR010987 Glutathione S-transferase, C-terminal-like
IPR002946 Intracellular chloride channel
IPR004046 Glutathione S-transferase, C-terminal
IPR011679 Endoplasmic reticulum, protein ERp29, C-terminal
IPR012336 Thioredoxin-like fold
IPR004045 Glutathione S-transferase, N-terminal
IPR011767 Glutaredoxin active site
IPR013766 Thioredoxin domain
IPR005788 Disulphide isomerase
IPR012335 Thioredoxin fold
IPR016855 Endoplasmic reticulum, protein ERp29
IPR006662 Thioredoxin-like subdomain
IPR011899 Glutaredoxin, eukaryotic/virial
IPR014025 Glutaredoxin subgroup
IPR002109 Glutaredoxin
IPR005792 Protein disulphide isomerase
IPR017068 Protein disulphide-isomerase A4
IPR017933 Glutathione S-transferase/chloride channel, C-terminal
IPR017936 Thioredoxin-like
IPR017937 Thioredoxin, conserved site
ModBase
SWISS-MODEL
PDB Chain
CATH Domain
SCOP Domain

PublicationsHelp
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1. Buchanan BB, Balmer Y.
Redox regulation: a broadening horizon.
56 187-220 2005 [PubMed: 15862094]
http://dx.doi.org/10.1146/annurev.arplant.56.032604.144246
2. Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF.
Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme.
Structure 9 1071-81 2001 [PubMed: 11709171]
http://dx.doi.org/10.1016/S0969-2126(01)00672-4
3. Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH.
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum.
Nat. Struct. Biol. 5 476-83 1998 [PubMed: 9628486]
http://dx.doi.org/10.1038/nsb0698-476
4. Garces RG, Wu N, Gillon W, Pai EF.
Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC.
EMBO J. 23 1688-98 2004 [PubMed: 15071498]
http://dx.doi.org/10.1038/sj.emboj.7600190
5. McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P.
Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
Nat. Struct. Biol. 7 196-9 2000 [PubMed: 10700276]
http://dx.doi.org/10.1038/73295
6. Heras B, Edeling MA, Schirra HJ, Raina S, Martin JL.
Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.
Proc. Natl. Acad. Sci. U.S.A. 101 8876-81 2004 [PubMed: 15184683]
http://dx.doi.org/10.1073/pnas.0402769101
7. Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, Martin JL.
Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.
Protein Sci. 6 1893-900 1997 [PubMed: 9300489]
http://www.proteinscience.org/cgi/content/abstract/6/9/1893
8. Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, Mkrtchian S.
Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.
Structure 9 457-71 2001 [PubMed: 11435111]
http://dx.doi.org/10.1016/S0969-2126(01)00607-4
9. Tellez-Sanz R, Cesareo E, Nuccetelli M, Aguilera AM, Baron C, Parker LJ, Adams JJ, Morton CJ, Lo Bello M, Parker MW, Garcia-Fuentes L.
Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase P1-1.
Protein Sci. 15 1093-105 2006 [PubMed: 16597834]
http://dx.doi.org/10.1110/ps.052055206
10. Brockmann C, Diehl A, Rehbein K, Strauss H, Schmieder P, Korn B, Kuhne R, Oschkinat H.
The oxidized subunit B8 from human complex I adopts a thioredoxin fold.
Structure 12 1645-54 2004 [PubMed: 15341729]
http://dx.doi.org/10.1016/j.str.2004.06.021
11. Gaudet R, Bohm A, Sigler PB.
Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin.
Cell 87 577-88 1996 [PubMed: 8898209]
http://dx.doi.org/10.1016/S0092-8674(00)81376-8
12. Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, Darby NJ.
The structure in solution of the b domain of protein disulfide isomerase.
J. Biomol. NMR 13 357-68 1999 [PubMed: 10383197]
http://dx.doi.org/10.1023/A:1008341820489
13. Epp O, Ladenstein R, Wendel A.
The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.
Eur. J. Biochem. 133 51-69 1983 [PubMed: 6852035]
http://dx.doi.org/10.1111/j.1432-1033.1983.tb07429.x
14. Ferguson AD, Labunskyy VM, Fomenko DE, Arac D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J.
NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.
J. Biol. Chem. 281 3536-43 2006 [PubMed: 16319061]
http://dx.doi.org/10.1074/jbc.M511386200
15. Nardini M, Mazzocco M, Massaro A, Maffei M, Vergano A, Donadini A, Scartezzini P, Bolognesi M.
Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution.
Biochem. Biophys. Res. Commun. 318 470-6 2004 [PubMed: 15120624]
http://dx.doi.org/10.1016/j.bbrc.2004.04.050
16. Reuter K, Nottrott S, Fabrizio P, Luhrmann R, Ficner R.
Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein.
J. Mol. Biol. 294 515-25 1999 [PubMed: 10610776]
http://dx.doi.org/10.1006/jmbi.1999.3258
17. Katti SK, LeMaster DM, Eklund H.
Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution.
J. Mol. Biol. 212 167-84 1990 [PubMed: 2181145]
http://dx.doi.org/10.1016/0022-2836(90)90313-B
18. Xia TH, Bushweller JH, Sodano P, Billeter M, Bjornberg O, Holmgren A, Wuthrich K.
NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Protein Sci. 1 310-21 1992 [PubMed: 1304339]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1304339
19. Kim SJ, Woo JR, Hwang YS, Jeong DG, Shin DH, Kim K, Ryu SE.
The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteins.
J. Biol. Chem. 278 10790-8 2003 [PubMed: 12529327]
http://dx.doi.org/10.1074/jbc.M209553200
20. Yeh AP, Ambroggio XI, Andrade SL, Einsle O, Chatelet C, Meyer J, Rees DC.
High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus.
J. Biol. Chem. 277 34499-507 2002 [PubMed: 12089152]
http://dx.doi.org/10.1074/jbc.M205096200

Additional ReadingHelp
Open in usermanual
Nakamura T, Yamamoto T, Abe M, Matsumura H, Hagihara Y, Goto T, Yamaguchi T, Inoue T.
Oxidation of archaeal peroxiredoxin involves a hypervalent sulfur intermediate.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 6238-42 [PubMed: 18436649]
http://dx.doi.org/10.1073/pnas.0709822105
Bao R, Zhang Y, Zhou CZ, Chen Y.
Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues.
Biochim. Biophys. Acta 1794 2009 716-21 [PubMed: 19166985]
Smeets A, Loumaye E, Clippe A, Rees JF, Knoops B, Declercq JP.
The crystal structure of the C45S mutant of annelid Arenicola marina peroxiredoxin 6 supports its assignment to the mechanistically typical 2-Cys subfamily without any formation of toroid-shaped decamers.
Protein Sci. 17 2008 700-10 [PubMed: 18359859]
http://dx.doi.org/10.1110/ps.073399308
Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C.
Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site.
Proteins 71 2008 16-23 [PubMed: 18076047]
http://dx.doi.org/10.1002/prot.21835
Perbandt M, Hoppner J, Burmeister C, Luersen K, Betzel C, Liebau E.
Structure of the extracellular glutathione S-transferase OvGST1 from the human pathogenic parasite Onchocerca volvulus.
J. Mol. Biol. 377 2008 501-11 [PubMed: 18258257]
http://dx.doi.org/10.1016/j.jmb.2008.01.029
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