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InterPro: IPR012336 Thioredoxin-like fold

Protein matches Help

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Matches:

60528 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Architectures
Accession List
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Accession

IPR012336 Thioredoxin-like_fold

Type

Domain

Signatures Help

Database	ID	Name	Proteins
SuperFamily	SSF52833	Thiordxn-like_fd	60528
Signatures in BioMart

InterPro Relationships Help

Children

IPR011649 KaiB
IPR012335 Thioredoxin fold
IPR012941 Phenol hydroxylase, C-terminal dimerisation

Found in

IPR010296 Protein of unknown function DUF899, thioredoxin-like
IPR010350 Protein of unknown function DUF942, thioredoxin-like
IPR012863 Protein of unknown function DUF1636
IPR012883 ERp29, N-terminal
IPR014109 Type-F conjugative transfer system pilin assembly thiol-disulphide isomerase TrbB
IPR014111 Type IV conjugative transfer system protein TraF
IPR014440 HCCA isomerase/glutathione S-transferase kappa
IPR016639 Glutathione S-transferase, predicted
IPR017167 Uncharacterised conserved protein UCP037291, glutaredoxin-related
IPR017346 Uncharacterised conserved protein UCP037991, UAS, UBX

Contains

IPR002109 Glutaredoxin
IPR006662 Thioredoxin-like subdomain
IPR008261 Iodothyronine deiodinase, active site
IPR011767 Glutaredoxin active site
IPR017937 Thioredoxin, conserved site
IPR018219 Antioxidant Tpx conserved site
IPR018233 Calsequestrin, conserved site
IPR019479 Peroxiredoxin, C-terminal

InterPro annotation

Entry Details in BioMart

Abstract

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 links Help

PDB - click here

SCOP: a.45.1.1 , c.47.1.1 , c.47.1.10 , c.47.1.11 , c.47.1.12 , c.47.1.13 , c.47.1.14 , c.47.1.15 , c.47.1.16 , c.47.1.2 , c.47.1.20 , c.47.1.21 , c.47.1.3 , c.47.1.5 , c.47.1.6 , c.47.1.7 , c.47.1.8 , c.47.1.9

CATH: 1.10.168.10 , 1.10.472.60 , 1.20.1050.10 , 3.30.1020.10 , 3.40.30.10 , 3.40.30.20

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012336

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

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

Publications Open in usermanual
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 Reading 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]
	Parish D, Benach J, Liu G, Singarapu KK, Xiao R, Acton T, Su M, Bansal S, Prestegard JH, Hunt J, Montelione GT, Szyperski T. Protein chaperones Q8ZP25_SALTY from Salmonella typhimurium and HYAE_ECOLI from Escherichia coli exhibit thioredoxin-like structures despite lack of canonical thioredoxin active site sequence motif. J. Struct. Funct. Genomics 9 2008 41-9 [PubMed: 19039680] http://dx.doi.org/10.1007/s10969-008-9050-y
	Hegazy UM, Tars K, Hellman U, Mannervik B. Modulating catalytic activity by unnatural amino acid residues in a GSH-binding loop of GST P1-1. J. Mol. Biol. 376 2008 811-26 [PubMed: 18177897] http://dx.doi.org/10.1016/j.jmb.2007.12.013
	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

InterPro 23.1